#ID(s) interactor A	ID(s) interactor B	Alt. ID(s) interactor A	Alt. ID(s) interactor B	Alias(es) interactor A	Alias(es) interactor B	Interaction detection method(s)	Publication 1st author(s)	Publication Identifier(s)	Taxid interactor A	Taxid interactor B	Interaction type(s)	Source database(s)	Interaction identifier(s)	Confidence value(s)	Expansion method(s)	Biological role(s) interactor A	Biological role(s) interactor B	Experimental role(s) interactor A	Experimental role(s) interactor B	Type(s) interactor A	Type(s) interactor B	Xref(s) interactor A	Xref(s) interactor B	Interaction Xref(s)	Annotation(s) interactor A	Annotation(s) interactor B	Interaction annotation(s)	Host organism(s)	Interaction parameter(s)	Creation date	Update date	Checksum(s) interactor A	Checksum(s) interactor B	Interaction Checksum(s)	Negative	Feature(s) interactor A	Feature(s) interactor B	Stoichiometry(s) interactor A	Stoichiometry(s) interactor B	Identification method participant A	Identification method participant B
uniprotkb:P13423	uniprotkb:P15917	intact:EBI-456868|uniprotkb:Q937W2|uniprotkb:Q937W3|uniprotkb:Q9F5R7|uniprotkb:Q9KH69|uniprotkb:Q9RQU2|ensemblbacteria:AAT28905	intact:EBI-456923|uniprotkb:Q8KYJ6|uniprotkb:Q933F6|ensemblbacteria:AAT28913	psi-mi:pag_bacan(display_long)|uniprotkb:PA-83(gene name synonym)|uniprotkb:Anthrax toxins translocating protein(gene name synonym)|uniprotkb:pagA(gene name)|psi-mi:pagA(display_short)|uniprotkb:pag(gene name synonym)|uniprotkb:pXO1-110(locus name)|uniprotkb:BXA0164(locus name)|uniprotkb:GBAA_pXO1_0164(locus name)	psi-mi:lef_bacan(display_long)|uniprotkb:Anthrax lethal toxin endopeptidase component(gene name synonym)|uniprotkb:lef(gene name)|psi-mi:lef(display_short)|uniprotkb:pXO1-107(locus name)|uniprotkb:BXA0172(locus name)|uniprotkb:GBAA_pXO1_0172(locus name)	psi-mi:"MI:0069"(mass spectrometry studies of complexes)	Melnyk et al. (2006)	pubmed:16293620|imex:IM-19353	taxid:1392(bacan)|taxid:1392(Bacillus anthracis)	taxid:1392(bacan)|taxid:1392(Bacillus anthracis)	psi-mi:"MI:0915"(physical association)	psi-mi:"MI:0469"(IntAct)	intact:EBI-980670|imex:IM-19353-1	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_052806.1|refseq:WP_000746488.1|ensemblbacteria:AAT28905(transcript)|ensemblbacteria:GBAA_pXO1_0164(gene)|go:"GO:0005509"(calcium ion binding)|go:"GO:0005576"(extracellular region)|go:"GO:0015267"(channel activity)|go:"GO:0016021"(integral component of membrane)|go:"GO:0020002"(host cell plasma membrane)|go:"GO:0042802"(identical protein binding)|go:"GO:0043409"(negative regulation of MAPK cascade)|go:"GO:0044164"(host cell cytosol)|go:"GO:0044175"(host cell endosome membrane)|go:"GO:0044533"(positive regulation of apoptotic process in another organism)|go:"GO:0046872"(metal ion binding)|go:"GO:0051260"(protein homooligomerization)|go:"GO:0051844"(translocation of peptides or proteins into symbiont)|go:"GO:0071806"(protein transmembrane transport)|go:"GO:0090729"(toxin activity)|interpro:IPR003896(Bacterial exotoxin B)|interpro:IPR011658(PA14)|interpro:IPR027439|refseq:WP_000746487.1|refseq:WP_000746486.1|dip:DIP-29841N|mint:P13423|rcsb pdb:3Q8B|rcsb pdb:3Q8C|rcsb pdb:3Q8E|rcsb pdb:3Q8F|rcsb pdb:3TEW|rcsb pdb:3TEX|rcsb pdb:3TEY|rcsb pdb:3TEZ|rcsb pdb:4EE2|rcsb pdb:4H2A|rcsb pdb:4NAM|rcsb pdb:5FR3|rcsb pdb:6PSN|rcsb pdb:6UJI|rcsb pdb:6UZB|rcsb pdb:6UZD|rcsb pdb:6UZE|rcsb pdb:6VRA|rcsb pdb:3Q8A|rcsb pdb:6WJJ|rcsb pdb:6ZXJ|interpro:IPR027441|interpro:IPR035088|interpro:IPR035331|interpro:IPR037149|interpro:IPR037524|rcsb pdb:1ACC|rcsb pdb:1T6B|rcsb pdb:1TX5|rcsb pdb:1TZN|rcsb pdb:1TZO|rcsb pdb:1V36|rcsb pdb:3ETB|rcsb pdb:3INO|rcsb pdb:3J9C|rcsb pdb:3KWV|rcsb pdb:3MHZ|rcsb pdb:6ZXL|rcsb pdb:7O85|reactome:R-HSA-5210891|rcsb pdb:6ZXK	refseq:NP_052803.1|refseq:WP_001022097.1|refseq:WP_010890024.1|dip:DIP-29871N|mint:P15917|ensemblbacteria:AAT28913(transcript)|ensemblbacteria:GBAA_pXO1_0172(gene)|go:"GO:0004222"(metalloendopeptidase activity)|go:"GO:0005576"(extracellular region)|go:"GO:0006508"(proteolysis)|go:"GO:0008237"(metallopeptidase activity)|go:"GO:0008270"(zinc ion binding)|go:"GO:0044164"(host cell cytosol)|go:"GO:0090729"(toxin activity)|interpro:IPR003541(Anthrax toxin, lethal/endema factor, N-terminal)|interpro:IPR014781(Anthrax toxin, lethal/endema factor, N- and C-terminal)|interpro:IPR015239(Anthrax toxin, lethal factor, central)|interpro:IPR024079|rcsb pdb:1J7N|rcsb pdb:1JKY|rcsb pdb:1PWP|rcsb pdb:1PWQ|rcsb pdb:1PWU|rcsb pdb:1PWV|rcsb pdb:1PWW|rcsb pdb:1YQY|rcsb pdb:1ZXV|rcsb pdb:2L0R|rcsb pdb:3KWV|rcsb pdb:4DV8|rcsb pdb:4PKQ|rcsb pdb:4PKR|rcsb pdb:