<?xml version="1.0" encoding="UTF-8"?>
<uniprot xmlns="http://uniprot.org/uniprot"
 xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance"
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<entry dataset="TrEMBL" created="2021-02-10" modified="2022-08-03" version="7" xmlns="http://uniprot.org/uniprot">
    <accession>A0A7H2C765</accession>
    <name>A0A7H2C765_ECOLI</name>
    <protein>
        <recommendedName>
            <fullName evidence="5 13">Penicillin-binding protein 1B</fullName>
            <shortName evidence="13">PBP-1b</shortName>
            <shortName evidence="13">PBP1b</shortName>
        </recommendedName>
        <alternativeName>
            <fullName evidence="12 13">Murein polymerase</fullName>
        </alternativeName>
    </protein>
    <gene>
        <name evidence="20" type="primary">mrcB</name>
        <name evidence="20" type="synonym">ECK0148</name>
        <name evidence="20" type="synonym">pbpF</name>
        <name evidence="20" type="synonym">ponB</name>
        <name evidence="20" type="ORF">b0149</name>
    </gene>
    <organism evidence="20 21">
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference evidence="20 21" key="1">
        <citation type="journal article" date="1997" name="Science" volume="277" first="1453" last="1462">
            <title>The complete genome sequence of Escherichia coli K-12.</title>
            <authorList>
                <person name="Blattner F.R."/>
                <person name="Plunkett G.III."/>
                <person name="Bloch C.A."/>
                <person name="Perna N.T."/>
                <person name="Burland V."/>
                <person name="Riley M."/>
                <person name="Collado-Vides J."/>
                <person name="Glasner J.D."/>
                <person name="Rode C.K."/>
                <person name="Mayhew G.F."/>
                <person name="Gregor J."/>
                <person name="Davis N.W."/>
                <person name="Kirkpatrick H.A."/>
                <person name="Goeden M.A."/>
                <person name="Rose D.J."/>
                <person name="Mau B."/>
                <person name="Shao Y."/>
            </authorList>
            <dbReference type="PubMed" id="9278503"/>
            <dbReference type="DOI" id="10.1126/science.277.5331.1453"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain evidence="21">K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <comment type="function">
        <text evidence="1 13">Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).</text>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="11">
            <text>[GlcNAc-(1-&gt;4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1-&gt;4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1-&gt;4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)</text>
            <dbReference type="Rhea" id="RHEA:23708"/>
            <dbReference type="Rhea" id="RHEA-COMP:9602"/>
            <dbReference type="Rhea" id="RHEA-COMP:9603"/>
            <dbReference type="ChEBI" id="CHEBI:15378"/>
            <dbReference type="ChEBI" id="CHEBI:58405"/>
            <dbReference type="ChEBI" id="CHEBI:60033"/>
            <dbReference type="ChEBI" id="CHEBI:78435"/>
            <dbReference type="EC" id="2.4.1.129"/>
        </reaction>
    </comment>
    <comment type="pathway">
        <text evidence="2 13">Cell wall biogenesis; peptidoglycan biosynthesis.</text>
    </comment>
    <comment type="similarity">
        <text evidence="3 13">In the C-terminal section; belongs to the transpeptidase family.</text>
    </comment>
    <comment type="similarity">
        <text evidence="4 13">In the N-terminal section; belongs to the glycosyltransferase 51 family.</text>
    </comment>
    <dbReference type="EMBL" id="U00096">
        <property type="protein sequence ID" value="QNV50512.1"/>
        <property type="molecule type" value="Genomic_DNA"/>
    </dbReference>
    <dbReference type="SMR" id="A0A7H2C765"/>
    <dbReference type="UniPathway" id="UPA00219"/>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <dbReference type="GO" id="GO:0016021">
        <property type="term" value="C:integral component of membrane"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0009274">
        <property type="term" value="C:peptidoglycan-based cell wall"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-UniRule"/>
    </dbReference>
    <dbReference type="GO" id="GO:0008658">
        <property type="term" value="F:penicillin binding"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="GO" id="GO:0008955">
        <property type="term" value="F:peptidoglycan glycosyltransferase activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-UniRule"/>
    </dbReference>
    <dbReference type="GO" id="GO:0009002">
        <property type="term" value="F:serine-type D-Ala-D-Ala carboxypeptidase activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-EC"/>
    </dbReference>
    <dbReference type="GO" id="GO:0071555">
        <property type="term" value="P:cell wall organization"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-UniRule"/>
    </dbReference>
    <dbReference type="GO" id="GO:0009252">
        <property type="term" value="P:peptidoglycan biosynthetic process"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-UniRule"/>
    </dbReference>
    <dbReference type="GO" id="GO:0006508">
        <property type="term" value="P:proteolysis"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0008360">
        <property type="term" value="P:regulation of cell shape"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-UniRule"/>
    </dbReference>
    <dbReference type="GO" id="GO:0046677">
        <property type="term" value="P:response to antibiotic"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="Gene3D" id="1.10.3810.10">
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Gene3D" id="3.40.710.10">
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR012338">
        <property type="entry name" value="Beta-lactam/transpept-like"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR001264">
        <property type="entry name" value="Glyco_trans_51"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR023346">
        <property type="entry name" value="Lysozyme-like_dom_sf"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR011813">
        <property type="entry name" value="PBP_1b"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR036950">
        <property type="entry name" value="PBP_transglycosylase"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR001460">
        <property type="entry name" value="PCN-bd_Tpept"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR028166">
        <property type="entry name" value="UB2H"/>
    </dbReference>
    <dbReference type="Pfam" id="PF00912">
        <property type="entry name" value="Transgly"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Pfam" id="PF00905">
        <property type="entry name" value="Transpeptidase"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Pfam" id="PF14814">
        <property type="entry name" value="UB2H"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PIRSF" id="PIRSF002799">
        <property type="entry name" value="PBP_1b"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="SUPFAM" id="SSF53955">
        <property type="entry name" value="SSF53955"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="SUPFAM" id="SSF56601">
        <property type="entry name" value="SSF56601"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="TIGRFAMs" id="TIGR02071">
        <property type="entry name" value="PBP_1b"/>
        <property type="match status" value="1"/>
    </dbReference>
    <proteinExistence type="inferred from homology"/>
    <keyword evidence="6" id="KW-0121">Carboxypeptidase</keyword>
    <keyword evidence="13" id="KW-0133">Cell shape</keyword>
    <keyword evidence="13" id="KW-0961">Cell wall biogenesis/degradation</keyword>
    <keyword evidence="8 13" id="KW-0328">Glycosyltransferase</keyword>
    <keyword evidence="9" id="KW-0378">Hydrolase</keyword>
    <keyword evidence="16" id="KW-0472">Membrane</keyword>
    <keyword evidence="10" id="KW-0511">Multifunctional enzyme</keyword>
    <keyword evidence="13" id="KW-0573">Peptidoglycan synthesis</keyword>
    <keyword evidence="7" id="KW-0645">Protease</keyword>
    <keyword evidence="21" id="KW-1185">Reference proteome</keyword>
    <keyword evidence="13" id="KW-0808">Transferase</keyword>
    <keyword evidence="16" id="KW-0812">Transmembrane</keyword>
    <keyword evidence="16" id="KW-1133">Transmembrane helix</keyword>
    <feature type="transmembrane region" description="Helical" evidence="16">
        <location>
            <begin position="20"/>
            <end position="41"/>
        </location>
    </feature>
    <feature type="domain" description="UB2H" evidence="19">
        <location>
            <begin position="68"/>
            <end position="152"/>
        </location>
    </feature>
    <feature type="domain" description="Transgly" evidence="18">
        <location>
            <begin position="164"/>
            <end position="335"/>
        </location>
    </feature>
    <feature type="domain" description="Transpeptidase" evidence="17">
        <location>
            <begin position="428"/>
            <end position="669"/>
        </location>
    </feature>
    <feature type="region of interest" description="Disordered" evidence="15">
        <location>
            <begin position="748"/>
            <end position="790"/>
        </location>
    </feature>
    <feature type="compositionally biased region" description="Polar residues" evidence="15">
        <location>
            <begin position="748"/>
            <end position="783"/>
        </location>
    </feature>
    <feature type="active site" description="Proton donor; for transglycosylase activity" evidence="14">
        <location>
            <position position="188"/>
        </location>
    </feature>
    <feature type="active site" description="Acyl-ester intermediate; for transpeptidase activity" evidence="14">
        <location>
            <position position="465"/>
        </location>
    </feature>
    <evidence type="ECO:0000256" key="1">
        <source>
            <dbReference type="ARBA" id="ARBA00002624"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="2">
        <source>
            <dbReference type="ARBA" id="ARBA00004752"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="3">
        <source>
            <dbReference type="ARBA" id="ARBA00007090"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="4">
        <source>
            <dbReference type="ARBA" id="ARBA00007739"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="5">
        <source>
            <dbReference type="ARBA" id="ARBA00018637"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="6">
        <source>
            <dbReference type="ARBA" id="ARBA00022645"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="7">
        <source>
            <dbReference type="ARBA" id="ARBA00022670"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="8">
        <source>
            <dbReference type="ARBA" id="ARBA00022676"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="9">
        <source>
            <dbReference type="ARBA" id="ARBA00022801"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="10">
        <source>
            <dbReference type="ARBA" id="ARBA00023268"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="11">
        <source>
            <dbReference type="ARBA" id="ARBA00023988"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="12">
        <source>
            <dbReference type="ARBA" id="ARBA00032454"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="13">
        <source>
            <dbReference type="PIRNR" id="PIRNR002799"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="14">
        <source>
            <dbReference type="PIRSR" id="PIRSR002799-1"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="15">
        <source>
            <dbReference type="SAM" id="MobiDB-lite"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="16">
        <source>
            <dbReference type="SAM" id="Phobius"/>
        </source>
    </evidence>
    <evidence type="ECO:0000259" key="17">
        <source>
            <dbReference type="Pfam" id="PF00905"/>
        </source>
    </evidence>
    <evidence type="ECO:0000259" key="18">
        <source>
            <dbReference type="Pfam" id="PF00912"/>
        </source>
    </evidence>
    <evidence type="ECO:0000259" key="19">
        <source>
            <dbReference type="Pfam" id="PF14814"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="20">
        <source>
            <dbReference type="EMBL" id="QNV50512.1"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="21">
        <source>
            <dbReference type="Proteomes" id="UP000000625"/>
        </source>
    </evidence>
    <sequence length="799" mass="88890" checksum="2A4869BED79A2530" modified="2021-02-10" version="1"> </sequence>
</entry>
<entry dataset="TrEMBL" created="2021-02-10" modified="2022-08-03" version="5" xmlns="http://uniprot.org/uniprot">
    <accession>A0A7H2C766</accession>
    <name>A0A7H2C766_ECOLI</name>
    <protein>
        <recommendedName>
            <fullName evidence="3">NAD-dependent protein deacylase</fullName>
            <ecNumber evidence="3">2.3.1.286</ecNumber>
        </recommendedName>
        <alternativeName>
            <fullName evidence="3">Regulatory protein SIR2 homolog</fullName>
        </alternativeName>
    </protein>
    <gene>
        <name evidence="3 5" type="primary">cobB</name>
        <name evidence="5" type="synonym">ECK1106</name>
        <name evidence="5" type="synonym">ycfY</name>
        <name evidence="5" type="ORF">b1120</name>
    </gene>
    <organism evidence="5 6">
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference evidence="5 6" key="1">
        <citation type="journal article" date="1997" name="Science" volume="277" first="1453" last="1462">
            <title>The complete genome sequence of Escherichia coli K-12.</title>
            <authorList>
                <person name="Blattner F.R."/>
                <person name="Plunkett G.III."/>
                <person name="Bloch C.A."/>
                <person name="Perna N.T."/>
                <person name="Burland V."/>
                <person name="Riley M."/>
                <person name="Collado-Vides J."/>
                <person name="Glasner J.D."/>
                <person name="Rode C.K."/>
                <person name="Mayhew G.F."/>
                <person name="Gregor J."/>
                <person name="Davis N.W."/>
                <person name="Kirkpatrick H.A."/>
                <person name="Goeden M.A."/>
                <person name="Rose D.J."/>
                <person name="Mau B."/>
                <person name="Shao Y."/>
            </authorList>
            <dbReference type="PubMed" id="9278503"/>
            <dbReference type="DOI" id="10.1126/science.277.5331.1453"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain evidence="6">K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <comment type="function">
        <text evidence="3">NAD-dependent lysine deacetylase that specifically removes acetyl groups on target proteins. Also acts as a protein-lysine deacylase by mediating protein desuccinylation and de-2-hydroxyisobutyrylation. Modulates the activities of several proteins which are inactive in their acylated form.</text>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="3">
            <text>H2O + N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein] + NAD(+) = 2''-O-(2-hydroxyisobutanoyl)-ADP-D-ribose + L-lysyl-[protein] + nicotinamide</text>
            <dbReference type="Rhea" id="RHEA:24364"/>
            <dbReference type="Rhea" id="RHEA-COMP:9752"/>
            <dbReference type="Rhea" id="RHEA-COMP:15921"/>
            <dbReference type="ChEBI" id="CHEBI:15377"/>
            <dbReference type="ChEBI" id="CHEBI:17154"/>
            <dbReference type="ChEBI" id="CHEBI:29969"/>
            <dbReference type="ChEBI" id="CHEBI:57540"/>
            <dbReference type="ChEBI" id="CHEBI:144968"/>
            <dbReference type="ChEBI" id="CHEBI:144969"/>
        </reaction>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="3">
            <text>H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide</text>
            <dbReference type="Rhea" id="RHEA:43636"/>
            <dbReference type="Rhea" id="RHEA-COMP:9752"/>
            <dbReference type="Rhea" id="RHEA-COMP:10731"/>
            <dbReference type="ChEBI" id="CHEBI:15377"/>
            <dbReference type="ChEBI" id="CHEBI:17154"/>
            <dbReference type="ChEBI" id="CHEBI:29969"/>
            <dbReference type="ChEBI" id="CHEBI:57540"/>
            <dbReference type="ChEBI" id="CHEBI:61930"/>
            <dbReference type="ChEBI" id="CHEBI:83767"/>
            <dbReference type="EC" id="2.3.1.286"/>
        </reaction>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="3">
            <text>H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide</text>
            <dbReference type="Rhea" id="RHEA:47668"/>
            <dbReference type="Rhea" id="RHEA-COMP:9752"/>
            <dbReference type="Rhea" id="RHEA-COMP:11877"/>
            <dbReference type="ChEBI" id="CHEBI:15377"/>
            <dbReference type="ChEBI" id="CHEBI:17154"/>
            <dbReference type="ChEBI" id="CHEBI:29969"/>
            <dbReference type="ChEBI" id="CHEBI:57540"/>
            <dbReference type="ChEBI" id="CHEBI:87830"/>
            <dbReference type="ChEBI" id="CHEBI:87832"/>
        </reaction>
    </comment>
    <comment type="cofactor">
        <cofactor evidence="3">
            <name>Zn(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:29105"/>
        </cofactor>
        <text evidence="3">Binds 1 zinc ion per subunit.</text>
    </comment>
    <comment type="subcellular location">
        <subcellularLocation>
            <location evidence="3">Cytoplasm</location>
        </subcellularLocation>
    </comment>
    <comment type="domain">
        <text evidence="3">2 residues (Tyr-55 and Arg-58) present in a large hydrophobic pocket are probably involved in substrate specificity. They are important for desuccinylation activity, but dispensable for deacetylation activity.</text>
    </comment>
    <comment type="similarity">
        <text evidence="3">Belongs to the sirtuin family. Class III subfamily.</text>
    </comment>
    <comment type="caution">
        <text evidence="3">Lacks conserved residue(s) required for the propagation of feature annotation.</text>
    </comment>
    <dbReference type="EC" id="2.3.1.286" evidence="3"/>
    <dbReference type="EMBL" id="U00096">
        <property type="protein sequence ID" value="QNV50513.1"/>
        <property type="molecule type" value="Genomic_DNA"/>
    </dbReference>
    <dbReference type="SMR" id="A0A7H2C766"/>
    <dbReference type="OMA" id="SMQVYPA"/>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <dbReference type="GO" id="GO:0005737">
        <property type="term" value="C:cytoplasm"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-SubCell"/>
    </dbReference>
    <dbReference type="GO" id="GO:0070403">
        <property type="term" value="F:NAD+ binding"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-UniRule"/>
    </dbReference>
    <dbReference type="GO" id="GO:0034979">
        <property type="term" value="F:NAD-dependent protein deacetylase activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-UniRule"/>
    </dbReference>
    <dbReference type="GO" id="GO:0036054">
        <property type="term" value="F:protein-malonyllysine demalonylase activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="GO" id="GO:0036055">
        <property type="term" value="F:protein-succinyllysine desuccinylase activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-UniRule"/>
    </dbReference>
    <dbReference type="GO" id="GO:0016740">
        <property type="term" value="F:transferase activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0008270">
        <property type="term" value="F:zinc ion binding"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-UniRule"/>
    </dbReference>
    <dbReference type="GO" id="GO:0006476">
        <property type="term" value="P:protein deacetylation"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-UniRule"/>
    </dbReference>
    <dbReference type="CDD" id="cd01412">
        <property type="entry name" value="SIRT5_Af1_CobB"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Gene3D" id="3.30.1600.10">
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="HAMAP" id="MF_01121">
        <property type="entry name" value="Sirtuin_ClassIII"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR029035">
        <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR003000">
        <property type="entry name" value="Sirtuin"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR026591">
        <property type="entry name" value="Sirtuin_cat_small_dom_sf"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR027546">
        <property type="entry name" value="Sirtuin_class_III"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR026590">
        <property type="entry name" value="Ssirtuin_cat_dom"/>
    </dbReference>
    <dbReference type="Pfam" id="PF02146">
        <property type="entry name" value="SIR2"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="SUPFAM" id="SSF52467">
        <property type="entry name" value="SSF52467"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PROSITE" id="PS50305">
        <property type="entry name" value="SIRTUIN"/>
        <property type="match status" value="1"/>
    </dbReference>
    <proteinExistence type="inferred from homology"/>
    <keyword evidence="3" id="KW-0963">Cytoplasm</keyword>
    <keyword evidence="3" id="KW-0479">Metal-binding</keyword>
    <keyword evidence="2 3" id="KW-0520">NAD</keyword>
    <keyword evidence="6" id="KW-1185">Reference proteome</keyword>
    <keyword evidence="1" id="KW-0808">Transferase</keyword>
    <keyword evidence="3" id="KW-0862">Zinc</keyword>
    <feature type="domain" description="Deacetylase sirtuin-type" evidence="4">
        <location>
            <begin position="1"/>
            <end position="237"/>
        </location>
    </feature>
    <feature type="active site" description="Proton acceptor" evidence="3">
        <location>
            <position position="110"/>
        </location>
    </feature>
    <feature type="binding site" evidence="3">
        <location>
            <begin position="11"/>
            <end position="30"/>
        </location>
        <ligand>
            <name>NAD(+)</name>
            <dbReference type="ChEBI" id="CHEBI:57540"/>
        </ligand>
    </feature>
    <feature type="binding site" evidence="3">
        <location>
            <position position="55"/>
        </location>
        <ligand>
            <name>substrate</name>
        </ligand>
    </feature>
    <feature type="binding site" evidence="3">
        <location>
            <position position="58"/>
        </location>
        <ligand>
            <name>substrate</name>
        </ligand>
    </feature>
    <feature type="binding site" evidence="3">
        <location>
            <begin position="92"/>
            <end position="95"/>
        </location>
        <ligand>
            <name>NAD(+)</name>
            <dbReference type="ChEBI" id="CHEBI:57540"/>
        </ligand>
    </feature>
    <feature type="binding site" evidence="3">
        <location>
            <position position="118"/>
        </location>
        <ligand>
            <name>Zn(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:29105"/>
        </ligand>
    </feature>
    <feature type="binding site" evidence="3">
        <location>
            <position position="137"/>
        </location>
        <ligand>
            <name>Zn(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:29105"/>
        </ligand>
    </feature>
    <feature type="binding site" evidence="3">
        <location>
            <begin position="177"/>
            <end position="179"/>
        </location>
        <ligand>
            <name>NAD(+)</name>
            <dbReference type="ChEBI" id="CHEBI:57540"/>
        </ligand>
    </feature>
    <feature type="binding site" evidence="3">
        <location>
            <begin position="203"/>
            <end position="205"/>
        </location>
        <ligand>
            <name>NAD(+)</name>
            <dbReference type="ChEBI" id="CHEBI:57540"/>
        </ligand>
    </feature>
    <feature type="binding site" evidence="3">
        <location>
            <position position="221"/>
        </location>
        <ligand>
            <name>NAD(+)</name>
            <dbReference type="ChEBI" id="CHEBI:57540"/>
        </ligand>
    </feature>
    <evidence type="ECO:0000256" key="1">
        <source>
            <dbReference type="ARBA" id="ARBA00022679"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="2">
        <source>
            <dbReference type="ARBA" id="ARBA00023027"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="3">
        <source>
            <dbReference type="HAMAP-Rule" id="MF_01121"/>
        </source>
    </evidence>
    <evidence type="ECO:0000259" key="4">
        <source>
            <dbReference type="PROSITE" id="PS50305"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="5">
        <source>
            <dbReference type="EMBL" id="QNV50513.1"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="6">
        <source>
            <dbReference type="Proteomes" id="UP000000625"/>
        </source>
    </evidence>
    <sequence length="242" mass="26716" checksum="D4EEEBF856898698" modified="2021-02-10" version="1">MEKPRVLVLTGAGISAESGIRTFRAADGLWEEHRVEDVATPEGFDRDPELVQAFYNARRRQLQQPEIQPNAAHLALAKLQDALGDRFLLVTQNIDNLHERAGNTNVIHMHGELLKVRCSQSGQVLDWTGDVTPEDKCHCCQFPAPLRPHVVWFGEMPLGMDEIYMALSMADIFIAIGTSGHVYPAAGFVHEAKLHGAHTVELNLEPSQVGNEFAEKYYGPASQVVPEFVEKLLKGLKAGSIA</sequence>
</entry>
<entry dataset="TrEMBL" created="2021-02-10" modified="2022-08-03" version="6" xmlns="http://uniprot.org/uniprot">
    <accession>A0A7H2C767</accession>
    <name>A0A7H2C767_ECOLI</name>
    <protein>
        <recommendedName>
            <fullName evidence="2">Chaperone protein ClpB</fullName>
        </recommendedName>
    </protein>
    <gene>
        <name evidence="12" type="primary">clpB</name>
        <name evidence="12" type="synonym">ECK2590</name>
        <name evidence="12" type="synonym">htpM</name>
        <name evidence="12" type="ORF">b2592</name>
    </gene>
    <organism evidence="12 13">
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference evidence="12 13" key="1">
        <citation type="journal article" date="1997" name="Science" volume="277" first="1453" last="1462">
            <title>The complete genome sequence of Escherichia coli K-12.</title>
            <authorList>
                <person name="Blattner F.R."/>
                <person name="Plunkett G.III."/>
                <person name="Bloch C.A."/>
                <person name="Perna N.T."/>
                <person name="Burland V."/>
                <person name="Riley M."/>
                <person name="Collado-Vides J."/>
                <person name="Glasner J.D."/>
                <person name="Rode C.K."/>
                <person name="Mayhew G.F."/>
                <person name="Gregor J."/>
                <person name="Davis N.W."/>
                <person name="Kirkpatrick H.A."/>
                <person name="Goeden M.A."/>
                <person name="Rose D.J."/>
                <person name="Mau B."/>
                <person name="Shao Y."/>
            </authorList>
            <dbReference type="PubMed" id="9278503"/>
            <dbReference type="DOI" id="10.1126/science.277.5331.1453"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain evidence="13">K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <comment type="subunit">
        <text evidence="7">Homohexamer. The oligomerization is ATP-dependent.</text>
    </comment>
    <comment type="similarity">
        <text evidence="1 8">Belongs to the ClpA/ClpB family.</text>
    </comment>
    <dbReference type="EMBL" id="U00096">
        <property type="protein sequence ID" value="QNV50514.1"/>
        <property type="molecule type" value="Genomic_DNA"/>
    </dbReference>
    <dbReference type="SMR" id="A0A7H2C767"/>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <dbReference type="GO" id="GO:0005737">
        <property type="term" value="C:cytoplasm"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="GO" id="GO:0005524">
        <property type="term" value="F:ATP binding"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0016887">
        <property type="term" value="F:ATP hydrolysis activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="GO" id="GO:0042026">
        <property type="term" value="P:protein refolding"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="GO" id="GO:0009408">
        <property type="term" value="P:response to heat"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="Gene3D" id="3.40.50.300">
        <property type="match status" value="3"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR003593">
        <property type="entry name" value="AAA+_ATPase"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR003959">
        <property type="entry name" value="ATPase_AAA_core"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR017730">
        <property type="entry name" value="Chaperonin_ClpB"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR019489">
        <property type="entry name" value="Clp_ATPase_C"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR001270">
        <property type="entry name" value="ClpA/B"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR018368">
        <property type="entry name" value="ClpA/B_CS1"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR028299">
        <property type="entry name" value="ClpA/B_CS2"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR041546">
        <property type="entry name" value="ClpA/ClpB_AAA_lid"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR027417">
        <property type="entry name" value="P-loop_NTPase"/>
    </dbReference>
    <dbReference type="Pfam" id="PF00004">
        <property type="entry name" value="AAA"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Pfam" id="PF07724">
        <property type="entry name" value="AAA_2"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Pfam" id="PF17871">
        <property type="entry name" value="AAA_lid_9"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Pfam" id="PF10431">
        <property type="entry name" value="ClpB_D2-small"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PRINTS" id="PR00300">
        <property type="entry name" value="CLPPROTEASEA"/>
    </dbReference>
    <dbReference type="SMART" id="SM00382">
        <property type="entry name" value="AAA"/>
        <property type="match status" value="2"/>
    </dbReference>
    <dbReference type="SMART" id="SM01086">
        <property type="entry name" value="ClpB_D2-small"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="SUPFAM" id="SSF52540">
        <property type="entry name" value="SSF52540"/>
        <property type="match status" value="2"/>
    </dbReference>
    <dbReference type="TIGRFAMs" id="TIGR03346">
        <property type="entry name" value="chaperone_ClpB"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PROSITE" id="PS00870">
        <property type="entry name" value="CLPAB_1"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PROSITE" id="PS00871">
        <property type="entry name" value="CLPAB_2"/>
        <property type="match status" value="1"/>
    </dbReference>
    <proteinExistence type="inferred from homology"/>
    <keyword evidence="4 8" id="KW-0067">ATP-binding</keyword>
    <keyword evidence="6 8" id="KW-0143">Chaperone</keyword>
    <keyword evidence="5 9" id="KW-0175">Coiled coil</keyword>
    <keyword evidence="3 8" id="KW-0547">Nucleotide-binding</keyword>
    <keyword evidence="13" id="KW-1185">Reference proteome</keyword>
    <feature type="domain" description="AAA" evidence="10">
        <location>
            <begin position="50"/>
            <end position="195"/>
        </location>
    </feature>
    <feature type="domain" description="AAA" evidence="10">
        <location>
            <begin position="449"/>
            <end position="604"/>
        </location>
    </feature>
    <feature type="domain" description="ClpB_D2-small" evidence="11">
        <location>
            <begin position="618"/>
            <end position="707"/>
        </location>
    </feature>
    <feature type="coiled-coil region" evidence="9">
        <location>
            <begin position="264"/>
            <end position="344"/>
        </location>
    </feature>
    <evidence type="ECO:0000256" key="1">
        <source>
            <dbReference type="ARBA" id="ARBA00008675"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="2">
        <source>
            <dbReference type="ARBA" id="ARBA00017574"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="3">
        <source>
            <dbReference type="ARBA" id="ARBA00022741"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="4">
        <source>
            <dbReference type="ARBA" id="ARBA00022840"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="5">
        <source>
            <dbReference type="ARBA" id="ARBA00023054"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="6">
        <source>
            <dbReference type="ARBA" id="ARBA00023186"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="7">
        <source>
            <dbReference type="ARBA" id="ARBA00026057"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="8">
        <source>
            <dbReference type="RuleBase" id="RU004432"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="9">
        <source>
            <dbReference type="SAM" id="Coils"/>
        </source>
    </evidence>
    <evidence type="ECO:0000259" key="10">
        <source>
            <dbReference type="SMART" id="SM00382"/>
        </source>
    </evidence>
    <evidence type="ECO:0000259" key="11">
        <source>
            <dbReference type="SMART" id="SM01086"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="12">
        <source>
            <dbReference type="EMBL" id="QNV50514.1"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="13">
        <source>
            <dbReference type="Proteomes" id="UP000000625"/>
        </source>
    </evidence>
    <sequence length="709" mass="79870" checksum="60270862D6198B55" modified="2021-02-10" version="1"> </sequence>
</entry>
<entry dataset="TrEMBL" created="2021-02-10" modified="2022-01-19" version="4" xmlns="http://uniprot.org/uniprot">
    <accession>A0A7H2C768</accession>
    <name>A0A7H2C768_ECOLI</name>
    <protein>
        <submittedName>
            <fullName evidence="11">Putative type II secretion system L-type protein YghE</fullName>
        </submittedName>
    </protein>
    <gene>
        <name evidence="11" type="primary">yghE</name>
        <name evidence="11" type="synonym">ecfB</name>
        <name evidence="11" type="synonym">ECK2964</name>
        <name evidence="11" type="ORF">b2969</name>
    </gene>
    <organism evidence="11 12">
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference evidence="11 12" key="1">
        <citation type="journal article" date="1997" name="Science" volume="277" first="1453" last="1462">
            <title>The complete genome sequence of Escherichia coli K-12.</title>
            <authorList>
                <person name="Blattner F.R."/>
                <person name="Plunkett G.III."/>
                <person name="Bloch C.A."/>
                <person name="Perna N.T."/>
                <person name="Burland V."/>
                <person name="Riley M."/>
                <person name="Collado-Vides J."/>
                <person name="Glasner J.D."/>
                <person name="Rode C.K."/>
                <person name="Mayhew G.F."/>
                <person name="Gregor J."/>
                <person name="Davis N.W."/>
                <person name="Kirkpatrick H.A."/>
                <person name="Goeden M.A."/>
                <person name="Rose D.J."/>
                <person name="Mau B."/>
                <person name="Shao Y."/>
            </authorList>
            <dbReference type="PubMed" id="9278503"/>
            <dbReference type="DOI" id="10.1126/science.277.5331.1453"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain evidence="12">K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <comment type="similarity">
        <text evidence="1">Belongs to the GSP L family.</text>
    </comment>
    <dbReference type="EMBL" id="U00096">
        <property type="protein sequence ID" value="QNV50515.1"/>
        <property type="molecule type" value="Genomic_DNA"/>
    </dbReference>
    <dbReference type="SMR" id="A0A7H2C768"/>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <dbReference type="GO" id="GO:0009276">
        <property type="term" value="C:Gram-negative-bacterium-type cell wall"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="GO" id="GO:0016021">
        <property type="term" value="C:integral component of membrane"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0005886">
        <property type="term" value="C:plasma membrane"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0015627">
        <property type="term" value="C:type II protein secretion system complex"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="GO" id="GO:0015628">
        <property type="term" value="P:protein secretion by the type II secretion system"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR025691">
        <property type="entry name" value="GspL_pp_dom"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR007812">
        <property type="entry name" value="T2SS_protein-GspL"/>
    </dbReference>
    <dbReference type="Pfam" id="PF12693">
        <property type="entry name" value="GspL_C"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="TIGRFAMs" id="TIGR01709">
        <property type="entry name" value="typeII_sec_gspL"/>
        <property type="match status" value="1"/>
    </dbReference>
    <proteinExistence type="inferred from homology"/>
    <keyword evidence="4" id="KW-0997">Cell inner membrane</keyword>
    <keyword evidence="3" id="KW-1003">Cell membrane</keyword>
    <keyword evidence="8 9" id="KW-0472">Membrane</keyword>
    <keyword evidence="6" id="KW-0653">Protein transport</keyword>
    <keyword evidence="12" id="KW-1185">Reference proteome</keyword>
    <keyword evidence="5 9" id="KW-0812">Transmembrane</keyword>
    <keyword evidence="7 9" id="KW-1133">Transmembrane helix</keyword>
    <keyword evidence="2" id="KW-0813">Transport</keyword>
    <feature type="transmembrane region" description="Helical" evidence="9">
        <location>
            <begin position="136"/>
            <end position="159"/>
        </location>
    </feature>
    <feature type="domain" description="GspL_C" evidence="10">
        <location>
            <begin position="128"/>
            <end position="285"/>
        </location>
    </feature>
    <evidence type="ECO:0000256" key="1">
        <source>
            <dbReference type="ARBA" id="ARBA00005318"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="2">
        <source>
            <dbReference type="ARBA" id="ARBA00022448"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="3">
        <source>
            <dbReference type="ARBA" id="ARBA00022475"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="4">
        <source>
            <dbReference type="ARBA" id="ARBA00022519"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="5">
        <source>
            <dbReference type="ARBA" id="ARBA00022692"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="6">
        <source>
            <dbReference type="ARBA" id="ARBA00022927"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="7">
        <source>
            <dbReference type="ARBA" id="ARBA00022989"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="8">
        <source>
            <dbReference type="ARBA" id="ARBA00023136"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="9">
        <source>
            <dbReference type="SAM" id="Phobius"/>
        </source>
    </evidence>
    <evidence type="ECO:0000259" key="10">
        <source>
            <dbReference type="Pfam" id="PF12693"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="11">
        <source>
            <dbReference type="EMBL" id="QNV50515.1"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="12">
        <source>
            <dbReference type="Proteomes" id="UP000000625"/>
        </source>
    </evidence>
    <sequence length="286" mass="32058" checksum="15305711D0597FCA" modified="2021-02-10" version="1">MIHQQHMRNIAQWLQENGITRATVAPDWMSIPCGFMACDAQRVICRIDECRGWSAGLALAPVMFRAQLNEQDLPLSLTVVGIAPEKLSAWAGADAERLTVTALPAITTYGEPEGNLLTGPWQPRVSYRKQWARWRVMILPILLILVALAVERGVTLWSVSEQVAQSRTQAEEQFLTLFPEQKRIVNLRSQVTMALKKYRPQADDTRLLAELSAIASTLKSASLSDIEMRGFTFDQKRQILHLQLRAANFASFDKLRSVLATDYVVQQDALQKEGDAVSGGVTLRRK</sequence>
</entry>
<entry dataset="TrEMBL" created="2021-02-10" modified="2022-08-03" version="5" xmlns="http://uniprot.org/uniprot">
    <accession>A0A7H2C769</accession>
    <name>A0A7H2C769_ECOLI</name>
    <protein>
        <submittedName>
            <fullName evidence="9">Putative type II secretion system C-type protein YghF</fullName>
        </submittedName>
    </protein>
    <gene>
        <name evidence="9" type="primary">yghF</name>
        <name evidence="9" type="synonym">ecfA</name>
        <name evidence="9" type="synonym">ECK2965</name>
        <name evidence="9" type="ORF">b2970</name>
    </gene>
    <organism evidence="9 10">
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference evidence="9 10" key="1">
        <citation type="journal article" date="1997" name="Science" volume="277" first="1453" last="1462">
            <title>The complete genome sequence of Escherichia coli K-12.</title>
            <authorList>
                <person name="Blattner F.R."/>
                <person name="Plunkett G.III."/>
                <person name="Bloch C.A."/>
                <person name="Perna N.T."/>
                <person name="Burland V."/>
                <person name="Riley M."/>
                <person name="Collado-Vides J."/>
                <person name="Glasner J.D."/>
                <person name="Rode C.K."/>
                <person name="Mayhew G.F."/>
                <person name="Gregor J."/>
                <person name="Davis N.W."/>
                <person name="Kirkpatrick H.A."/>
                <person name="Goeden M.A."/>
                <person name="Rose D.J."/>
                <person name="Mau B."/>
                <person name="Shao Y."/>
            </authorList>
            <dbReference type="PubMed" id="9278503"/>
            <dbReference type="DOI" id="10.1126/science.277.5331.1453"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain evidence="10">K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <comment type="similarity">
        <text evidence="1">Belongs to the GSP C family.</text>
    </comment>
    <dbReference type="EMBL" id="U00096">
        <property type="protein sequence ID" value="QNV50516.1"/>
        <property type="molecule type" value="Genomic_DNA"/>
    </dbReference>
    <dbReference type="RefSeq" id="WP_000135077.1">
        <property type="nucleotide sequence ID" value="NZ_LN832404.1"/>
    </dbReference>
    <dbReference type="SMR" id="A0A7H2C769"/>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <dbReference type="GO" id="GO:0016021">
        <property type="term" value="C:integral component of membrane"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0005886">
        <property type="term" value="C:plasma membrane"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0015627">
        <property type="term" value="C:type II protein secretion system complex"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="GO" id="GO:0016787">
        <property type="term" value="F:hydrolase activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProt"/>
    </dbReference>
    <dbReference type="GO" id="GO:0015628">
        <property type="term" value="P:protein secretion by the type II secretion system"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="GO" id="GO:0006508">
        <property type="term" value="P:proteolysis"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProt"/>
    </dbReference>
    <dbReference type="Gene3D" id="2.30.42.10">
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR036034">
        <property type="entry name" value="PDZ_sf"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR024961">
        <property type="entry name" value="T2SS_GspC_N"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR001639">
        <property type="entry name" value="T2SS_protein-GspC"/>
    </dbReference>
    <dbReference type="Pfam" id="PF11356">
        <property type="entry name" value="T2SSC"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="SUPFAM" id="SSF50156">
        <property type="entry name" value="SSF50156"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="TIGRFAMs" id="TIGR01713">
        <property type="entry name" value="typeII_sec_gspC"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PROSITE" id="PS01141">
        <property type="entry name" value="T2SP_C"/>
        <property type="match status" value="1"/>
    </dbReference>
    <proteinExistence type="inferred from homology"/>
    <keyword evidence="4" id="KW-0997">Cell inner membrane</keyword>
    <keyword evidence="3" id="KW-1003">Cell membrane</keyword>
    <keyword evidence="7" id="KW-0472">Membrane</keyword>
    <keyword evidence="10" id="KW-1185">Reference proteome</keyword>
    <keyword evidence="5" id="KW-0812">Transmembrane</keyword>
    <keyword evidence="6" id="KW-1133">Transmembrane helix</keyword>
    <keyword evidence="2" id="KW-0813">Transport</keyword>
    <feature type="domain" description="T2SSC" evidence="8">
        <location>
            <begin position="46"/>
            <end position="185"/>
        </location>
    </feature>
    <evidence type="ECO:0000256" key="1">
        <source>
            <dbReference type="ARBA" id="ARBA00007986"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="2">
        <source>
            <dbReference type="ARBA" id="ARBA00022448"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="3">
        <source>
            <dbReference type="ARBA" id="ARBA00022475"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="4">
        <source>
            <dbReference type="ARBA" id="ARBA00022519"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="5">
        <source>
            <dbReference type="ARBA" id="ARBA00022692"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="6">
        <source>
            <dbReference type="ARBA" id="ARBA00022989"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="7">
        <source>
            <dbReference type="ARBA" id="ARBA00023136"/>
        </source>
    </evidence>
    <evidence type="ECO:0000259" key="8">
        <source>
            <dbReference type="Pfam" id="PF11356"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="9">
        <source>
            <dbReference type="EMBL" id="QNV50516.1"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="10">
        <source>
            <dbReference type="Proteomes" id="UP000000625"/>
        </source>
    </evidence>
    <sequence length="331" mass="37349" checksum="3E26353F4DD5785C" modified="2021-02-10" version="1">MARVVFRDARIYLIQWLTKIRHTLNQRQSLNTDKEHLRKIARGMFWLMLLIISAKMAHSLWRYISFSAEYTAVSQPVNKPSRVDAKTFDKNDVQLISQQNWFGKYQPVAAQVKQPEPVPVAETRLNVVLRGIAFGARPGAVIEEGGKQQVYLQGETLGSHNAVIEEINRDHVMLRYQGKIERLSLAEEERSTVAVTNKKAVSDEAKQAVAEPAVSVPVEIPAAVRQALAKDPQKIFNYIQLTPVRKEGIVGYAAKPGADRSLFDASGFKEGDIAIALNQQDFTDPRAMIALMRQLPSMDSIQLTVLRKGARHDISIALRYRLFCPPYWKKS</sequence>
</entry>
<entry dataset="TrEMBL" created="2021-02-10" modified="2022-01-19" version="5" xmlns="http://uniprot.org/uniprot">
    <accession>A0A7H2C770</accession>
    <name>A0A7H2C770_ECOLI</name>
    <protein>
        <submittedName>
            <fullName evidence="2">McrBS</fullName>
        </submittedName>
    </protein>
    <gene>
        <name evidence="2" type="primary">mcrB</name>
        <name evidence="2" type="synonym">ECK4336</name>
        <name evidence="2" type="synonym">rglB</name>
        <name evidence="2" type="ORF">b4346</name>
    </gene>
    <organism evidence="2 3">
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference evidence="2 3" key="1">
        <citation type="journal article" date="1997" name="Science" volume="277" first="1453" last="1462">
            <title>The complete genome sequence of Escherichia coli K-12.</title>
            <authorList>
                <person name="Blattner F.R."/>
                <person name="Plunkett G.III."/>
                <person name="Bloch C.A."/>
                <person name="Perna N.T."/>
                <person name="Burland V."/>
                <person name="Riley M."/>
                <person name="Collado-Vides J."/>
                <person name="Glasner J.D."/>
                <person name="Rode C.K."/>
                <person name="Mayhew G.F."/>
                <person name="Gregor J."/>
                <person name="Davis N.W."/>
                <person name="Kirkpatrick H.A."/>
                <person name="Goeden M.A."/>
                <person name="Rose D.J."/>
                <person name="Mau B."/>
                <person name="Shao Y."/>
            </authorList>
            <dbReference type="PubMed" id="9278503"/>
            <dbReference type="DOI" id="10.1126/science.277.5331.1453"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain evidence="3">K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <dbReference type="EMBL" id="U00096">
        <property type="protein sequence ID" value="QNV50517.1"/>
        <property type="molecule type" value="Genomic_DNA"/>
    </dbReference>
    <dbReference type="SMR" id="A0A7H2C770"/>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <dbReference type="GO" id="GO:0005524">
        <property type="term" value="F:ATP binding"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="GO" id="GO:0016887">
        <property type="term" value="F:ATP hydrolysis activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="Gene3D" id="3.40.50.300">
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR003593">
        <property type="entry name" value="AAA+_ATPase"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR011704">
        <property type="entry name" value="ATPase_dyneun-rel_AAA"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR027417">
        <property type="entry name" value="P-loop_NTPase"/>
    </dbReference>
    <dbReference type="Pfam" id="PF07728">
        <property type="entry name" value="AAA_5"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="SMART" id="SM00382">
        <property type="entry name" value="AAA"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="SUPFAM" id="SSF52540">
        <property type="entry name" value="SSF52540"/>
        <property type="match status" value="1"/>
    </dbReference>
    <proteinExistence type="predicted"/>
    <keyword evidence="3" id="KW-1185">Reference proteome</keyword>
    <feature type="domain" description="AAA" evidence="1">
        <location>
            <begin position="32"/>
            <end position="195"/>
        </location>
    </feature>
    <evidence type="ECO:0000259" key="1">
        <source>
            <dbReference type="SMART" id="SM00382"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="2">
        <source>
            <dbReference type="EMBL" id="QNV50517.1"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="3">
        <source>
            <dbReference type="Proteomes" id="UP000000625"/>
        </source>
    </evidence>
    <sequence length="298" mass="34660" checksum="B05DE88C3CAB9321" modified="2021-02-10" version="1">MSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKAPQRVNMVQFHQSYSYEDFIQGYRPNGVGFRRKDGIFYNFCQQAKEQPEKKYIFIIDEINRANLSKVFGEVMMLMEHDKRGENWSVPLTYSENDEERFYVPENVYIIGLMNTADRSLAVVDYALRRRFSFIDIEPGFDTPQFRNFLLNKKAEPSFVESLCQKMNELNQEISKEATILGKGFRIGHSYFCCGLEDGTSPDTQWLNEIVMTDIAPLLEEYFFDDPYKQQKWTNKLLGDS</sequence>
</entry>
<entry dataset="TrEMBL" created="2021-02-10" modified="2021-02-10" version="1" xmlns="http://uniprot.org/uniprot">
    <accession>A0A7H2C771</accession>
    <name>A0A7H2C771_ECOLI</name>
    <protein>
        <submittedName>
            <fullName evidence="1">Protein YadX</fullName>
        </submittedName>
    </protein>
    <gene>
        <name evidence="1" type="primary">yadX</name>
        <name evidence="1" type="synonym">ECK4622</name>
        <name evidence="1" type="ORF">b4765</name>
    </gene>
    <organism evidence="1 2">
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference evidence="1 2" key="1">
        <citation type="journal article" date="1997" name="Science" volume="277" first="1453" last="1462">
            <title>The complete genome sequence of Escherichia coli K-12.</title>
            <authorList>
                <person name="Blattner F.R."/>
                <person name="Plunkett G.III."/>
                <person name="Bloch C.A."/>
                <person name="Perna N.T."/>
                <person name="Burland V."/>
                <person name="Riley M."/>
                <person name="Collado-Vides J."/>
                <person name="Glasner J.D."/>
                <person name="Rode C.K."/>
                <person name="Mayhew G.F."/>
                <person name="Gregor J."/>
                <person name="Davis N.W."/>
                <person name="Kirkpatrick H.A."/>
                <person name="Goeden M.A."/>
                <person name="Rose D.J."/>
                <person name="Mau B."/>
                <person name="Shao Y."/>
            </authorList>
            <dbReference type="PubMed" id="9278503"/>
            <dbReference type="DOI" id="10.1126/science.277.5331.1453"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain evidence="2">K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <dbReference type="EMBL" id="U00096">
        <property type="protein sequence ID" value="QNV50518.1"/>
        <property type="molecule type" value="Genomic_DNA"/>
    </dbReference>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <proteinExistence type="predicted"/>
    <keyword evidence="2" id="KW-1185">Reference proteome</keyword>
    <evidence type="ECO:0000313" key="1">
        <source>
            <dbReference type="EMBL" id="QNV50518.1"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="2">
        <source>
            <dbReference type="Proteomes" id="UP000000625"/>
        </source>
    </evidence>
    <sequence length="15" mass="1806" checksum="29BB5AD8798AEB9E" modified="2021-02-10" version="1">MERASKMPSSYLYDQ</sequence>
</entry>
<entry dataset="TrEMBL" created="2021-02-10" modified="2021-02-10" version="1" xmlns="http://uniprot.org/uniprot">
    <accession>A0A7H2C772</accession>
    <name>A0A7H2C772_ECOLI</name>
    <protein>
        <submittedName>
            <fullName evidence="1">Putative translational regulatory protein ArgL</fullName>
        </submittedName>
    </protein>
    <gene>
        <name evidence="1" type="primary">argL</name>
        <name evidence="1" type="synonym">ECK4623</name>
        <name evidence="1" type="ORF">b4766</name>
    </gene>
    <organism evidence="1 2">
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference evidence="1 2" key="1">
        <citation type="journal article" date="1997" name="Science" volume="277" first="1453" last="1462">
            <title>The complete genome sequence of Escherichia coli K-12.</title>
            <authorList>
                <person name="Blattner F.R."/>
                <person name="Plunkett G.III."/>
                <person name="Bloch C.A."/>
                <person name="Perna N.T."/>
                <person name="Burland V."/>
                <person name="Riley M."/>
                <person name="Collado-Vides J."/>
                <person name="Glasner J.D."/>
                <person name="Rode C.K."/>
                <person name="Mayhew G.F."/>
                <person name="Gregor J."/>
                <person name="Davis N.W."/>
                <person name="Kirkpatrick H.A."/>
                <person name="Goeden M.A."/>
                <person name="Rose D.J."/>
                <person name="Mau B."/>
                <person name="Shao Y."/>
            </authorList>
            <dbReference type="PubMed" id="9278503"/>
            <dbReference type="DOI" id="10.1126/science.277.5331.1453"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain evidence="2">K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <dbReference type="EMBL" id="U00096">
        <property type="protein sequence ID" value="QNV50519.1"/>
        <property type="molecule type" value="Genomic_DNA"/>
    </dbReference>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <proteinExistence type="predicted"/>
    <keyword evidence="2" id="KW-1185">Reference proteome</keyword>
    <evidence type="ECO:0000313" key="1">
        <source>
            <dbReference type="EMBL" id="QNV50519.1"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="2">
        <source>
            <dbReference type="Proteomes" id="UP000000625"/>
        </source>
    </evidence>
    <sequence length="31" mass="3681" checksum="05BD49DCAABCA776" modified="2021-02-10" version="1">MNNYTYKVNFNSISGVRHARIKCPIYTKNTF</sequence>
</entry>
<entry dataset="TrEMBL" created="2021-02-10" modified="2021-02-10" version="1" xmlns="http://uniprot.org/uniprot">
    <accession>A0A7H2C773</accession>
    <name>A0A7H2C773_ECOLI</name>
    <protein>
        <submittedName>
            <fullName evidence="1">Protein YtiB</fullName>
        </submittedName>
    </protein>
    <gene>
        <name evidence="1" type="primary">ytiB</name>
        <name evidence="1" type="synonym">ECK4624</name>
        <name evidence="1" type="ORF">b4767</name>
    </gene>
    <organism evidence="1 2">
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference evidence="1 2" key="1">
        <citation type="journal article" date="1997" name="Science" volume="277" first="1453" last="1462">
            <title>The complete genome sequence of Escherichia coli K-12.</title>
            <authorList>
                <person name="Blattner F.R."/>
                <person name="Plunkett G.III."/>
                <person name="Bloch C.A."/>
                <person name="Perna N.T."/>
                <person name="Burland V."/>
                <person name="Riley M."/>
                <person name="Collado-Vides J."/>
                <person name="Glasner J.D."/>
                <person name="Rode C.K."/>
                <person name="Mayhew G.F."/>
                <person name="Gregor J."/>
                <person name="Davis N.W."/>
                <person name="Kirkpatrick H.A."/>
                <person name="Goeden M.A."/>
                <person name="Rose D.J."/>
                <person name="Mau B."/>
                <person name="Shao Y."/>
            </authorList>
            <dbReference type="PubMed" id="9278503"/>
            <dbReference type="DOI" id="10.1126/science.277.5331.1453"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain evidence="2">K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <dbReference type="EMBL" id="U00096">
        <property type="protein sequence ID" value="QNV50520.1"/>
        <property type="molecule type" value="Genomic_DNA"/>
    </dbReference>
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            <title>The complete genome sequence of Escherichia coli K-12.</title>
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                <person name="Bloch C.A."/>
                <person name="Perna N.T."/>
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                <person name="Riley M."/>
                <person name="Collado-Vides J."/>
                <person name="Glasner J.D."/>
                <person name="Rode C.K."/>
                <person name="Mayhew G.F."/>
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                <person name="Kirkpatrick H.A."/>
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            <title>The complete genome sequence of Escherichia coli K-12.</title>
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            <title>The complete genome sequence of Escherichia coli K-12.</title>
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            <title>The complete genome sequence of Escherichia coli K-12.</title>
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            <title>The complete genome sequence of Escherichia coli K-12.</title>
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            <title>The complete genome sequence of Escherichia coli K-12.</title>
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            <title>The complete genome sequence of Escherichia coli K-12.</title>
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            <title>The complete genome sequence of Escherichia coli K-12.</title>
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                <person name="Bloch C.A."/>
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                <person name="Riley M."/>
                <person name="Collado-Vides J."/>
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    </reference>
    <comment type="function">
        <text evidence="1">A small protein (arrest peptide) encoded upstream of inducible ornithine carboxylase gene (speF) that controls expression of downstream genes (usually speF and potE) by transcriptional and translational attenuation.</text>
    </comment>
    <comment type="subunit">
        <text evidence="1">Binds ornithine in stalled 70S ribosomes, blocking the upper two-thirds of the exit tunnel. Contacts 23S rRNA and ribosomal proteins L4 and L22.</text>
    </comment>
    <comment type="induction">
        <text evidence="1">Induced by ornithine, repressed by putrescine. Part of the speFL-speF-potE operon.</text>
    </comment>
    <comment type="similarity">
        <text evidence="1">Belongs to the speF operon leader peptide family.</text>
    </comment>
    <dbReference type="EMBL" id="U00096">
        <property type="protein sequence ID" value="QNV50557.1"/>
        <property type="molecule type" value="Genomic_DNA"/>
    </dbReference>
    <dbReference type="SMR" id="A0A7H2C7B0"/>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <dbReference type="GO" id="GO:0019843">
        <property type="term" value="F:rRNA binding"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0006448">
        <property type="term" value="P:regulation of translational elongation"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-UniRule"/>
    </dbReference>
    <dbReference type="GO" id="GO:0031556">
        <property type="term" value="P:transcriptional attenuation by ribosome"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-UniRule"/>
    </dbReference>
    <dbReference type="HAMAP" id="MF_00851">
        <property type="entry name" value="Leader_SpeFL"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR021237">
        <property type="entry name" value="SpeFL"/>
    </dbReference>
    <proteinExistence type="evidence at transcript level"/>
    <keyword evidence="1" id="KW-0428">Leader peptide</keyword>
    <keyword evidence="3" id="KW-1185">Reference proteome</keyword>
    <keyword evidence="1" id="KW-0694">RNA-binding</keyword>
    <keyword evidence="1" id="KW-0699">rRNA-binding</keyword>
    <keyword evidence="1" id="KW-0804">Transcription</keyword>
    <keyword evidence="1" id="KW-0805">Transcription regulation</keyword>
    <keyword evidence="1" id="KW-0810">Translation regulation</keyword>
    <feature type="short sequence motif" description="Ornithine recognition loop" evidence="1">
        <location>
            <begin position="10"/>
            <end position="16"/>
        </location>
    </feature>
    <feature type="binding site" evidence="1">
        <location>
            <position position="13"/>
        </location>
        <ligand>
            <name>L-ornithine</name>
            <dbReference type="ChEBI" id="CHEBI:46911"/>
        </ligand>
    </feature>
    <evidence type="ECO:0000256" key="1">
        <source>
            <dbReference type="HAMAP-Rule" id="MF_00851"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="2">
        <source>
            <dbReference type="EMBL" id="QNV50557.1"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="3">
        <source>
            <dbReference type="Proteomes" id="UP000000625"/>
        </source>
    </evidence>
    <sequence length="34" mass="4249" checksum="67E222CF9D30C2C5" modified="2021-02-10" version="1">MENNSRTMPHIRRTTHIMKFAHRNSFDFHFFNAR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1986-07-21" modified="2022-08-03" version="207" xmlns="http://uniprot.org/uniprot">
    <accession>P00452-2</accession>
    <name>RIR1_ECOLI</name>
    <protein>
        <recommendedName>
            <fullName>Isoform Alpha' of Ribonucleoside-diphosphate reductase 1 subunit alpha</fullName>
            <ecNumber>1.17.4.1</ecNumber>
        </recommendedName>
        <alternativeName>
            <fullName>Protein B1</fullName>
        </alternativeName>
        <alternativeName>
            <fullName>Ribonucleoside-diphosphate reductase 1 R1 subunit</fullName>
        </alternativeName>
        <alternativeName>
            <fullName>Ribonucleotide reductase 1</fullName>
        </alternativeName>
    </protein>
    <gene>
        <name type="primary">nrdA</name>
        <name type="synonym">dnaF</name>
        <name type="ordered locus">b2234</name>
        <name type="ordered locus">JW2228</name>
    </gene>
    <organism>
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference key="1">
        <citation type="journal article" date="1984" name="Proc. Natl. Acad. Sci. U.S.A." volume="81" first="4294" last="4297">
            <title>Primary structure of the Escherichia coli ribonucleoside diphosphate reductase operon.</title>
            <authorList>
                <person name="Carlson J."/>
                <person name="Fuchs J.A."/>
                <person name="Messing J."/>
            </authorList>
            <dbReference type="PubMed" id="6087316"/>
            <dbReference type="DOI" id="10.1073/pnas.81.14.4294"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    </reference>
    <reference key="2">
        <citation type="journal article" date="1985" name="Eur. J. Biochem." volume="150" first="423" last="427">
            <title>Protein B1 of ribonucleotide reductase. Direct analytical data and comparisons with data indirectly deduced from the nucleotide sequence of the Escherichia coli nrdA gene.</title>
            <authorList>
                <person name="Sjoeberg B.-M."/>
                <person name="Eriksson S."/>
                <person name="Joernvall H."/>
                <person name="Carlquist M."/>
                <person name="Eklund H."/>
            </authorList>
            <dbReference type="PubMed" id="3894026"/>
            <dbReference type="DOI" id="10.1111/j.1432-1033.1985.tb09037.x"/>
        </citation>
        <scope>PARTIAL PROTEIN SEQUENCE</scope>
    </reference>
    <reference key="3">
        <citation type="journal article" date="1988" name="Nucleic Acids Res." volume="16" first="4174" last="4174">
            <title>Nucleotide sequence of the gene coding for the large subunit of ribonucleotide reductase of Escherichia coli. Correction.</title>
            <authorList>
                <person name="Nilsson O."/>
                <person name="Aaberg A."/>
                <person name="Lundqvist T."/>
                <person name="Sjoeberg B.-M."/>
            </authorList>
            <dbReference type="PubMed" id="3287341"/>
            <dbReference type="DOI" id="10.1093/nar/16.9.4174"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
        <source>
            <strain>K12</strain>
        </source>
    </reference>
    <reference key="4">
        <citation type="journal article" date="1989" name="J. Biol. Chem." volume="264" first="12249" last="12252">
            <title>Evidence for two different classes of redox-active cysteines in ribonucleotide reductase of Escherichia coli.</title>
            <authorList>
                <person name="Aaberg A."/>
                <person name="Hahne S."/>
                <person name="Karlsson M."/>
                <person name="Larsson A."/>
                <person name="Ormoe M."/>
                <person name="Aahgren A."/>
                <person name="Sjoeberg B.-M."/>
            </authorList>
            <dbReference type="PubMed" id="2663852"/>
        </citation>
        <scope>ACTIVE SITES</scope>
    </reference>
    <reference key="5">
        <citation type="journal article" date="1994" name="Nature" volume="370" first="533" last="539">
            <title>Structure of ribonucleotide reductase protein R1.</title>
            <authorList>
                <person name="Uhlin U."/>
                <person name="Eklund H."/>
            </authorList>
            <dbReference type="PubMed" id="8052308"/>
            <dbReference type="DOI" id="10.1038/370533a0"/>
        </citation>
        <scope>X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)</scope>
    </reference>
    <reference key="6">
        <citation type="journal article" date="1996" name="J. Biol. Chem." volume="271" first="20655" last="20659">
            <title>Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase.</title>
            <authorList>
                <person name="Ekberg M."/>
                <person name="Sahlin M."/>
                <person name="Eriksson M."/>
                <person name="Sjoberg B.M."/>
            </authorList>
            <dbReference type="PubMed" id="8702814"/>
            <dbReference type="DOI" id="10.1074/jbc.271.34.20655"/>
        </citation>
        <scope>ACTIVE SITES</scope>
        <scope>MUTAGENESIS OF TYR-730 AND TYR-731</scope>
    </reference>
    <reference key="7">
        <citation type="journal article" date="1997" name="DNA Res." volume="4" first="91" last="113">
            <title>Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features.</title>
            <authorList>
                <person name="Yamamoto Y."/>
                <person name="Aiba H."/>
                <person name="Baba T."/>
                <person name="Hayashi K."/>
                <person name="Inada T."/>
                <person name="Isono K."/>
                <person name="Itoh T."/>
                <person name="Kimura S."/>
                <person name="Kitagawa M."/>
                <person name="Makino K."/>
                <person name="Miki T."/>
                <person name="Mitsuhashi N."/>
                <person name="Mizobuchi K."/>
                <person name="Mori H."/>
                <person name="Nakade S."/>
                <person name="Nakamura Y."/>
                <person name="Nashimoto H."/>
                <person name="Oshima T."/>
                <person name="Oyama S."/>
                <person name="Saito N."/>
                <person name="Sampei G."/>
                <person name="Satoh Y."/>
                <person name="Sivasundaram S."/>
                <person name="Tagami H."/>
                <person name="Takahashi H."/>
                <person name="Takeda J."/>
                <person name="Takemoto K."/>
                <person name="Uehara K."/>
                <person name="Wada C."/>
                <person name="Yamagata S."/>
                <person name="Horiuchi T."/>
            </authorList>
            <dbReference type="PubMed" id="9205837"/>
            <dbReference type="DOI" id="10.1093/dnares/4.2.91"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / W3110 / ATCC 27325 / DSM 5911</strain>
        </source>
    </reference>
    <reference key="8">
        <citation type="journal article" date="1997" name="J. Biol. Chem." volume="272" first="31533" last="31541">
            <title>A new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductase.</title>
            <authorList>
                <person name="Persson A.L."/>
                <person name="Eriksson M."/>
                <person name="Katterle B."/>
                <person name="Potsch S."/>
                <person name="Sahlin M."/>
                <person name="Sjoberg B.M."/>
            </authorList>
            <dbReference type="PubMed" id="9395490"/>
            <dbReference type="DOI" id="10.1074/jbc.272.50.31533"/>
        </citation>
        <scope>X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF MUTANTS ALA-441; ASP-441 AND GLN-441</scope>
        <scope>DISULFIDE BOND</scope>
        <scope>SUBUNIT</scope>
        <scope>ACTIVE SITE</scope>
        <scope>ACTIVITY REGULATION</scope>
        <scope>ENZYME MECHANISM</scope>
        <scope>MUTAGENESIS OF GLU-441</scope>
    </reference>
    <reference key="9">
        <citation type="journal article" date="1997" name="Science" volume="277" first="1453" last="1462">
            <title>The complete genome sequence of Escherichia coli K-12.</title>
            <authorList>
                <person name="Blattner F.R."/>
                <person name="Plunkett G.III."/>
                <person name="Bloch C.A."/>
                <person name="Perna N.T."/>
                <person name="Burland V."/>
                <person name="Riley M."/>
                <person name="Collado-Vides J."/>
                <person name="Glasner J.D."/>
                <person name="Rode C.K."/>
                <person name="Mayhew G.F."/>
                <person name="Gregor J."/>
                <person name="Davis N.W."/>
                <person name="Kirkpatrick H.A."/>
                <person name="Goeden M.A."/>
                <person name="Rose D.J."/>
                <person name="Mau B."/>
                <person name="Shao Y."/>
            </authorList>
            <dbReference type="PubMed" id="9278503"/>
            <dbReference type="DOI" id="10.1126/science.277.5331.1453"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <reference evidence="1 2 3" key="10">
        <citation type="journal article" date="1997" name="Structure" volume="5" first="1077" last="1092">
            <title>Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding.</title>
            <authorList>
                <person name="Eriksson M."/>
                <person name="Uhlin U."/>
                <person name="Ramaswamy S."/>
                <person name="Ekberg M."/>
                <person name="Regnstroem K."/>
                <person name="Sjoeberg B.-M."/>
                <person name="Eklund H."/>
            </authorList>
            <dbReference type="PubMed" id="9309223"/>
            <dbReference type="DOI" id="10.1016/S0969-2126(97)00259-1"/>
        </citation>
        <scope>X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEXES WITH ATP; GDP AND DTTP</scope>
        <scope>DISULFIDE BOND</scope>
        <scope>SUBUNIT</scope>
        <scope>ACTIVITY REGULATION</scope>
    </reference>
    <reference key="11">
        <citation type="journal article" date="1999" name="J. Mol. Biol." volume="292" first="151" last="161">
            <title>Binding specificity and mechanistic insight into glutaredoxin-catalyzed protein disulfide reduction.</title>
            <authorList>
                <person name="Berardi M.J."/>
                <person name="Bushweller J.H."/>
            </authorList>
            <dbReference type="PubMed" id="10493864"/>
            <dbReference type="DOI" id="10.1006/jmbi.1999.3067"/>
        </citation>
        <scope>STRUCTURE BY NMR OF 737-761</scope>
        <scope>BINDING SITES</scope>
    </reference>
    <reference key="12">
        <citation type="submission" date="2004-04" db="EMBL/GenBank/DDBJ databases">
            <authorList>
                <person name="Sjoeberg B.-M."/>
            </authorList>
        </citation>
        <scope>SEQUENCE REVISION TO 526-527</scope>
    </reference>
    <reference key="13">
        <citation type="journal article" date="2006" name="Mol. Syst. Biol." volume="2" first="E1" last="E5">
            <title>Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.</title>
            <authorList>
                <person name="Hayashi K."/>
                <person name="Morooka N."/>
                <person name="Yamamoto Y."/>
                <person name="Fujita K."/>
                <person name="Isono K."/>
                <person name="Choi S."/>
                <person name="Ohtsubo E."/>
                <person name="Baba T."/>
                <person name="Wanner B.L."/>
                <person name="Mori H."/>
                <person name="Horiuchi T."/>
            </authorList>
            <dbReference type="PubMed" id="16738553"/>
            <dbReference type="DOI" id="10.1038/msb4100049"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / W3110 / ATCC 27325 / DSM 5911</strain>
        </source>
    </reference>
    <reference key="14">
        <citation type="journal article" date="2009" name="Mol. Cell" volume="36" first="845" last="860">
            <title>Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli.</title>
            <authorList>
                <person name="Davies B.W."/>
                <person name="Kohanski M.A."/>
                <person name="Simmons L.A."/>
                <person name="Winkler J.A."/>
                <person name="Collins J.J."/>
                <person name="Walker G.C."/>
            </authorList>
            <dbReference type="PubMed" id="20005847"/>
            <dbReference type="DOI" id="10.1016/j.molcel.2009.11.024"/>
        </citation>
        <scope>ACTIVITY REGULATION</scope>
        <scope>INDUCTION BY HYDROXYUREA</scope>
        <source>
            <strain>K12 / MC4100 / ATCC 35695 / DSM 6574</strain>
        </source>
    </reference>
    <reference key="15">
        <citation type="journal article" date="2009" name="Mol. Cell. Proteomics" volume="8" first="215" last="225">
            <title>Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.</title>
            <authorList>
                <person name="Zhang J."/>
                <person name="Sprung R."/>
                <person name="Pei J."/>
                <person name="Tan X."/>
                <person name="Kim S."/>
                <person name="Zhu H."/>
                <person name="Liu C.F."/>
                <person name="Grishin N.V."/>
                <person name="Zhao Y."/>
            </authorList>
            <dbReference type="PubMed" id="18723842"/>
            <dbReference type="DOI" id="10.1074/mcp.M800187-MCP200"/>
        </citation>
        <scope>ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283</scope>
        <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
        <source>
            <strain>K12 / JW1106</strain>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <comment type="alternative products">
        <event type="alternative initiation"/>
        <isoform>
            <id>P00452-2</id>
            <name>Alpha'</name>
            <sequence type="described" ref="VSP_018871 VSP_018872"/>
        </isoform>
        <isoform>
            <id>P00452-1</id>
            <name>Alpha</name>
            <sequence type="displayed"/>
        </isoform>
    </comment>
    <dbReference type="EC" id="1.17.4.1"/>
    <dbReference type="Proteomes" id="UP000000318">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <proteinExistence type="evidence at protein level"/>
    <evidence type="ECO:0007744" key="1">
        <source>
            <dbReference type="PDB" id="1R1R"/>
        </source>
    </evidence>
    <evidence type="ECO:0007744" key="2">
        <source>
            <dbReference type="PDB" id="2R1R"/>
        </source>
    </evidence>
    <evidence type="ECO:0007744" key="3">
        <source>
            <dbReference type="PDB" id="3R1R"/>
        </source>
    </evidence>
    <sequence length="736" mass="82860" checksum="498ADEDC2154C084" modified="1997-11-01" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1986-07-21" modified="2022-08-03" version="218" xmlns="http://uniprot.org/uniprot">
    <accession>P02919-2</accession>
    <name>PBPB_ECOLI</name>
    <protein>
        <recommendedName>
            <fullName>Isoform Gamma of Penicillin-binding protein 1B</fullName>
            <shortName>PBP-1b</shortName>
            <shortName>PBP1b</shortName>
        </recommendedName>
        <alternativeName>
            <fullName>Murein polymerase</fullName>
        </alternativeName>
        <domain>
            <recommendedName>
                <fullName>Penicillin-insensitive transglycosylase</fullName>
                <ecNumber evidence="1 2">2.4.1.129</ecNumber>
            </recommendedName>
            <alternativeName>
                <fullName>Peptidoglycan TGase</fullName>
            </alternativeName>
            <alternativeName>
                <fullName>Peptidoglycan glycosyltransferase</fullName>
            </alternativeName>
        </domain>
        <domain>
            <recommendedName>
                <fullName>Penicillin-sensitive transpeptidase</fullName>
                <ecNumber evidence="2">3.4.16.4</ecNumber>
            </recommendedName>
            <alternativeName>
                <fullName>DD-transpeptidase</fullName>
            </alternativeName>
        </domain>
    </protein>
    <gene>
        <name type="primary">mrcB</name>
        <name type="synonym">pbpF</name>
        <name type="synonym">ponB</name>
        <name type="ordered locus">b0149</name>
        <name type="ordered locus">JW0145</name>
    </gene>
    <organism>
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference key="1">
        <citation type="journal article" date="1984" name="J. Biol. Chem." volume="259" first="13937" last="13946">
            <title>Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides. Penicillin-binding protein 1Bs of Escherichia coli with activities of transglycosylase and transpeptidase.</title>
            <authorList>
                <person name="Nakagawa J."/>
                <person name="Tamaki S."/>
                <person name="Tomioka S."/>
                <person name="Matsuhashi M."/>
            </authorList>
            <dbReference type="PubMed" id="6389538"/>
        </citation>
        <scope>CATALYTIC ACTIVITY</scope>
    </reference>
    <reference key="2">
        <citation type="journal article" date="1985" name="Eur. J. Biochem." volume="147" first="437" last="446">
            <title>The nucleotide sequences of the ponA and ponB genes encoding penicillin-binding protein 1A and 1B of Escherichia coli K12.</title>
            <authorList>
                <person name="Broome-Smith J.K."/>
                <person name="Edelman A."/>
                <person name="Yousif S."/>
                <person name="Spratt B.G."/>
            </authorList>
            <dbReference type="PubMed" id="3882429"/>
            <dbReference type="DOI" id="10.1111/j.1432-1033.1985.tb08768.x"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
        <source>
            <strain>K12</strain>
        </source>
    </reference>
    <reference key="3">
        <citation type="journal article" date="1985" name="Proc. Natl. Acad. Sci. U.S.A." volume="82" first="1999" last="2003">
            <title>Sequences of the active-site peptides of three of the high-Mr penicillin-binding proteins of Escherichia coli K-12.</title>
            <authorList>
                <person name="Keck W."/>
                <person name="Glauner B."/>
                <person name="Schwarz U."/>
                <person name="Broome-Smith J.K."/>
                <person name="Spratt B.G."/>
            </authorList>
            <dbReference type="PubMed" id="3920658"/>
            <dbReference type="DOI" id="10.1073/pnas.82.7.1999"/>
        </citation>
        <scope>PROTEIN SEQUENCE OF 497-525</scope>
        <source>
            <strain>K12</strain>
        </source>
    </reference>
    <reference key="4">
        <citation type="journal article" date="1987" name="Mol. Microbiol." volume="1" first="101" last="106">
            <title>Use of a beta-lactamase fusion vector to investigate the organization of penicillin-binding protein 1B in the cytoplasmic membrane of Escherichia coli.</title>
            <authorList>
                <person name="Edelman A."/>
                <person name="Bowler L."/>
                <person name="Broome-Smith J.K."/>
                <person name="Spratt B.G."/>
            </authorList>
            <dbReference type="PubMed" id="3330753"/>
            <dbReference type="DOI" id="10.1111/j.1365-2958.1987.tb00533.x"/>
        </citation>
        <scope>TOPOLOGY</scope>
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        <scope>SEQUENCE REVISION TO 103 AND 754</scope>
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        <scope>INTERACTION WITH MLTA; UVRA; FTSL AND FTSN</scope>
        <scope>MEMBRANE TOPOLOGY</scope>
        <scope>CATALYTIC ACTIVITY</scope>
        <scope>DOMAIN</scope>
        <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
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    <comment type="alternative products">
        <event type="alternative initiation"/>
        <isoform>
            <id>P02919-1</id>
            <name>Alpha</name>
            <name>Long</name>
            <sequence type="displayed"/>
        </isoform>
        <isoform>
            <id>P02919-2</id>
            <name>Gamma</name>
            <name>Short</name>
            <sequence type="described" ref="VSP_018737"/>
        </isoform>
    </comment>
    <dbReference type="EC" id="2.4.1.129" evidence="1 2"/>
    <dbReference type="EC" id="3.4.16.4" evidence="2"/>
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            <dbReference type="PubMed" id="19458048"/>
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    <evidence type="ECO:0000269" key="2">
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            <dbReference type="PubMed" id="6389538"/>
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    <sequence length="799" mass="88890" checksum="2A4869BED79A2530" modified="2003-07-19" version="2"> </sequence>
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<entry dataset="Swiss-Prot" created="1988-01-01" modified="2022-08-03" version="204" xmlns="http://uniprot.org/uniprot">
    <accession>P06710-2</accession>
    <name>DPO3X_ECOLI</name>
    <protein>
        <recommendedName>
            <fullName>Isoform gamma of DNA polymerase III subunit tau</fullName>
            <ecNumber>2.7.7.7</ecNumber>
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        <name type="primary">dnaX</name>
        <name type="synonym">dnaZ</name>
        <name type="synonym">dnaZX</name>
        <name type="ordered locus">b0470</name>
        <name type="ordered locus">JW0459</name>
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    <organism>
        <name type="scientific">Escherichia coli (strain K12)</name>
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            <taxon>Bacteria</taxon>
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            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
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                <person name="Conrad J."/>
                <person name="Scheres S.H."/>
                <person name="Lamers M.H."/>
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            <dbReference type="PubMed" id="26499492"/>
            <dbReference type="DOI" id="10.7554/eLife.11134"/>
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        <scope>STRUCTURE BY ELECTRON MICROSCOPY (8.00 ANGSTROMS) OF 500-643 OF DNAE; DNAN; DNAQ; DNAX WITH AND WITHOUT DNA</scope>
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    <comment type="function">
        <text evidence="5">Interacts with the delta and delta' subunits to transfer the beta subunit on the DNA (PubMed:9927437). Interacts with ATP, drives ATP-induced conformational changes in the gamma complex that opens the beta sliding clamp ring. After loading of primed DNA ATP is hydrolyzed and the beta sliding clamp ring closes (PubMed:9927437).</text>
    </comment>
    <comment type="interaction">
        <interactant intactId="EBI-2604194">
            <id>P06710-2</id>
        </interactant>
        <interactant intactId="EBI-554913">
            <id>P23367</id>
            <label>mutL</label>
        </interactant>
        <organismsDiffer>false</organismsDiffer>
        <experiments>2</experiments>
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    <comment type="interaction">
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            <id>P06710-2</id>
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            <label>dnaX</label>
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        <interactant intactId="EBI-2604194">
            <id>P06710-2</id>
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        <interactant intactId="EBI-549176">
            <id>P28632</id>
            <label>holD</label>
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        <organismsDiffer>false</organismsDiffer>
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    <comment type="interaction">
        <interactant intactId="EBI-2604194">
            <id>P06710-2</id>
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        <interactant intactId="EBI-549153">
            <id>P28630</id>
            <label>holA</label>
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        <organismsDiffer>false</organismsDiffer>
        <experiments>6</experiments>
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    <comment type="alternative products">
        <event type="ribosomal frameshifting"/>
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            <id>P06710-2</id>
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        </isoform>
        <isoform>
            <id>P06710-1</id>
            <name>tau</name>
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        </isoform>
        <text evidence="1 2 3">The production of the two protein products from this region is due to programmed ribosomal frameshifting. Frameshifting is about 40% efficient.</text>
    </comment>
    <comment type="miscellaneous">
        <text evidence="1 2 3 4">Formed by programmed ribosomal frameshifting to a premature stop codon in the -1 frame at codon 430, the last residue is thus Glu and not Ser. Mutants which remove the frameshift are viable, suggesting strongly that gamma is not essential for viability (PubMed:8376347).</text>
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    </evidence>
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    </evidence>
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            <dbReference type="PDB" id="1JR3"/>
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    </evidence>
    <evidence type="ECO:0007744" key="7">
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            <dbReference type="PDB" id="5FKU"/>
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    <evidence type="ECO:0007744" key="8">
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    <sequence length="431" mass="47545" checksum="8177A07F31BC86E3" modified="1988-01-01" version="1">MSYQVLARKWRPQTFADVVGQEHVLTALANGLSLGRIHHAYLFSGTRGVGKTSIARLLAKGLNCETGITATPCGVCDNCREIEQGRFVDLIEIDAASRTKVEDTRDLLDNVQYAPARGRFKVYLIDEVHMLSRHSFNALLKTLEEPPEHVKFLLATTDPQKLPVTILSRCLQFHLKALDVEQIRHQLEHILNEEHIAHEPRALQLLARAAEGSLRDALSLTDQAIASGDGQVSTQAVSAMLGTLDDDQALSLVEAMVEANGERVMALINEAAARGIEWEALLVEMLGLLHRIAMVQLSPAALGNDMAAIELRMRELARTIPPTDIQLYYQTLLIGRKELPYAPDRRMGVEMTLLRALAFHPRMPLPEPEVPRQSFAPVAPTAVMTPTQVPPQPQSAPQQAPTVPLPETTSQVLAARQQLQRVQGATKAKKE</sequence>
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    <accession>P07363-2</accession>
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        <recommendedName>
            <fullName>Isoform cheA(S) of Chemotaxis protein CheA</fullName>
            <ecNumber>2.7.13.3</ecNumber>
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    <gene>
        <name type="primary">cheA</name>
        <name type="ordered locus">b1888</name>
        <name type="ordered locus">JW1877</name>
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        <name type="scientific">Escherichia coli (strain K12)</name>
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        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference key="1">
        <citation type="journal article" date="1986" name="J. Bacteriol." volume="165" first="161" last="166">
            <title>Nucleotide sequence corresponding to five chemotaxis genes in Escherichia coli.</title>
            <authorList>
                <person name="Mutoh N."/>
                <person name="Simon M.I."/>
            </authorList>
            <dbReference type="PubMed" id="3510184"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 430-654</scope>
    </reference>
    <reference key="2">
        <citation type="journal article" date="1988" name="Cell" volume="53" first="89" last="96">
            <title>Mutants defective in bacterial chemotaxis show modified protein phosphorylation.</title>
            <authorList>
                <person name="Oosawa K."/>
                <person name="Hess J.F."/>
                <person name="Simon M.I."/>
            </authorList>
            <dbReference type="PubMed" id="2832069"/>
            <dbReference type="DOI" id="10.1016/0092-8674(88)90490-4"/>
        </citation>
        <scope>PHOSPHORYLATION AT HIS-48</scope>
        <scope>DOMAINS</scope>
    </reference>
    <reference key="3">
        <citation type="journal article" date="1991" name="J. Bacteriol." volume="173" first="2116" last="2119">
            <title>Tandem translation starts in the cheA locus of Escherichia coli.</title>
            <authorList>
                <person name="Kofoid E.C."/>
                <person name="Parkinson J.S."/>
            </authorList>
            <dbReference type="PubMed" id="2002011"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    </reference>
    <reference key="4">
        <citation type="journal article" date="1991" name="Proc. Natl. Acad. Sci. U.S.A." volume="88" first="6269" last="6273">
            <title>Bacterial chemotaxis signaling complexes: formation of a CheA/CheW complex enhances autophosphorylation and affinity for CheY.</title>
            <authorList>
                <person name="McNally D.F."/>
                <person name="Matsumura P."/>
            </authorList>
            <dbReference type="PubMed" id="2068106"/>
            <dbReference type="DOI" id="10.1073/pnas.88.14.6269"/>
        </citation>
        <scope>SUBUNIT</scope>
    </reference>
    <reference key="5">
        <citation type="journal article" date="1996" name="Biochemistry" volume="35" first="433" last="443">
            <title>Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker.</title>
            <authorList>
                <person name="Zhou H."/>
                <person name="McEvoy M.M."/>
                <person name="Lowry D.F."/>
                <person name="Swanson R.V."/>
                <person name="Simon M.I."/>
                <person name="Dahlquist F.W."/>
            </authorList>
            <dbReference type="PubMed" id="8555213"/>
            <dbReference type="DOI" id="10.1021/bi951960e"/>
        </citation>
        <scope>STRUCTURE BY NMR OF 1-233</scope>
    </reference>
    <reference key="6">
        <citation type="journal article" date="1996" name="Biochemistry" volume="35" first="5633" last="5640">
            <title>Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy.</title>
            <authorList>
                <person name="McEvoy M.M."/>
                <person name="Muhandiram D.R."/>
                <person name="Kyw L.E."/>
                <person name="Dahlquist F.W."/>
            </authorList>
            <dbReference type="PubMed" id="8639521"/>
            <dbReference type="DOI" id="10.1021/bi952707h"/>
        </citation>
        <scope>STRUCTURE BY NMR OF 124-257</scope>
    </reference>
    <reference key="7">
        <citation type="journal article" date="1996" name="DNA Res." volume="3" first="379" last="392">
            <title>A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map.</title>
            <authorList>
                <person name="Itoh T."/>
                <person name="Aiba H."/>
                <person name="Baba T."/>
                <person name="Hayashi K."/>
                <person name="Inada T."/>
                <person name="Isono K."/>
                <person name="Kasai H."/>
                <person name="Kimura S."/>
                <person name="Kitakawa M."/>
                <person name="Kitagawa M."/>
                <person name="Makino K."/>
                <person name="Miki T."/>
                <person name="Mizobuchi K."/>
                <person name="Mori H."/>
                <person name="Mori T."/>
                <person name="Motomura K."/>
                <person name="Nakade S."/>
                <person name="Nakamura Y."/>
                <person name="Nashimoto H."/>
                <person name="Nishio Y."/>
                <person name="Oshima T."/>
                <person name="Saito N."/>
                <person name="Sampei G."/>
                <person name="Seki Y."/>
                <person name="Sivasundaram S."/>
                <person name="Tagami H."/>
                <person name="Takeda J."/>
                <person name="Takemoto K."/>
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                <person name="Yamamoto Y."/>
                <person name="Horiuchi T."/>
            </authorList>
            <dbReference type="PubMed" id="9097040"/>
            <dbReference type="DOI" id="10.1093/dnares/3.6.379"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / W3110 / ATCC 27325 / DSM 5911</strain>
        </source>
    </reference>
    <reference key="8">
        <citation type="journal article" date="1997" name="Biochemistry" volume="36" first="699" last="710">
            <title>Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.</title>
            <authorList>
                <person name="Zhou H."/>
                <person name="Dahlquist F.W."/>
            </authorList>
            <dbReference type="PubMed" id="9020767"/>
            <dbReference type="DOI" id="10.1021/bi961663p"/>
        </citation>
        <scope>STRUCTURE BY NMR OF 1-134</scope>
    </reference>
    <reference key="9">
        <citation type="journal article" date="1997" name="Science" volume="277" first="1453" last="1462">
            <title>The complete genome sequence of Escherichia coli K-12.</title>
            <authorList>
                <person name="Blattner F.R."/>
                <person name="Plunkett G.III."/>
                <person name="Bloch C.A."/>
                <person name="Perna N.T."/>
                <person name="Burland V."/>
                <person name="Riley M."/>
                <person name="Collado-Vides J."/>
                <person name="Glasner J.D."/>
                <person name="Rode C.K."/>
                <person name="Mayhew G.F."/>
                <person name="Gregor J."/>
                <person name="Davis N.W."/>
                <person name="Kirkpatrick H.A."/>
                <person name="Goeden M.A."/>
                <person name="Rose D.J."/>
                <person name="Mau B."/>
                <person name="Shao Y."/>
            </authorList>
            <dbReference type="PubMed" id="9278503"/>
            <dbReference type="DOI" id="10.1126/science.277.5331.1453"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <reference key="10">
        <citation type="journal article" date="1998" name="Nat. Struct. Biol." volume="5" first="25" last="29">
            <title>Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY.</title>
            <authorList>
                <person name="Welch M."/>
                <person name="Chinardet N."/>
                <person name="Mourey L."/>
                <person name="Birck C."/>
                <person name="Samama J.-P."/>
            </authorList>
            <dbReference type="PubMed" id="9437425"/>
            <dbReference type="DOI" id="10.1038/nsb0198-25"/>
        </citation>
        <scope>X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 158-228</scope>
    </reference>
    <reference key="11">
        <citation type="journal article" date="1998" name="Proc. Natl. Acad. Sci. U.S.A." volume="95" first="7333" last="7338">
            <title>Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway.</title>
            <authorList>
                <person name="McEvoy M.M."/>
                <person name="Hausrath A.C."/>
                <person name="Randolph G.B."/>
                <person name="Remington S.J."/>
                <person name="Dahlquist F.W."/>
            </authorList>
            <dbReference type="PubMed" id="9636149"/>
            <dbReference type="DOI" id="10.1073/pnas.95.13.7333"/>
        </citation>
        <scope>X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 158-226</scope>
    </reference>
    <reference key="12">
        <citation type="journal article" date="2006" name="Mol. Syst. Biol." volume="2" first="E1" last="E5">
            <title>Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.</title>
            <authorList>
                <person name="Hayashi K."/>
                <person name="Morooka N."/>
                <person name="Yamamoto Y."/>
                <person name="Fujita K."/>
                <person name="Isono K."/>
                <person name="Choi S."/>
                <person name="Ohtsubo E."/>
                <person name="Baba T."/>
                <person name="Wanner B.L."/>
                <person name="Mori H."/>
                <person name="Horiuchi T."/>
            </authorList>
            <dbReference type="PubMed" id="16738553"/>
            <dbReference type="DOI" id="10.1038/msb4100049"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / W3110 / ATCC 27325 / DSM 5911</strain>
        </source>
    </reference>
    <comment type="alternative products">
        <event type="alternative initiation"/>
        <isoform>
            <id>P07363-2</id>
            <name>cheA(S)</name>
            <name>short</name>
            <sequence type="described" ref="VSP_018886"/>
        </isoform>
        <isoform>
            <id>P07363-1</id>
            <name>cheA(L)</name>
            <name>large</name>
            <name>long</name>
            <sequence type="displayed"/>
        </isoform>
    </comment>
    <dbReference type="EC" id="2.7.13.3"/>
    <dbReference type="Proteomes" id="UP000000318">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <proteinExistence type="evidence at protein level"/>
    <sequence length="557" mass="60422" checksum="8982A8C04F2AEDBA" modified="1997-11-01" version="3"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1986-07-21" modified="2022-08-03" version="142" xmlns="http://uniprot.org/uniprot">
    <accession>P0A705-2</accession>
    <name>IF2_ECOLI</name>
    <protein>
        <recommendedName>
            <fullName>Isoform Beta of Translation initiation factor IF-2</fullName>
        </recommendedName>
    </protein>
    <gene>
        <name type="primary">infB</name>
        <name type="synonym">gicD</name>
        <name type="synonym">ssyG</name>
        <name type="ordered locus">b3168</name>
        <name type="ordered locus">JW3137</name>
    </gene>
    <organism>
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference key="1">
        <citation type="journal article" date="1984" name="Nucleic Acids Res." volume="12" first="3333" last="3342">
            <title>The nucleotide sequence of the cloned nusA gene and its flanking region of Escherichia coli.</title>
            <authorList>
                <person name="Ishii S."/>
                <person name="Ihara M."/>
                <person name="Maekawa T."/>
                <person name="Nakamura Y."/>
                <person name="Uchida H."/>
                <person name="Imamoto F."/>
            </authorList>
            <dbReference type="PubMed" id="6326058"/>
            <dbReference type="DOI" id="10.1093/nar/12.7.3333"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22</scope>
    </reference>
    <reference key="2">
        <citation type="journal article" date="1984" name="Proc. Natl. Acad. Sci. U.S.A." volume="81" first="7787" last="7791">
            <title>Sequence of the initiation factor IF2 gene: unusual protein features and homologies with elongation factors.</title>
            <authorList>
                <person name="Sacerdot C."/>
                <person name="Dessen P."/>
                <person name="Hershey J.W.B."/>
                <person name="Plumbridge J.A."/>
                <person name="Grunberg-Manago M."/>
            </authorList>
            <dbReference type="PubMed" id="6096856"/>
            <dbReference type="DOI" id="10.1073/pnas.81.24.7787"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    </reference>
    <reference key="3">
        <citation type="journal article" date="1985" name="EMBO J." volume="4" first="223" last="229">
            <title>Two translational initiation sites in the infB gene are used to express initiation factor IF2 alpha and IF2 beta in Escherichia coli.</title>
            <authorList>
                <person name="Plumbridge J.A."/>
                <person name="Deville F."/>
                <person name="Sacerdot C."/>
                <person name="Petersen H.U."/>
                <person name="Cenatiempo Y."/>
                <person name="Cozzone A."/>
                <person name="Grunberg-Manago M."/>
                <person name="Hershey J.W."/>
            </authorList>
            <dbReference type="PubMed" id="3894004"/>
        </citation>
        <scope>PROTEIN SEQUENCE OF 1-11 AND 159-174 (ISOFORMS ALPHA AND BETA)</scope>
    </reference>
    <reference key="4">
        <citation type="journal article" date="1987" name="Biochemistry" volume="26" first="5070" last="5076">
            <title>The protein synthesis initiation factor 2 G-domain. Study of a functionally active C-terminal 65-kilodalton fragment of IF2 from Escherichia coli.</title>
            <authorList>
                <person name="Cenatiempo Y."/>
                <person name="Deville F."/>
                <person name="Dondon J."/>
                <person name="Grunberg-Manago M."/>
                <person name="Sacerdot C."/>
                <person name="Hershey J.W."/>
                <person name="Hansen H.F."/>
                <person name="Petersen H.U."/>
                <person name="Clark B.F."/>
                <person name="Kjeldgaard M."/>
            </authorList>
            <dbReference type="PubMed" id="2444251"/>
            <dbReference type="DOI" id="10.1021/bi00390a028"/>
        </citation>
        <scope>PROTEIN SEQUENCE OF 290-304</scope>
        <scope>FUNCTION</scope>
        <scope>PROTEOLYTIC CLEAVAGE</scope>
    </reference>
    <reference key="5">
        <citation type="journal article" date="1988" name="Nucleic Acids Res." volume="16" first="10803" last="10816">
            <title>The existence of two genes between infB and rpsO in the Escherichia coli genome: DNA sequencing and S1 nuclease mapping.</title>
            <authorList>
                <person name="Sands J.F."/>
                <person name="Regnier P."/>
                <person name="Cummings H.S."/>
                <person name="Grunberg-Manago M."/>
                <person name="Hershey J.W.B."/>
            </authorList>
            <dbReference type="PubMed" id="2849753"/>
            <dbReference type="DOI" id="10.1093/nar/16.22.10803"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 864-890</scope>
        <scope>INDUCTION</scope>
        <scope>OPERON</scope>
        <source>
            <strain>K12</strain>
        </source>
    </reference>
    <reference key="6">
        <citation type="journal article" date="1991" name="Biochem. Biophys. Res. Commun." volume="181" first="1572" last="1579">
            <title>Tandem translation of E. coli initiation factor IF2 beta: purification and characterization in vitro of two active forms.</title>
            <authorList>
                <person name="Nyengaard N.R."/>
                <person name="Mortensen K.K."/>
                <person name="Lassen S.F."/>
                <person name="Hershey J.W.B."/>
                <person name="Sperling-Petersen H.U."/>
            </authorList>
            <dbReference type="PubMed" id="1764105"/>
            <dbReference type="DOI" id="10.1016/0006-291X(91)92118-4"/>
        </citation>
        <scope>PROTEIN SEQUENCE OF 159-174 AND 166-174 (ISOFORMS BETA AND BETA')</scope>
        <scope>FUNCTION</scope>
        <scope>SUBCELLULAR LOCATION</scope>
    </reference>
    <reference key="7">
        <citation type="journal article" date="1991" name="Biochimie" volume="73" first="1557" last="1566">
            <title>Structural and functional domains of E coli initiation factor IF2.</title>
            <authorList>
                <person name="Laalami S."/>
                <person name="Sacerdot C."/>
                <person name="Vachon G."/>
                <person name="Mortensen K."/>
                <person name="Sperling-Petersen H.U."/>
                <person name="Cenatiempo Y."/>
                <person name="Grunberg-Manago M."/>
            </authorList>
            <dbReference type="PubMed" id="1805969"/>
            <dbReference type="DOI" id="10.1016/0300-9084(91)90191-3"/>
        </citation>
        <scope>DOMAIN STRUCTURE</scope>
        <scope>REVIEW</scope>
    </reference>
    <reference key="8">
        <citation type="journal article" date="1992" name="J. Mol. Biol." volume="225" first="67" last="80">
            <title>Both forms of translational initiation factor IF2 (alpha and beta) are required for maximal growth of Escherichia coli. Evidence for two translational initiation codons for IF2 beta.</title>
            <authorList>
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            </authorList>
            <dbReference type="PubMed" id="1374802"/>
            <dbReference type="DOI" id="10.1016/0022-2836(92)91026-L"/>
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        <scope>PROTEIN SEQUENCE OF 159-169 AND 166-171 (ISOFORMS BETA AND BETA')</scope>
        <scope>FUNCTION</scope>
        <scope>DISRUPTION PHENOTYPE</scope>
        <scope>MUTAGENESIS OF VAL-158 AND MET-165</scope>
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            <dbReference type="PubMed" id="9298644"/>
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        <scope>IDENTIFICATION BY 2D-GEL</scope>
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            </authorList>
            <dbReference type="PubMed" id="9428651"/>
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        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
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            <strain>Various clinical strains</strain>
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            <dbReference type="PubMed" id="9278503"/>
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        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
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            <dbReference type="PubMed" id="12600987"/>
            <dbReference type="DOI" id="10.1074/jbc.M212960200"/>
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        <scope>STRUCTURE BY NMR OF 2-50</scope>
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            <strain>K12</strain>
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        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
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            <dbReference type="PubMed" id="18223068"/>
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        <scope>PARTIALLY SUPPRESSES A RSGA MUTANT</scope>
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            <strain>K12</strain>
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        <scope>ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-808</scope>
        <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
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            <strain>K12 / JW1106</strain>
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        <scope>FUNCTION</scope>
        <scope>SUBUNIT</scope>
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        <scope>MODEL BY ELECTRON MICROSCOPY (18.3 ANGSTROMS)</scope>
        <scope>SUBUNIT</scope>
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        <scope>FUNCTION</scope>
        <scope>SUBUNIT</scope>
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    <comment type="alternative products">
        <event type="alternative initiation"/>
        <isoform>
            <id>P0A705-2</id>
            <name evidence="1 2 3">Beta</name>
            <sequence type="described" ref="VSP_018758 VSP_018759"/>
        </isoform>
        <isoform>
            <id>P0A705-1</id>
            <name evidence="3">Alpha</name>
            <sequence type="displayed"/>
        </isoform>
        <isoform>
            <id>P0A705-3</id>
            <name evidence="1 2">Beta'</name>
            <sequence type="described" ref="VSP_018760"/>
        </isoform>
    </comment>
    <comment type="miscellaneous">
        <text evidence="4">Also called beta1.</text>
    </comment>
    <dbReference type="Proteomes" id="UP000000318">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <proteinExistence type="evidence at protein level"/>
    <evidence type="ECO:0000269" key="1">
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            <dbReference type="PubMed" id="1374802"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="2">
        <source>
            <dbReference type="PubMed" id="1764105"/>
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    <evidence type="ECO:0000269" key="3">
        <source>
            <dbReference type="PubMed" id="3894004"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="4">
        <source>
            <dbReference type="PubMed" id="1374802"/>
        </source>
    </evidence>
    <sequence length="733" mass="79745" checksum="A85674E0145D5E66" modified="2005-06-07" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1986-07-21" modified="2022-08-03" version="142" xmlns="http://uniprot.org/uniprot">
    <accession>P0A705-3</accession>
    <name>IF2_ECOLI</name>
    <protein>
        <recommendedName>
            <fullName>Isoform Beta' of Translation initiation factor IF-2</fullName>
        </recommendedName>
    </protein>
    <gene>
        <name type="primary">infB</name>
        <name type="synonym">gicD</name>
        <name type="synonym">ssyG</name>
        <name type="ordered locus">b3168</name>
        <name type="ordered locus">JW3137</name>
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    <organism>
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
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        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22</scope>
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        <scope>PROTEIN SEQUENCE OF 1-11 AND 159-174 (ISOFORMS ALPHA AND BETA)</scope>
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        <scope>PROTEIN SEQUENCE OF 290-304</scope>
        <scope>FUNCTION</scope>
        <scope>PROTEOLYTIC CLEAVAGE</scope>
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        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 864-890</scope>
        <scope>INDUCTION</scope>
        <scope>OPERON</scope>
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        <scope>PROTEIN SEQUENCE OF 159-174 AND 166-174 (ISOFORMS BETA AND BETA')</scope>
        <scope>FUNCTION</scope>
        <scope>SUBCELLULAR LOCATION</scope>
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            <dbReference type="PubMed" id="1805969"/>
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        <scope>DOMAIN STRUCTURE</scope>
        <scope>REVIEW</scope>
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            <dbReference type="PubMed" id="1374802"/>
            <dbReference type="DOI" id="10.1016/0022-2836(92)91026-L"/>
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        <scope>PROTEIN SEQUENCE OF 159-169 AND 166-171 (ISOFORMS BETA AND BETA')</scope>
        <scope>FUNCTION</scope>
        <scope>DISRUPTION PHENOTYPE</scope>
        <scope>MUTAGENESIS OF VAL-158 AND MET-165</scope>
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            <dbReference type="PubMed" id="9298644"/>
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        <scope>IDENTIFICATION BY 2D-GEL</scope>
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            <dbReference type="PubMed" id="9428651"/>
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        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
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        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
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        <scope>STRUCTURE BY NMR OF 2-50</scope>
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                <person name="Fujita K."/>
                <person name="Isono K."/>
                <person name="Choi S."/>
                <person name="Ohtsubo E."/>
                <person name="Baba T."/>
                <person name="Wanner B.L."/>
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                <person name="Horiuchi T."/>
            </authorList>
            <dbReference type="PubMed" id="16738553"/>
            <dbReference type="DOI" id="10.1038/msb4100049"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / W3110 / ATCC 27325 / DSM 5911</strain>
        </source>
    </reference>
    <reference key="15">
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            <title>Genetic interaction screens with ordered overexpression and deletion clone sets implicate the Escherichia coli GTPase YjeQ in late ribosome biogenesis.</title>
            <authorList>
                <person name="Campbell T.L."/>
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            </authorList>
            <dbReference type="PubMed" id="18223068"/>
            <dbReference type="DOI" id="10.1128/JB.01744-07"/>
        </citation>
        <scope>PARTIALLY SUPPRESSES A RSGA MUTANT</scope>
        <source>
            <strain>K12</strain>
        </source>
    </reference>
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            <dbReference type="PubMed" id="18723842"/>
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        <scope>ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-808</scope>
        <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
        <source>
            <strain>K12 / JW1106</strain>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
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                <person name="Milon P."/>
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            <dbReference type="PubMed" id="20224578"/>
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        </citation>
        <scope>FUNCTION</scope>
        <scope>SUBUNIT</scope>
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            <authorList>
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            <dbReference type="PubMed" id="21750663"/>
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        </citation>
        <scope>MODEL BY ELECTRON MICROSCOPY (18.3 ANGSTROMS)</scope>
        <scope>SUBUNIT</scope>
    </reference>
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                <person name="Milon P."/>
                <person name="Rodnina M.V."/>
            </authorList>
            <dbReference type="PubMed" id="22515367"/>
            <dbReference type="DOI" id="10.3109/10409238.2012.678284"/>
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        <scope>REVIEW</scope>
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            <title>Real-time assembly landscape of bacterial 30S translation initiation complex.</title>
            <authorList>
                <person name="Milon P."/>
                <person name="Maracci C."/>
                <person name="Filonava L."/>
                <person name="Gualerzi C.O."/>
                <person name="Rodnina M.V."/>
            </authorList>
            <dbReference type="PubMed" id="22562136"/>
            <dbReference type="DOI" id="10.1038/nsmb.2285"/>
        </citation>
        <scope>FUNCTION</scope>
        <scope>SUBUNIT</scope>
    </reference>
    <comment type="alternative products">
        <event type="alternative initiation"/>
        <isoform>
            <id>P0A705-3</id>
            <name evidence="1 2">Beta'</name>
            <sequence type="described" ref="VSP_018760"/>
        </isoform>
        <isoform>
            <id>P0A705-2</id>
            <name evidence="1 2 3">Beta</name>
            <sequence type="described" ref="VSP_018759 VSP_018758"/>
        </isoform>
        <isoform>
            <id>P0A705-1</id>
            <name evidence="3">Alpha</name>
            <sequence type="displayed"/>
        </isoform>
    </comment>
    <comment type="miscellaneous">
        <text evidence="4">Also called beta2.</text>
    </comment>
    <dbReference type="Proteomes" id="UP000000318">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <proteinExistence type="evidence at protein level"/>
    <evidence type="ECO:0000269" key="1">
        <source>
            <dbReference type="PubMed" id="1374802"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="2">
        <source>
            <dbReference type="PubMed" id="1764105"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="3">
        <source>
            <dbReference type="PubMed" id="3894004"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="4">
        <source>
            <dbReference type="PubMed" id="1374802"/>
        </source>
    </evidence>
    <sequence length="726" mass="78927" checksum="08C16925C01D0199" modified="2005-06-07" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1986-07-21" modified="2022-08-03" version="145" xmlns="http://uniprot.org/uniprot">
    <accession>P0A988-2</accession>
    <name>DPO3B_ECOLI</name>
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        <recommendedName>
            <fullName evidence="3">Isoform Beta* of Beta sliding clamp</fullName>
            <shortName>Beta clamp</shortName>
            <shortName>Sliding clamp</shortName>
        </recommendedName>
        <alternativeName>
            <fullName>Beta-clamp processivity factor</fullName>
        </alternativeName>
        <alternativeName>
            <fullName>DNA polymerase III beta sliding clamp subunit</fullName>
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    <gene>
        <name type="primary">dnaN</name>
        <name type="ordered locus">b3701</name>
        <name type="ordered locus">JW3678</name>
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    <organism>
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference key="1">
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            <dbReference type="PubMed" id="6234204"/>
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        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    </reference>
    <reference key="2">
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        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 342-366</scope>
    </reference>
    <reference key="3">
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            <authorList>
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            <dbReference type="PubMed" id="6379647"/>
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        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 297-366</scope>
    </reference>
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            </authorList>
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        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-170</scope>
    </reference>
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        </citation>
        <scope>FUNCTION AS PROCESSIVITY FACTOR</scope>
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        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14</scope>
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        <scope>FUNCTION WITH DNA POLYMERASE II (POLB)</scope>
        <scope>SUBUNIT</scope>
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                <person name="Stukenberg P.T."/>
                <person name="Studwell-Vaughan P.S."/>
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            <dbReference type="PubMed" id="2040637"/>
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        <scope>FUNCTION AS A TETHER</scope>
        <scope>SUBUNIT</scope>
        <scope>INTERACTION WITH DNAE</scope>
    </reference>
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            <dbReference type="PubMed" id="1575709"/>
            <dbReference type="DOI" id="10.1002/bies.950140206"/>
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        <scope>REVIEW</scope>
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            <dbReference type="PubMed" id="1349852"/>
            <dbReference type="DOI" id="10.1016/0092-8674(92)90445-I"/>
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        <scope>X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)</scope>
    </reference>
    <reference key="11">
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        <scope>FUNCTION WITH DNA POLYMERASE II (POLB)</scope>
        <scope>SUBUNIT</scope>
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            <dbReference type="PubMed" id="7686882"/>
            <dbReference type="DOI" id="10.1006/geno.1993.1230"/>
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        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
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            <title>A smaller form of the sliding clamp subunit of DNA polymerase III is induced by UV irradiation in Escherichia coli.</title>
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                <person name="Skaliter R."/>
                <person name="Paz-Elizur T."/>
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            <dbReference type="PubMed" id="8576210"/>
            <dbReference type="DOI" id="10.1074/jbc.271.5.2478"/>
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        <scope>IDENTIFICATION OF ISOFORM BETA*</scope>
        <scope>FUNCTION</scope>
        <scope>INDUCTION BY UV</scope>
        <source>
            <strain>K12 / MC4100 / ATCC 35695 / DSM 6574</strain>
        </source>
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        </citation>
        <scope>ALTERNATIVE PROMOTER USAGE (ISOFORMS BETA AND BETA*)</scope>
        <scope>INDUCTION BY NALIDIXIC ACID</scope>
        <scope>MUTAGENESIS OF ALA-133; MET-135 AND MET-146</scope>
        <source>
            <strain>K12 / MC4100 / ATCC 35695 / DSM 6574</strain>
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            <dbReference type="PubMed" id="8576212"/>
            <dbReference type="DOI" id="10.1074/jbc.271.5.2491"/>
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        <scope>CHARACTERIZATION OF BETA*</scope>
        <scope>SUBUNIT</scope>
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            <dbReference type="PubMed" id="9298644"/>
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        <scope>IDENTIFICATION BY 2D-GEL</scope>
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            <dbReference type="PubMed" id="9278503"/>
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        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
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                <person name="Hingorani M.M."/>
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            </authorList>
            <dbReference type="PubMed" id="9927437"/>
            <dbReference type="DOI" id="10.1093/emboj/18.3.771"/>
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        <scope>RING OPENING BY DELTA SUBUNIT (HOLA)</scope>
        <scope>SUBUNIT</scope>
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                <person name="Pham P."/>
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            <dbReference type="DOI" id="10.1038/35010020"/>
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        <scope>FUNCTION WITH DNA POLYMERASES IV (DINB) AND V (UMUCD)</scope>
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        <scope>X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH DELTA SUBUNIT (HOLA)</scope>
        <scope>PROBABLE MECHANISM OF CLAMP OPENING</scope>
        <scope>MUTAGENESIS OF 272-ILE-LEU-273</scope>
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        <scope>INTERACTION WITH MUTS; LIGASE AND POLA</scope>
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        <scope>INTERACTION WITH DINB; DNAE; HOLA; MUTS; POLB AND UMUC</scope>
        <source>
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                <person name="Oakley A.J."/>
                <person name="Prosselkov P."/>
                <person name="Wijffels G."/>
                <person name="Beck J.L."/>
                <person name="Wilce M.C."/>
                <person name="Dixon N.E."/>
            </authorList>
            <dbReference type="PubMed" id="12832762"/>
            <dbReference type="DOI" id="10.1107/S0907444903009958"/>
        </citation>
        <scope>X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS)</scope>
    </reference>
    <reference evidence="8" key="24">
        <citation type="journal article" date="2003" name="EMBO J." volume="22" first="5883" last="5892">
            <title>Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the beta-clamp.</title>
            <authorList>
                <person name="Bunting K.A."/>
                <person name="Roe S.M."/>
                <person name="Pearl L.H."/>
            </authorList>
            <dbReference type="PubMed" id="14592985"/>
            <dbReference type="DOI" id="10.1093/emboj/cdg568"/>
        </citation>
        <scope>X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH DINB</scope>
        <scope>FUNCTION</scope>
    </reference>
    <reference key="25">
        <citation type="journal article" date="2004" name="Biochemistry" volume="43" first="5661" last="5671">
            <title>Inhibition of protein interactions with the beta(2) sliding clamp of Escherichia coli DNA polymerase III by peptides from beta(2)-binding proteins.</title>
            <authorList>
                <person name="Wijffels G."/>
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                <person name="Prosselkov P."/>
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                <person name="Lilley P.E."/>
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                <person name="Brown S.E."/>
                <person name="Alewood P.F."/>
                <person name="Jennings P.A."/>
                <person name="Dixon N.E."/>
            </authorList>
            <dbReference type="PubMed" id="15134440"/>
            <dbReference type="DOI" id="10.1021/bi036229j"/>
        </citation>
        <scope>CONSENSUS SEQUENCE FOR BINDING TO THE SLIDING CLAMP</scope>
    </reference>
    <reference key="26">
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            <title>Interaction of the sliding clamp beta-subunit and Hda, a DnaA-related protein.</title>
            <authorList>
                <person name="Kurz M."/>
                <person name="Dalrymple B."/>
                <person name="Wijffels G."/>
                <person name="Kongsuwan K."/>
            </authorList>
            <dbReference type="PubMed" id="15150238"/>
            <dbReference type="DOI" id="10.1128/JB.186.11.3508-3515.2004"/>
        </citation>
        <scope>INTERACTION WITH HDA</scope>
    </reference>
    <reference key="27">
        <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6738" last="6748">
            <title>The Escherichia coli dnaN159 mutant displays altered DNA polymerase usage and chronic SOS induction.</title>
            <authorList>
                <person name="Sutton M.D."/>
            </authorList>
            <dbReference type="PubMed" id="15466025"/>
            <dbReference type="DOI" id="10.1128/JB.186.20.6738-6748.2004"/>
        </citation>
        <scope>FUNCTION AT REPLICATION FORK</scope>
        <scope>INTERACTION WITH DNAE</scope>
        <scope>MUTAGENESIS OF GLY-66 AND GLY-174</scope>
    </reference>
    <reference evidence="7" key="28">
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                <person name="Burnouf D.Y."/>
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                <person name="Dumas P."/>
            </authorList>
            <dbReference type="PubMed" id="14729336"/>
            <dbReference type="DOI" id="10.1016/J.JMB.2003.11.049"/>
        </citation>
        <scope>X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH PEPTIDE OF DINB</scope>
        <scope>FUNCTION</scope>
        <scope>SUBUNIT</scope>
    </reference>
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            <title>Cellular DNA replicases: components and dynamics at the replication fork.</title>
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                <person name="Johnson A."/>
                <person name="O'Donnell M."/>
            </authorList>
            <dbReference type="PubMed" id="15952889"/>
            <dbReference type="DOI" id="10.1146/annurev.biochem.73.011303.073859"/>
        </citation>
        <scope>REVIEW</scope>
    </reference>
    <reference key="30">
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            <title>A sliding-clamp toolbelt binds high- and low-fidelity DNA polymerases simultaneously.</title>
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                <person name="Indiani C."/>
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                <person name="Goodman M.F."/>
                <person name="O'Donnell M."/>
            </authorList>
            <dbReference type="PubMed" id="16168375"/>
            <dbReference type="DOI" id="10.1016/j.molcel.2005.08.011"/>
        </citation>
        <scope>FUNCTION IN POLYMERASE CHOICE</scope>
        <scope>SUBUNIT</scope>
        <scope>MUTAGENESIS OF 272-ILE-LEU-273</scope>
    </reference>
    <reference key="31">
        <citation type="journal article" date="2006" name="Mol. Syst. Biol." volume="2" first="E1" last="E5">
            <title>Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.</title>
            <authorList>
                <person name="Hayashi K."/>
                <person name="Morooka N."/>
                <person name="Yamamoto Y."/>
                <person name="Fujita K."/>
                <person name="Isono K."/>
                <person name="Choi S."/>
                <person name="Ohtsubo E."/>
                <person name="Baba T."/>
                <person name="Wanner B.L."/>
                <person name="Mori H."/>
                <person name="Horiuchi T."/>
            </authorList>
            <dbReference type="PubMed" id="16738553"/>
            <dbReference type="DOI" id="10.1038/msb4100049"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / W3110 / ATCC 27325 / DSM 5911</strain>
        </source>
    </reference>
    <reference evidence="10" key="32">
        <citation type="journal article" date="2008" name="Cell" volume="132" first="43" last="54">
            <title>Structure of a sliding clamp on DNA.</title>
            <authorList>
                <person name="Georgescu R.E."/>
                <person name="Kim S.S."/>
                <person name="Yurieva O."/>
                <person name="Kuriyan J."/>
                <person name="Kong X.P."/>
                <person name="O'Donnell M."/>
            </authorList>
            <dbReference type="PubMed" id="18191219"/>
            <dbReference type="DOI" id="10.1016/j.cell.2007.11.045"/>
        </citation>
        <scope>X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) IN COMPLEX WITH PRIMED DNA</scope>
        <scope>FUNCTION</scope>
        <scope>SUBUNIT</scope>
        <scope>DNA-BINDING</scope>
        <scope>MUTAGENESIS OF ARG-24; GLN-149; 153-TYR-TYR-154 AND 272-ILE-LEU-273</scope>
    </reference>
    <reference key="33">
        <citation type="journal article" date="2008" name="J. Biol. Chem." volume="283" first="36118" last="36131">
            <title>Hda monomerization by ADP binding promotes replicase clamp-mediated DnaA-ATP hydrolysis.</title>
            <authorList>
                <person name="Su'etsugu M."/>
                <person name="Nakamura K."/>
                <person name="Keyamura K."/>
                <person name="Kudo Y."/>
                <person name="Katayama T."/>
            </authorList>
            <dbReference type="PubMed" id="18977760"/>
            <dbReference type="DOI" id="10.1074/jbc.M803158200"/>
        </citation>
        <scope>IDENTIFICATION IN RIDA COMPLEX</scope>
    </reference>
    <reference evidence="11 12 13" key="34">
        <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="11116" last="11121">
            <title>Structure of a small-molecule inhibitor of a DNA polymerase sliding clamp.</title>
            <authorList>
                <person name="Georgescu R.E."/>
                <person name="Yurieva O."/>
                <person name="Kim S.S."/>
                <person name="Kuriyan J."/>
                <person name="Kong X.P."/>
                <person name="O'Donnell M."/>
            </authorList>
            <dbReference type="PubMed" id="18678908"/>
            <dbReference type="DOI" id="10.1073/pnas.0804754105"/>
        </citation>
        <scope>X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) IN COMPLEX WITH VARIOUS PEPTIDES</scope>
        <scope>SUBUNIT</scope>
        <scope>BIOTECHNOLOGY</scope>
    </reference>
    <reference key="35">
        <citation type="journal article" date="2009" name="Mol. Cell" volume="36" first="845" last="860">
            <title>Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli.</title>
            <authorList>
                <person name="Davies B.W."/>
                <person name="Kohanski M.A."/>
                <person name="Simmons L.A."/>
                <person name="Winkler J.A."/>
                <person name="Collins J.J."/>
                <person name="Walker G.C."/>
            </authorList>
            <dbReference type="PubMed" id="20005847"/>
            <dbReference type="DOI" id="10.1016/j.molcel.2009.11.024"/>
        </citation>
        <scope>INDUCTION BY HYDROXYUREA</scope>
        <source>
            <strain>K12 / MC4100 / ATCC 35695 / DSM 6574</strain>
        </source>
    </reference>
    <reference key="36">
        <citation type="journal article" date="2010" name="Science" volume="328" first="498" last="501">
            <title>Stoichiometry and architecture of active DNA replication machinery in Escherichia coli.</title>
            <authorList>
                <person name="Reyes-Lamothe R."/>
                <person name="Sherratt D.J."/>
                <person name="Leake M.C."/>
            </authorList>
            <dbReference type="PubMed" id="20413500"/>
            <dbReference type="DOI" id="10.1126/science.1185757"/>
        </citation>
        <scope>REPLISOME COMPLEX</scope>
        <scope>SUBUNIT</scope>
    </reference>
    <reference key="37">
        <citation type="journal article" date="2011" name="Nat. Struct. Mol. Biol." volume="19" first="113" last="116">
            <title>Single-molecule studies reveal the function of a third polymerase in the replisome.</title>
            <authorList>
                <person name="Georgescu R.E."/>
                <person name="Kurth I."/>
                <person name="O'Donnell M.E."/>
            </authorList>
            <dbReference type="PubMed" id="22157955"/>
            <dbReference type="DOI" id="10.1038/nsmb.2179"/>
        </citation>
        <scope>REPLISOME COMPLEX</scope>
        <scope>SUBUNIT</scope>
    </reference>
    <reference key="38">
        <citation type="journal article" date="2012" name="Mol. Microbiol." volume="85" first="648" last="668">
            <title>Evidence for roles of the Escherichia coli Hda protein beyond regulatory inactivation of DnaA.</title>
            <authorList>
                <person name="Baxter J.C."/>
                <person name="Sutton M.D."/>
            </authorList>
            <dbReference type="PubMed" id="22716942"/>
            <dbReference type="DOI" id="10.1111/j.1365-2958.2012.08129.x"/>
        </citation>
        <scope>FUNCTION IN REPLICATION FORK</scope>
        <scope>SUBUNIT</scope>
    </reference>
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            <title>A replicase clamp-binding dynamin-like protein promotes colocalization of nascent DNA strands and equipartitioning of chromosomes in E. coli.</title>
            <authorList>
                <person name="Ozaki S."/>
                <person name="Matsuda Y."/>
                <person name="Keyamura K."/>
                <person name="Kawakami H."/>
                <person name="Noguchi Y."/>
                <person name="Kasho K."/>
                <person name="Nagata K."/>
                <person name="Masuda T."/>
                <person name="Sakiyama Y."/>
                <person name="Katayama T."/>
            </authorList>
            <dbReference type="PubMed" id="23994470"/>
            <dbReference type="DOI" id="10.1016/j.celrep.2013.07.040"/>
        </citation>
        <scope>INTERACTION WITH CRFC</scope>
        <scope>SUBUNIT</scope>
        <scope>SUBCELLULAR LOCATION</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <reference evidence="14 15 16" key="40">
        <citation type="journal article" date="2015" name="Elife" volume="4" first="0" last="0">
            <title>cryo-EM structures of the E. coli replicative DNA polymerase reveal its dynamic interactions with the DNA sliding clamp, exonuclease and tau.</title>
            <authorList>
                <person name="Fernandez-Leiro R."/>
                <person name="Conrad J."/>
                <person name="Scheres S.H."/>
                <person name="Lamers M.H."/>
            </authorList>
            <dbReference type="PubMed" id="26499492"/>
            <dbReference type="DOI" id="10.7554/eLife.11134"/>
        </citation>
        <scope>STRUCTURE BY ELECTRON MICROSCOPY (7.30 ANGSTROMS) OF DNAE; DNAN; DNAQ; DNAX WITH AND WITHOUT DNA</scope>
        <scope>FUNCTION</scope>
        <scope>SUBUNIT</scope>
        <scope>DNA-BINDING</scope>
    </reference>
    <comment type="alternative products">
        <event type="alternative promoter"/>
        <isoform>
            <id>P0A988-1</id>
            <name evidence="2">Beta</name>
            <sequence type="displayed"/>
        </isoform>
        <isoform>
            <id>P0A988-2</id>
            <name evidence="2">Beta*</name>
            <sequence type="described" ref="VSP_059030"/>
        </isoform>
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    <comment type="miscellaneous">
        <text evidence="1 2">Beta* protein is expressed in late logarithmic/early stationary phase and induced by UV treatment (PubMed:8576210). Mutations in the Shine-Dalgarno region of beta* (some silent at the amino acid level) decrease production of beta* (PubMed:8576211).</text>
    </comment>
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        <source>
            <dbReference type="PDB" id="1JQL"/>
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    </evidence>
    <evidence type="ECO:0007744" key="6">
        <source>
            <dbReference type="PDB" id="1MMI"/>
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    </evidence>
    <evidence type="ECO:0007744" key="7">
        <source>
            <dbReference type="PDB" id="1OK7"/>
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        <source>
            <dbReference type="PDB" id="1UNN"/>
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    </evidence>
    <evidence type="ECO:0007744" key="9">
        <source>
            <dbReference type="PDB" id="2POL"/>
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    </evidence>
    <evidence type="ECO:0007744" key="10">
        <source>
            <dbReference type="PDB" id="3BEP"/>
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    </evidence>
    <evidence type="ECO:0007744" key="11">
        <source>
            <dbReference type="PDB" id="3D1E"/>
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    </evidence>
    <evidence type="ECO:0007744" key="12">
        <source>
            <dbReference type="PDB" id="3D1F"/>
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    </evidence>
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        <source>
            <dbReference type="PDB" id="3D1G"/>
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    </evidence>
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        <source>
            <dbReference type="PDB" id="5FKU"/>
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    </evidence>
    <evidence type="ECO:0007744" key="15">
        <source>
            <dbReference type="PDB" id="5FKV"/>
        </source>
    </evidence>
    <evidence type="ECO:0007744" key="16">
        <source>
            <dbReference type="PDB" id="5FKW"/>
        </source>
    </evidence>
    <sequence length="232" mass="25968" checksum="D70A75A4CC15CB43" modified="1988-04-01" version="1">MKRLIEATQFSMAHQDVRYYLNGMLFETEGEELRTVATDGHRLAVCSMPIGQSLPSHSVIVPRKGVIELMRMLDGGDNPLRVQIGSNNIRAHVGDFIFTSKLVDGRFPDYRRVLPKNPDKHLEAGCDLLKQAFARAAILSNEKFRGVRLYVSENQLKITANNPEQEEAEEILDVTYSGAEMEIGFNVSYVLDVLNALKCENVRMMLTDSVSSVQIEDAASQSAAYVVMPMRL</sequence>
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    <accession>P0DSH3-2</accession>
    <name>YIBX_ECOLI</name>
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        <recommendedName>
            <fullName evidence="1">Isoform Ybix-S of Protein YibX</fullName>
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    <gene>
        <name evidence="1" type="primary">yibX</name>
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    <organism>
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            <taxon>Bacteria</taxon>
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            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
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    </organism>
    <reference key="1">
        <citation type="journal article" date="1997" name="Science" volume="277" first="1453" last="1462">
            <title>The complete genome sequence of Escherichia coli K-12.</title>
            <authorList>
                <person name="Blattner F.R."/>
                <person name="Plunkett G.III."/>
                <person name="Bloch C.A."/>
                <person name="Perna N.T."/>
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            </authorList>
            <dbReference type="PubMed" id="9278503"/>
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        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <reference key="2">
        <citation type="journal article" date="2019" name="MBio" volume="10" first="0" last="0">
            <title>Identifying small proteins by ribosome profiling with stalled initiation complexes.</title>
            <authorList>
                <person name="Weaver J."/>
                <person name="Mohammad F."/>
                <person name="Buskirk A.R."/>
                <person name="Storz G."/>
            </authorList>
            <dbReference type="PubMed" id="30837344"/>
            <dbReference type="DOI" id="10.1128/mBio.02819-18"/>
        </citation>
        <scope>IDENTIFICATION</scope>
        <scope>PROBABLE ALTERNATIVE INITITATION OF YBIX-S</scope>
        <scope>INDUCTION</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <comment type="alternative products">
        <event type="alternative initiation"/>
        <isoform>
            <id>P0DSH3-2</id>
            <name>Ybix-S</name>
            <sequence type="described" ref="VSP_060150"/>
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        <isoform>
            <id>P0DSH3-1</id>
            <name>YbiX</name>
            <sequence type="displayed"/>
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    </comment>
    <dbReference type="Proteomes" id="UP000000625">
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    <evidence type="ECO:0000303" key="1">
        <source>
            <dbReference type="PubMed" id="30837344"/>
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    <sequence length="24" mass="2660" checksum="4C0A4A6D05D06DFA" modified="2019-05-08" version="1">MNIFKPISYIASLAPREVTLLALV</sequence>
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<entry dataset="Swiss-Prot" created="1990-04-01" modified="2022-08-03" version="181" xmlns="http://uniprot.org/uniprot">
    <accession>P15005-2</accession>
    <name>MCRB_ECOLI</name>
    <protein>
        <recommendedName>
            <fullName evidence="3">Isoform 33 kDa of Type IV methyl-directed restriction enzyme EcoKMcrB subunit</fullName>
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            <fullName>5-methylcytosine-specific restriction enzyme B</fullName>
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    <gene>
        <name type="primary">mcrB</name>
        <name type="synonym">rglB</name>
        <name type="ordered locus">b4346</name>
        <name type="ordered locus">JW5871</name>
    </gene>
    <organism>
        <name type="scientific">Escherichia coli (strain K12)</name>
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        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
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            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference key="1">
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            <title>Nucleotide sequence of the McrB region of Escherichia coli K-12 and evidence for two independent translational initiation sites at the mcrB locus.</title>
            <authorList>
                <person name="Ross T.K."/>
                <person name="Achberger E.C."/>
                <person name="Braymer H.D."/>
            </authorList>
            <dbReference type="PubMed" id="2649480"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
        <scope>ISOFORMS 33 KDA AND 51 KDA</scope>
        <scope>FUNCTION</scope>
        <scope>DISRUPTION PHENOTYPE</scope>
        <source>
            <strain>K12</strain>
        </source>
    </reference>
    <reference key="2">
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                <person name="Moran L."/>
                <person name="Slatko B."/>
                <person name="Raleigh E.A."/>
            </authorList>
            <dbReference type="PubMed" id="2203735"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
        <source>
            <strain>K12</strain>
        </source>
    </reference>
    <reference key="3">
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            <authorList>
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            </authorList>
            <dbReference type="PubMed" id="1312983"/>
            <dbReference type="DOI" id="10.1016/0378-1119(92)90308-C"/>
        </citation>
        <scope>PROTEIN SEQUENCE OF 1-10 AND 163-175</scope>
        <scope>ISOFORMS 33 KDA AND 51 KDA</scope>
        <source>
            <strain>K12</strain>
        </source>
    </reference>
    <reference key="4">
        <citation type="journal article" date="1995" name="EMBO J." volume="14" first="2661" last="2669">
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                <person name="Wild C."/>
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            </authorList>
            <dbReference type="PubMed" id="7781618"/>
        </citation>
        <scope>CHARACTERIZATION</scope>
    </reference>
    <reference key="5">
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            <title>Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes.</title>
            <authorList>
                <person name="Burland V.D."/>
                <person name="Plunkett G. III"/>
                <person name="Sofia H.J."/>
                <person name="Daniels D.L."/>
                <person name="Blattner F.R."/>
            </authorList>
            <dbReference type="PubMed" id="7610040"/>
            <dbReference type="DOI" id="10.1093/nar/23.12.2105"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <reference key="6">
        <citation type="journal article" date="1997" name="Science" volume="277" first="1453" last="1462">
            <title>The complete genome sequence of Escherichia coli K-12.</title>
            <authorList>
                <person name="Blattner F.R."/>
                <person name="Plunkett G.III."/>
                <person name="Bloch C.A."/>
                <person name="Perna N.T."/>
                <person name="Burland V."/>
                <person name="Riley M."/>
                <person name="Collado-Vides J."/>
                <person name="Glasner J.D."/>
                <person name="Rode C.K."/>
                <person name="Mayhew G.F."/>
                <person name="Gregor J."/>
                <person name="Davis N.W."/>
                <person name="Kirkpatrick H.A."/>
                <person name="Goeden M.A."/>
                <person name="Rose D.J."/>
                <person name="Mau B."/>
                <person name="Shao Y."/>
            </authorList>
            <dbReference type="PubMed" id="9278503"/>
            <dbReference type="DOI" id="10.1126/science.277.5331.1453"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <reference key="7">
        <citation type="journal article" date="2003" name="Nucleic Acids Res." volume="31" first="1805" last="1812">
            <title>A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes.</title>
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                <person name="Roberts R.J."/>
                <person name="Belfort M."/>
                <person name="Bestor T."/>
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                <person name="Bickle T.A."/>
                <person name="Bitinaite J."/>
                <person name="Blumenthal R.M."/>
                <person name="Degtyarev S.K."/>
                <person name="Dryden D.T."/>
                <person name="Dybvig K."/>
                <person name="Firman K."/>
                <person name="Gromova E.S."/>
                <person name="Gumport R.I."/>
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                <person name="Murray N.E."/>
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                <person name="Pingoud A."/>
                <person name="Raleigh E."/>
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            <dbReference type="PubMed" id="12654995"/>
            <dbReference type="DOI" id="10.1093/nar/gkg274"/>
        </citation>
        <scope>NOMENCLATURE</scope>
    </reference>
    <reference key="8">
        <citation type="journal article" date="2006" name="Mol. Syst. Biol." volume="2" first="E1" last="E5">
            <title>Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.</title>
            <authorList>
                <person name="Hayashi K."/>
                <person name="Morooka N."/>
                <person name="Yamamoto Y."/>
                <person name="Fujita K."/>
                <person name="Isono K."/>
                <person name="Choi S."/>
                <person name="Ohtsubo E."/>
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            <dbReference type="PubMed" id="16738553"/>
            <dbReference type="DOI" id="10.1038/msb4100049"/>
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        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / W3110 / ATCC 27325 / DSM 5911</strain>
        </source>
    </reference>
    <comment type="alternative products">
        <event type="alternative initiation"/>
        <isoform>
            <id>P15005-1</id>
            <name evidence="1">51 kDa</name>
            <sequence type="displayed"/>
        </isoform>
        <isoform>
            <id>P15005-2</id>
            <name evidence="1">33 kDa</name>
            <sequence type="described" ref="VSP_018868"/>
        </isoform>
        <text evidence="2">Both isoforms are expressed at the same level. A frameshift mutation within the codon for residue 58 prevents formation of the 51 kDa but not 33 kDa isoform.</text>
    </comment>
    <dbReference type="EC" id="3.1.21.-"/>
    <dbReference type="Proteomes" id="UP000000318">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <proteinExistence type="evidence at protein level"/>
    <feature type="initiator methionine" description="Removed" evidence="1">
        <location>
            <position position="1"/>
        </location>
    </feature>
    <evidence type="ECO:0000269" key="1">
        <source>
            <dbReference type="PubMed" id="1312983"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="2">
        <source>
            <dbReference type="PubMed" id="2649480"/>
        </source>
    </evidence>
    <evidence type="ECO:0000303" key="3">
        <source>
            <dbReference type="PubMed" id="12654995"/>
        </source>
    </evidence>
    <evidence type="ECO:0000303" key="4">
        <source>
            <dbReference type="PubMed" id="1312983"/>
        </source>
    </evidence>
    <sequence length="298" mass="34660" checksum="B05DE88C3CAB9321" modified="1998-12-15" version="3">MSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKAPQRVNMVQFHQSYSYEDFIQGYRPNGVGFRRKDGIFYNFCQQAKEQPEKKYIFIIDEINRANLSKVFGEVMMLMEHDKRGENWSVPLTYSENDEERFYVPENVYIIGLMNTADRSLAVVDYALRRRFSFIDIEPGFDTPQFRNFLLNKKAEPSFVESLCQKMNELNQEISKEATILGKGFRIGHSYFCCGLEDGTSPDTQWLNEIVMTDIAPLLEEYFFDDPYKQQKWTNKLLGDS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1986-07-21" modified="2022-08-03" version="153" xmlns="http://uniprot.org/uniprot">
    <accession>P63284-2</accession>
    <name>CLPB_ECOLI</name>
    <protein>
        <recommendedName>
            <fullName>Isoform ClpB-3 of Chaperone protein ClpB</fullName>
        </recommendedName>
        <alternativeName>
            <fullName>Heat shock protein F84.1</fullName>
        </alternativeName>
    </protein>
    <gene>
        <name type="primary">clpB</name>
        <name type="synonym">htpM</name>
        <name type="ordered locus">b2592</name>
        <name type="ordered locus">JW2573</name>
    </gene>
    <organism>
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference key="1">
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            <authorList>
                <person name="Shen W.-F."/>
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            </authorList>
            <dbReference type="PubMed" id="6285294"/>
            <dbReference type="DOI" id="10.1093/nar/10.10.3303"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 753-857</scope>
    </reference>
    <reference key="2">
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            </authorList>
            <dbReference type="PubMed" id="2185473"/>
            <dbReference type="DOI" id="10.1073/pnas.87.9.3513"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    </reference>
    <reference key="3">
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                <person name="Reichard P."/>
            </authorList>
            <dbReference type="PubMed" id="1953774"/>
            <dbReference type="DOI" id="10.1016/S0006-291X(05)81326-9"/>
        </citation>
        <scope>PROTEIN SEQUENCE OF 1-14; 150-157; 355-364 AND 452-460</scope>
    </reference>
    <reference key="4">
        <citation type="journal article" date="1991" name="J. Bacteriol." volume="173" first="4247" last="4253">
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            <authorList>
                <person name="Kitagawa M."/>
                <person name="Wada C."/>
                <person name="Yoshioka S."/>
                <person name="Yura T."/>
            </authorList>
            <dbReference type="PubMed" id="1906060"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-593</scope>
        <source>
            <strain>K12</strain>
        </source>
    </reference>
    <reference key="5">
        <citation type="journal article" date="1991" name="J. Bacteriol." volume="173" first="4254" last="4262">
            <title>ClpB is the Escherichia coli heat shock protein F84.1.</title>
            <authorList>
                <person name="Squires C.L."/>
                <person name="Pedersen S."/>
                <person name="Ross B.M."/>
                <person name="Squires C."/>
            </authorList>
            <dbReference type="PubMed" id="2066329"/>
        </citation>
        <scope>IDENTIFICATION AS A HEAT SHOCK PROTEIN</scope>
    </reference>
    <reference key="6">
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            <title>Site-directed mutagenesis of the dual translational initiation sites of the clpB gene of Escherichia coli and characterization of its gene products.</title>
            <authorList>
                <person name="Park S.K."/>
                <person name="Kim K.I."/>
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                <person name="Seol J.H."/>
                <person name="Tanaka K."/>
                <person name="Ichihara A."/>
                <person name="Ha D.B."/>
                <person name="Chung C.H."/>
            </authorList>
            <dbReference type="PubMed" id="8376377"/>
        </citation>
        <scope>ALTERNATIVE INITIATION</scope>
        <scope>ATPASE ACTIVITY</scope>
        <scope>SUBCELLULAR LOCATION</scope>
    </reference>
    <reference key="7">
        <citation type="submission" date="1996-02" db="EMBL/GenBank/DDBJ databases">
            <authorList>
                <person name="Ogura T."/>
                <person name="Tomoyasu T."/>
            </authorList>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31</scope>
        <source>
            <strain>K12 / W3110 / ATCC 27325 / DSM 5911</strain>
        </source>
    </reference>
    <reference key="8">
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                <person name="Horiuchi T."/>
            </authorList>
            <dbReference type="PubMed" id="9205837"/>
            <dbReference type="DOI" id="10.1093/dnares/4.2.91"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / W3110 / ATCC 27325 / DSM 5911</strain>
        </source>
    </reference>
    <reference key="9">
        <citation type="journal article" date="1997" name="Electrophoresis" volume="18" first="1243" last="1251">
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            <authorList>
                <person name="VanBogelen R.A."/>
                <person name="Abshire K.Z."/>
                <person name="Moldover B."/>
                <person name="Olson E.R."/>
                <person name="Neidhardt F.C."/>
            </authorList>
            <dbReference type="PubMed" id="9298644"/>
            <dbReference type="DOI" id="10.1002/elps.1150180805"/>
        </citation>
        <scope>IDENTIFICATION BY 2D-GEL</scope>
    </reference>
    <reference key="10">
        <citation type="journal article" date="1997" name="Science" volume="277" first="1453" last="1462">
            <title>The complete genome sequence of Escherichia coli K-12.</title>
            <authorList>
                <person name="Blattner F.R."/>
                <person name="Plunkett G.III."/>
                <person name="Bloch C.A."/>
                <person name="Perna N.T."/>
                <person name="Burland V."/>
                <person name="Riley M."/>
                <person name="Collado-Vides J."/>
                <person name="Glasner J.D."/>
                <person name="Rode C.K."/>
                <person name="Mayhew G.F."/>
                <person name="Gregor J."/>
                <person name="Davis N.W."/>
                <person name="Kirkpatrick H.A."/>
                <person name="Goeden M.A."/>
                <person name="Rose D.J."/>
                <person name="Mau B."/>
                <person name="Shao Y."/>
            </authorList>
            <dbReference type="PubMed" id="9278503"/>
            <dbReference type="DOI" id="10.1126/science.277.5331.1453"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <reference key="11">
        <citation type="journal article" date="2000" name="J. Biol. Chem." volume="275" first="37565" last="37571">
            <title>Structure and activity of ClpB from Escherichia coli. Role of the amino- and -carboxyl-terminal domains.</title>
            <authorList>
                <person name="Barnett M.E."/>
                <person name="Zolkiewska A."/>
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            </authorList>
            <dbReference type="PubMed" id="10982797"/>
            <dbReference type="DOI" id="10.1074/jbc.M005211200"/>
        </citation>
        <scope>FUNCTION OF DOMAINS</scope>
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        <citation type="journal article" date="2000" name="J. Mol. Biol." volume="303" first="655" last="666">
            <title>Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli.</title>
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                <person name="Kim K.I."/>
                <person name="Cheong G.-W."/>
                <person name="Park S.-C."/>
                <person name="Ha J.-S."/>
                <person name="Woo K.M."/>
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                <person name="Chung C.H."/>
            </authorList>
            <dbReference type="PubMed" id="11061966"/>
            <dbReference type="DOI" id="10.1006/jmbi.2000.4165"/>
        </citation>
        <scope>SUBUNIT</scope>
        <scope>MUTAGENESIS OF LYS-212 AND LYS-611</scope>
    </reference>
    <reference key="13">
        <citation type="journal article" date="2001" name="Acta Crystallogr. D" volume="57" first="1933" last="1935">
            <title>Cloning, expression, purification and preliminary X-ray crystallographic studies of Escherichia coli Hsp100 ClpB N-terminal domain.</title>
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                <person name="Sha B."/>
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            <dbReference type="PubMed" id="11717522"/>
            <dbReference type="DOI" id="10.1107/S0907444901017322"/>
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        <scope>CRYSTALLIZATION OF N-TERMINAL DOMAIN</scope>
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        <citation type="journal article" date="2002" name="Acta Crystallogr. D" volume="58" first="1030" last="1031">
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            <dbReference type="PubMed" id="12037306"/>
            <dbReference type="DOI" id="10.1107/S0907444902006327"/>
        </citation>
        <scope>CRYSTALLIZATION OF NBD2</scope>
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            <dbReference type="PubMed" id="12220194"/>
            <dbReference type="DOI" id="10.1021/bi026161s"/>
        </citation>
        <scope>MUTAGENESIS OF LYS-212; LYS-611; ASP-797; ARG-815; ARG-819 AND GLU-826</scope>
    </reference>
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            <dbReference type="PubMed" id="12054807"/>
            <dbReference type="DOI" id="10.1016/S0022-2836(02)00188-2"/>
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        <scope>X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 159-351</scope>
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    <reference key="17">
        <citation type="journal article" date="2002" name="J. Mol. Biol." volume="321" first="111" last="120">
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                <person name="Zolkiewski M."/>
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            <dbReference type="PubMed" id="12139937"/>
            <dbReference type="DOI" id="10.1016/S0022-2836(02)00591-0"/>
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        <scope>MUTAGENESIS OF THR-7; SER-84; ASP-103 AND GLU-109</scope>
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        <citation type="journal article" date="2003" name="Biochemistry" volume="42" first="14242" last="14248">
            <title>Structure and function of the middle domain of ClpB from Escherichia coli.</title>
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                <person name="Kedzierska S."/>
                <person name="Akoev V."/>
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                <person name="Zolkiewski M."/>
            </authorList>
            <dbReference type="PubMed" id="14640692"/>
            <dbReference type="DOI" id="10.1021/bi035573d"/>
        </citation>
        <scope>FUNCTION OF MIDDLE DOMAIN</scope>
    </reference>
    <reference key="19">
        <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="17615" last="17624">
            <title>Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity.</title>
            <authorList>
                <person name="Mogk A."/>
                <person name="Schlieker C."/>
                <person name="Strub C."/>
                <person name="Rist W."/>
                <person name="Weibezahn J."/>
                <person name="Bukau B."/>
            </authorList>
            <dbReference type="PubMed" id="12624113"/>
            <dbReference type="DOI" id="10.1074/jbc.M209686200"/>
        </citation>
        <scope>FUNCTION OF DOMAINS</scope>
        <scope>MUTAGENESIS OF LYS-212; GLU-279; ARG-332; TRP-543; LYS-611; GLU-678; ARG-756 AND 813-GLY--ARG-815</scope>
        <source>
            <strain>K12 / MC4100 / ATCC 35695 / DSM 6574</strain>
        </source>
    </reference>
    <reference key="20">
        <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="32608" last="32617">
            <title>Characterization of a trap mutant of the AAA+ chaperone ClpB.</title>
            <authorList>
                <person name="Weibezahn J."/>
                <person name="Schlieker C."/>
                <person name="Bukau B."/>
                <person name="Mogk A."/>
            </authorList>
            <dbReference type="PubMed" id="12805357"/>
            <dbReference type="DOI" id="10.1074/jbc.M303653200"/>
        </citation>
        <scope>BINDING TO PROTEIN AGGREGATES</scope>
        <scope>INTERACTION WITH DNAK</scope>
        <source>
            <strain>K12 / MC4100 / ATCC 35695 / DSM 6574</strain>
        </source>
    </reference>
    <reference key="21">
        <citation type="journal article" date="2003" name="Structure" volume="11" first="323" last="328">
            <title>Crystal structure of the E. coli Hsp100 ClpB N-terminal domain.</title>
            <authorList>
                <person name="Li J."/>
                <person name="Sha B."/>
            </authorList>
            <dbReference type="PubMed" id="12623019"/>
            <dbReference type="DOI" id="10.1016/S0969-2126(03)00030-3"/>
        </citation>
        <scope>X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 4-142</scope>
        <scope>MUTAGENESIS OF LEU-93; LEU-97 AND LEU-110</scope>
    </reference>
    <reference key="22">
        <citation type="journal article" date="2004" name="Nat. Struct. Mol. Biol." volume="11" first="607" last="615">
            <title>Substrate recognition by the AAA+ chaperone ClpB.</title>
            <authorList>
                <person name="Schlieker C."/>
                <person name="Weibezahn J."/>
                <person name="Patzelt H."/>
                <person name="Tessarz P."/>
                <person name="Strub C."/>
                <person name="Zeth K."/>
                <person name="Erbse A."/>
                <person name="Schneider-Mergener J."/>
                <person name="Chin J.W."/>
                <person name="Schultz P.G."/>
                <person name="Bukau B."/>
                <person name="Mogk A."/>
            </authorList>
            <dbReference type="PubMed" id="15208691"/>
            <dbReference type="DOI" id="10.1038/nsmb787"/>
        </citation>
        <scope>SUBSTRATE-BINDING</scope>
        <scope>MUTAGENESIS OF TYR-251; GLU-254 AND GLU-257</scope>
        <source>
            <strain>K12 / MC4100 / ATCC 35695 / DSM 6574</strain>
        </source>
    </reference>
    <reference key="23">
        <citation type="journal article" date="2004" name="Protein Sci." volume="13" first="567" last="574">
            <title>Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB.</title>
            <authorList>
                <person name="Akoev V."/>
                <person name="Gogol E.P."/>
                <person name="Barnett M.E."/>
                <person name="Zolkiewski M."/>
            </authorList>
            <dbReference type="PubMed" id="14978298"/>
            <dbReference type="DOI" id="10.1110/ps.03422604"/>
        </citation>
        <scope>OLIGOMERIZATION</scope>
        <scope>NUCLEOTIDE-BINDING</scope>
        <source>
            <strain>K12 / MC1000 / ATCC 39531</strain>
        </source>
    </reference>
    <reference key="24">
        <citation type="journal article" date="2006" name="Mol. Syst. Biol." volume="2" first="E1" last="E5">
            <title>Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.</title>
            <authorList>
                <person name="Hayashi K."/>
                <person name="Morooka N."/>
                <person name="Yamamoto Y."/>
                <person name="Fujita K."/>
                <person name="Isono K."/>
                <person name="Choi S."/>
                <person name="Ohtsubo E."/>
                <person name="Baba T."/>
                <person name="Wanner B.L."/>
                <person name="Mori H."/>
                <person name="Horiuchi T."/>
            </authorList>
            <dbReference type="PubMed" id="16738553"/>
            <dbReference type="DOI" id="10.1038/msb4100049"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / W3110 / ATCC 27325 / DSM 5911</strain>
        </source>
    </reference>
    <reference key="25">
        <citation type="journal article" date="2009" name="Mol. Cell. Proteomics" volume="8" first="215" last="225">
            <title>Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.</title>
            <authorList>
                <person name="Zhang J."/>
                <person name="Sprung R."/>
                <person name="Pei J."/>
                <person name="Tan X."/>
                <person name="Kim S."/>
                <person name="Zhu H."/>
                <person name="Liu C.F."/>
                <person name="Grishin N.V."/>
                <person name="Zhao Y."/>
            </authorList>
            <dbReference type="PubMed" id="18723842"/>
            <dbReference type="DOI" id="10.1074/mcp.M800187-MCP200"/>
        </citation>
        <scope>ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-96; LYS-176 AND LYS-640</scope>
        <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
        <source>
            <strain>K12 / JW1106</strain>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <comment type="alternative products">
        <event type="alternative initiation"/>
        <isoform>
            <id>P63284-1</id>
            <name>ClpB</name>
            <sequence type="displayed"/>
        </isoform>
        <isoform>
            <id>P63284-2</id>
            <name>ClpB-3</name>
            <sequence type="described" ref="VSP_018987 VSP_018703"/>
        </isoform>
    </comment>
    <comment type="miscellaneous">
        <text evidence="1">ClpB-3 ATPase activity is not activated by proteins, as it is in ClpB.</text>
    </comment>
    <dbReference type="Proteomes" id="UP000000318">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <proteinExistence type="evidence at protein level"/>
    <evidence type="ECO:0000305" key="1"/>
    <sequence length="709" mass="79870" checksum="60270862D6198B55" modified="2004-10-11" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-10-18" modified="2022-08-03" version="171" xmlns="http://uniprot.org/uniprot">
    <accession>P75960-2</accession>
    <name>NPD_ECOLI</name>
    <protein>
        <recommendedName>
            <fullName evidence="2">Isoform CobB-Short of NAD-dependent protein deacylase</fullName>
            <ecNumber evidence="2">2.3.1.286</ecNumber>
        </recommendedName>
        <alternativeName>
            <fullName evidence="2">Regulatory protein SIR2 homolog</fullName>
        </alternativeName>
    </protein>
    <gene>
        <name evidence="2" type="primary">cobB</name>
        <name type="synonym">ycfY</name>
        <name type="ordered locus">b1120</name>
        <name type="ordered locus">JW1106</name>
    </gene>
    <organism>
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference key="1">
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            <title>A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.</title>
            <authorList>
                <person name="Oshima T."/>
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                <person name="Baba T."/>
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            </authorList>
            <dbReference type="PubMed" id="8905232"/>
            <dbReference type="DOI" id="10.1093/dnares/3.3.137"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / W3110 / ATCC 27325 / DSM 5911</strain>
        </source>
    </reference>
    <reference key="2">
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            <authorList>
                <person name="Blattner F.R."/>
                <person name="Plunkett G.III."/>
                <person name="Bloch C.A."/>
                <person name="Perna N.T."/>
                <person name="Burland V."/>
                <person name="Riley M."/>
                <person name="Collado-Vides J."/>
                <person name="Glasner J.D."/>
                <person name="Rode C.K."/>
                <person name="Mayhew G.F."/>
                <person name="Gregor J."/>
                <person name="Davis N.W."/>
                <person name="Kirkpatrick H.A."/>
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            </authorList>
            <dbReference type="PubMed" id="9278503"/>
            <dbReference type="DOI" id="10.1126/science.277.5331.1453"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <reference key="3">
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            <title>Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity.</title>
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            </authorList>
            <dbReference type="PubMed" id="10381378"/>
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        </citation>
        <scope>WEAK ADP-RIBOSYLTRANSFERASE ACTIVITY</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <reference key="4">
        <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="5807" last="5811">
            <title>The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases.</title>
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                <person name="Landry J."/>
                <person name="Sutton A."/>
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            </authorList>
            <dbReference type="PubMed" id="10811920"/>
            <dbReference type="DOI" id="10.1073/pnas.110148297"/>
        </citation>
        <scope>FUNCTION</scope>
        <scope>CATALYTIC ACTIVITY</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <reference key="5">
        <citation type="journal article" date="2004" name="J. Mol. Biol." volume="337" first="731" last="741">
            <title>Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli.</title>
            <authorList>
                <person name="Zhao K."/>
                <person name="Chai X."/>
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            </authorList>
            <dbReference type="PubMed" id="15019790"/>
            <dbReference type="DOI" id="10.1016/j.jmb.2004.01.060"/>
        </citation>
        <scope>X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 40-274 IN COMPLEX WITH PEPTIDE SUBSTRATE AND ZINC</scope>
        <scope>CATALYTIC ACTIVITY</scope>
        <scope>FUNCTION</scope>
        <scope>SUBSTRATE</scope>
        <scope>INTERACTION WITH ACETYL-COA SYNTHETASE</scope>
        <scope>COFACTOR</scope>
    </reference>
    <reference key="6">
        <citation type="journal article" date="2006" name="Mol. Syst. Biol." volume="2" first="E1" last="E5">
            <title>Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.</title>
            <authorList>
                <person name="Hayashi K."/>
                <person name="Morooka N."/>
                <person name="Yamamoto Y."/>
                <person name="Fujita K."/>
                <person name="Isono K."/>
                <person name="Choi S."/>
                <person name="Ohtsubo E."/>
                <person name="Baba T."/>
                <person name="Wanner B.L."/>
                <person name="Mori H."/>
                <person name="Horiuchi T."/>
            </authorList>
            <dbReference type="PubMed" id="16738553"/>
            <dbReference type="DOI" id="10.1038/msb4100049"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / W3110 / ATCC 27325 / DSM 5911</strain>
        </source>
    </reference>
    <reference key="7">
        <citation type="journal article" date="2007" name="Proteomics" volume="7" first="1097" last="1106">
            <title>From the genome sequence to the proteome and back: evaluation of E. coli genome annotation with a 2-D gel-based proteomics approach.</title>
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                <person name="Maillet I."/>
                <person name="Berndt P."/>
                <person name="Malo C."/>
                <person name="Rodriguez S."/>
                <person name="Brunisholz R.A."/>
                <person name="Pragai Z."/>
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            <dbReference type="PubMed" id="17366475"/>
            <dbReference type="DOI" id="10.1002/pmic.200600599"/>
        </citation>
        <scope>DISCUSSION OF START SITE</scope>
        <source>
            <strain>K12 / JM109 / ATCC 53323</strain>
        </source>
    </reference>
    <reference key="8">
        <citation type="journal article" date="2013" name="Mol. Cell. Proteomics" volume="12" first="3509" last="3520">
            <title>Identification of lysine succinylation substrates and the succinylation regulatory enzyme CobB in E. coli.</title>
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                <person name="Colak G."/>
                <person name="Xie Z."/>
                <person name="Zhu A.Y."/>
                <person name="Dai L."/>
                <person name="Lu Z."/>
                <person name="Zhang Y."/>
                <person name="Wan X."/>
                <person name="Chen Y."/>
                <person name="Cha Y.H."/>
                <person name="Lin H."/>
                <person name="Zhao Y."/>
                <person name="Tan M."/>
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            <dbReference type="PubMed" id="24176774"/>
            <dbReference type="DOI" id="10.1074/mcp.M113.031567"/>
        </citation>
        <scope>FUNCTION AS A DEACETYLASE AND A DESUCCINYLASE</scope>
        <scope>CATALYTIC ACTIVITY</scope>
        <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
        <scope>DOMAIN</scope>
        <scope>MUTAGENESIS OF TYR-92 AND ARG-95</scope>
    </reference>
    <reference key="9">
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            <title>Protein lysine de-2-hydroxyisobutyrylation by CobB in prokaryotes.</title>
            <authorList>
                <person name="Dong H."/>
                <person name="Zhai G."/>
                <person name="Chen C."/>
                <person name="Bai X."/>
                <person name="Tian S."/>
                <person name="Hu D."/>
                <person name="Fan E."/>
                <person name="Zhang K."/>
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            <dbReference type="PubMed" id="31328167"/>
            <dbReference type="DOI" id="10.1126/sciadv.aaw6703"/>
        </citation>
        <scope>FUNCTION</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <comment type="alternative products">
        <event type="alternative promoter"/>
        <isoform>
            <id>P75960-1</id>
            <name evidence="1">CobB-Long</name>
            <sequence type="displayed"/>
        </isoform>
        <isoform>
            <id>P75960-2</id>
            <name evidence="1">CobB-Short</name>
            <sequence type="described" ref="VSP_058458"/>
        </isoform>
    </comment>
    <dbReference type="EC" id="2.3.1.286" evidence="2"/>
    <dbReference type="Proteomes" id="UP000000318">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <proteinExistence type="evidence at protein level"/>
    <evidence type="ECO:0000250" key="1">
        <source>
            <dbReference type="UniProtKB" id="P0A2F2"/>
        </source>
    </evidence>
    <evidence type="ECO:0000255" key="2">
        <source>
            <dbReference type="HAMAP-Rule" id="MF_01121"/>
        </source>
    </evidence>
    <sequence length="242" mass="26716" checksum="D4EEEBF856898698" modified="2016-09-07" version="3">MEKPRVLVLTGAGISAESGIRTFRAADGLWEEHRVEDVATPEGFDRDPELVQAFYNARRRQLQQPEIQPNAAHLALAKLQDALGDRFLLVTQNIDNLHERAGNTNVIHMHGELLKVRCSQSGQVLDWTGDVTPEDKCHCCQFPAPLRPHVVWFGEMPLGMDEIYMALSMADIFIAIGTSGHVYPAAGFVHEAKLHGAHTVELNLEPSQVGNEFAEKYYGPASQVVPEFVEKLLKGLKAGSIA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="187" xmlns="http://uniprot.org/uniprot">
    <accession>Q59385-2</accession>
    <name>COPA_ECOLI</name>
    <protein>
        <recommendedName>
            <fullName evidence="1">Isoform Soluble copper chaperone CopA(Z) of Copper-exporting P-type ATPase</fullName>
            <ecNumber evidence="4 5">7.2.2.8</ecNumber>
        </recommendedName>
        <alternativeName>
            <fullName>Copper-exporting P-type ATPase A</fullName>
        </alternativeName>
        <alternativeName>
            <fullName>Cu(+)-exporting ATPase</fullName>
        </alternativeName>
        <alternativeName>
            <fullName evidence="2">Soluble copper chaperone CopA(Z)</fullName>
        </alternativeName>
    </protein>
    <gene>
        <name evidence="1" type="primary">copA</name>
        <name evidence="3" type="synonym">atcU</name>
        <name type="synonym">f834</name>
        <name type="synonym">ybaR</name>
        <name type="ordered locus">b0484</name>
        <name type="ordered locus">JW0473</name>
    </gene>
    <organism>
        <name type="scientific">Escherichia coli (strain K12)</name>
        <dbReference type="NCBI Taxonomy" id="83333"/>
        <lineage>
            <taxon>Bacteria</taxon>
            <taxon>Proteobacteria</taxon>
            <taxon>Gammaproteobacteria</taxon>
            <taxon>Enterobacterales</taxon>
            <taxon>Enterobacteriaceae</taxon>
            <taxon>Escherichia</taxon>
        </lineage>
    </organism>
    <reference key="1">
        <citation type="submission" date="1996-06" db="EMBL/GenBank/DDBJ databases">
            <authorList>
                <person name="Das S."/>
                <person name="Chuang E."/>
                <person name="Vulpe C."/>
                <person name="Goldman J."/>
                <person name="Gitschier J."/>
            </authorList>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
        <source>
            <strain>K12</strain>
        </source>
    </reference>
    <reference key="2">
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                <person name="Plunkett G.III."/>
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            <dbReference type="PubMed" id="9278503"/>
            <dbReference type="DOI" id="10.1126/science.277.5331.1453"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <reference key="3">
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            <title>Sequence of minutes 4-25 of Escherichia coli.</title>
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                <person name="Allen E."/>
                <person name="Araujo R."/>
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            </authorList>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <reference key="4">
        <citation type="journal article" date="1998" name="FEMS Microbiol. Lett." volume="169" first="375" last="382">
            <title>Small genes/gene-products in Escherichia coli K-12.</title>
            <authorList>
                <person name="Wasinger V.C."/>
                <person name="Humphery-Smith I."/>
            </authorList>
            <dbReference type="PubMed" id="9868784"/>
            <dbReference type="DOI" id="10.1111/j.1574-6968.1998.tb13343.x"/>
        </citation>
        <scope>PROTEIN SEQUENCE OF 2-11</scope>
        <source>
            <strain>K12</strain>
        </source>
    </reference>
    <reference key="5">
        <citation type="journal article" date="2000" name="Gene" volume="261" first="289" last="298">
            <title>Control of copper homeostasis in Escherichia coli by a P-type ATPase, CopA, and a MerR-like transcriptional activator, CopR.</title>
            <authorList>
                <person name="Petersen C."/>
                <person name="Moeller L.B."/>
            </authorList>
            <dbReference type="PubMed" id="11167016"/>
            <dbReference type="DOI" id="10.1016/S0378-1119(00)00509-6"/>
        </citation>
        <scope>FUNCTION</scope>
        <scope>INDUCTION BY COPPER</scope>
        <scope>DISRUPTION PHENOTYPE</scope>
        <source>
            <strain>K12</strain>
        </source>
    </reference>
    <reference key="6">
        <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="652" last="656">
            <title>CopA: an Escherichia coli Cu(I)-translocating P-type ATPase.</title>
            <authorList>
                <person name="Rensing C."/>
                <person name="Fan B."/>
                <person name="Sharma R."/>
                <person name="Mitra B."/>
                <person name="Rosen B.P."/>
            </authorList>
            <dbReference type="PubMed" id="10639134"/>
            <dbReference type="DOI" id="10.1073/pnas.97.2.652"/>
        </citation>
        <scope>FUNCTION</scope>
        <scope>CATALYTIC ACTIVITY</scope>
        <scope>ACTIVITY REGULATION</scope>
        <scope>INDUCTION BY COPPER AND SILVER</scope>
        <scope>DISRUPTION PHENOTYPE</scope>
        <source>
            <strain>K12 / W3110 / ATCC 27325 / DSM 5911</strain>
            <strain>LMG194</strain>
        </source>
    </reference>
    <reference key="7">
        <citation type="journal article" date="2001" name="Biochem. Biophys. Res. Commun." volume="286" first="414" last="418">
            <title>Escherichia coli CopA N-terminal Cys(X)(2)Cys motifs are not required for copper resistance or transport.</title>
            <authorList>
                <person name="Fan B."/>
                <person name="Grass G."/>
                <person name="Rensing C."/>
                <person name="Rosen B.P."/>
            </authorList>
            <dbReference type="PubMed" id="11500054"/>
            <dbReference type="DOI" id="10.1006/bbrc.2001.5367"/>
        </citation>
        <scope>FUNCTION</scope>
        <scope>MOTIF</scope>
        <scope>MUTAGENESIS OF 8-THR--LEU-150; 14-CYS--CYS-17 AND 110-CYS--CYS-113</scope>
        <source>
            <strain>LMG194</strain>
        </source>
    </reference>
    <reference key="8">
        <citation type="journal article" date="2002" name="J. Biol. Chem." volume="277" first="46987" last="46992">
            <title>Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase.</title>
            <authorList>
                <person name="Fan B."/>
                <person name="Rosen B.P."/>
            </authorList>
            <dbReference type="PubMed" id="12351646"/>
            <dbReference type="DOI" id="10.1074/jbc.M208490200"/>
        </citation>
        <scope>FUNCTION IN TRANSPORT</scope>
        <scope>FUNCTION AS AN ATPASE</scope>
        <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
        <scope>ACTIVITY REGULATION</scope>
        <scope>PHOSPHORYLATION</scope>
        <scope>MUTAGENESIS OF 3-GLN--CYS-113; 7-LEU--GLU-54; 14-CYS--CYS-17; 110-CYS--CYS-113; CYS-479 AND CYS-481</scope>
        <source>
            <strain>LMG194</strain>
        </source>
    </reference>
    <reference key="9">
        <citation type="journal article" date="2003" name="FEBS Lett." volume="546" first="391" last="394">
            <title>Measurement of cytoplasmic copper, silver, and gold with a lux biosensor shows copper and silver, but not gold, efflux by the CopA ATPase of Escherichia coli.</title>
            <authorList>
                <person name="Stoyanov J.V."/>
                <person name="Magnani D."/>
                <person name="Solioz M."/>
            </authorList>
            <dbReference type="PubMed" id="12832075"/>
            <dbReference type="DOI" id="10.1016/S0014-5793(03)00640-9"/>
        </citation>
        <scope>FUNCTION IN SILVER EXPORT</scope>
        <scope>DISRUPTION PHENOTYPE</scope>
        <source>
            <strain>K12 / W3110 / ATCC 27325 / DSM 5911</strain>
        </source>
    </reference>
    <reference key="10">
        <citation type="journal article" date="2005" name="Science" volume="308" first="1321" last="1323">
            <title>Global topology analysis of the Escherichia coli inner membrane proteome.</title>
            <authorList>
                <person name="Daley D.O."/>
                <person name="Rapp M."/>
                <person name="Granseth E."/>
                <person name="Melen K."/>
                <person name="Drew D."/>
                <person name="von Heijne G."/>
            </authorList>
            <dbReference type="PubMed" id="15919996"/>
            <dbReference type="DOI" id="10.1126/science.1109730"/>
        </citation>
        <scope>SUBCELLULAR LOCATION</scope>
        <scope>TOPOLOGY [LARGE SCALE ANALYSIS]</scope>
        <source>
            <strain>K12 / MG1655 / ATCC 47076</strain>
        </source>
    </reference>
    <reference key="11">
        <citation type="journal article" date="2006" name="Mol. Syst. Biol." volume="2" first="E1" last="E5">
            <title>Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.</title>
            <authorList>
                <person name="Hayashi K."/>
                <person name="Morooka N."/>
                <person name="Yamamoto Y."/>
                <person name="Fujita K."/>
                <person name="Isono K."/>
                <person name="Choi S."/>
                <person name="Ohtsubo E."/>
                <person name="Baba T."/>
                <person name="Wanner B.L."/>
                <person name="Mori H."/>
                <person name="Horiuchi T."/>
            </authorList>
            <dbReference type="PubMed" id="16738553"/>
            <dbReference type="DOI" id="10.1038/msb4100049"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain>K12 / W3110 / ATCC 27325 / DSM 5911</strain>
        </source>
    </reference>
    <reference key="12">
        <citation type="journal article" date="2014" name="J. Biol. Chem." volume="289" first="20492" last="20501">
            <title>Mechanism of ATPase-mediated Cu+ export and delivery to periplasmic chaperones: the interaction of Escherichia coli CopA and CusF.</title>
            <authorList>
                <person name="Padilla-Benavides T."/>
                <person name="George Thompson A.M."/>
                <person name="McEvoy M.M."/>
                <person name="Argueello J.M."/>
            </authorList>
            <dbReference type="PubMed" id="24917681"/>
            <dbReference type="DOI" id="10.1074/jbc.M114.577668"/>
        </citation>
        <scope>FUNCTION AS AN ATPASE</scope>
        <scope>FUNCTION IN TRANSFER TO CUSF</scope>
        <scope>CATALYTIC ACTIVITY</scope>
        <scope>REACTION MECHANISM</scope>
        <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
        <scope>COPPER-BINDING</scope>
        <scope>SUBUNIT</scope>
        <scope>DOMAIN</scope>
        <scope>TOPOLOGY</scope>
        <scope>MUTAGENESIS OF MET-204; 207-ASP--MET-210; 212-THR--ARG-216; 273-TRP--PHE-277; 279-MET--HIS-283; GLU-287 AND 797-TRP--THR-802</scope>
    </reference>
    <reference key="13">
        <citation type="journal article" date="2015" name="Mol. Microbiol." volume="97" first="423" last="438">
            <title>Distinct functions of serial metal-binding domains in the Escherichia coli P1 B-ATPase CopA.</title>
            <authorList>
                <person name="Drees S.L."/>
                <person name="Beyer D.F."/>
                <person name="Lenders-Lomscher C."/>
                <person name="Luebben M."/>
            </authorList>
            <dbReference type="PubMed" id="25899340"/>
            <dbReference type="DOI" id="10.1111/mmi.13038"/>
        </citation>
        <scope>FUNCTION AS AN ATPASE</scope>
        <scope>POSSIBLE CHAPERONE FUNCTION</scope>
        <scope>ACTIVITY REGULATION</scope>
        <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
        <scope>DOMAIN</scope>
        <scope>MUTAGENESIS OF 1-MET--ALA-70; 14-CYS--CYS-17 AND 110-CYS--CYS-113</scope>
        <source>
            <strain>LMG194</strain>
        </source>
    </reference>
    <reference key="14">
        <citation type="journal article" date="2017" name="Mol. Cell" volume="65" first="207" last="219">
            <title>Programmed ribosomal frameshifting generates a copper transporter and a copper chaperone from the same gene.</title>
            <authorList>
                <person name="Meydan S."/>
                <person name="Klepacki D."/>
                <person name="Karthikeyan S."/>
                <person name="Margus T."/>
                <person name="Thomas P."/>
                <person name="Jones J.E."/>
                <person name="Khan Y."/>
                <person name="Briggs J."/>
                <person name="Dinman J.D."/>
                <person name="Vazquez-Laslop N."/>
                <person name="Mankin A.S."/>
            </authorList>
            <dbReference type="PubMed" id="28107647"/>
            <dbReference type="DOI" id="10.1016/j.molcel.2016.12.008"/>
        </citation>
        <scope>RIBOSOMAL FRAMESHIFT TO TRANSLATE ISOFORM SOLUBLE COPPER CHAPERONE COPA(Z)</scope>
        <scope>FUNCTION AS A COPPER CHAPERONE</scope>
    </reference>
    <comment type="alternative products">
        <event type="ribosomal frameshifting"/>
        <isoform>
            <id>Q59385-2</id>
            <name>Soluble copper chaperone CopA(Z)</name>
            <sequence type="described" ref="VSP_059176"/>
        </isoform>
        <isoform>
            <id>Q59385-1</id>
            <name>Copper-exporting P-type ATPase</name>
            <sequence type="displayed"/>
        </isoform>
    </comment>
    <dbReference type="EC" id="7.2.2.8" evidence="4 5"/>
    <dbReference type="Proteomes" id="UP000000318">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <dbReference type="Proteomes" id="UP000000625">
        <property type="component" value="Chromosome"/>
    </dbReference>
    <proteinExistence type="evidence at protein level"/>
    <evidence type="ECO:0000303" key="1">
        <source>
            <dbReference type="PubMed" id="10639134"/>
        </source>
    </evidence>
    <evidence type="ECO:0000303" key="2">
        <source>
            <dbReference type="PubMed" id="28107647"/>
        </source>
    </evidence>
    <evidence type="ECO:0000303" key="3">
        <source>
            <dbReference type="PubMed" id="9868784"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="4">
        <source>
            <dbReference type="PubMed" id="10639134"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="5">
        <source>
            <dbReference type="PubMed" id="24917681"/>
        </source>
    </evidence>
    <sequence length="70" mass="7481" checksum="F0370BB67BCFDC7A" modified="2007-01-23" version="4">MSQTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVTGTASAEQLIETIKQAGYDASVSHPKG</sequence>
</entry>
<copyright>
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms Distributed under the Creative Commons Attribution (CC BY 4.0) License
</copyright>
</uniprot>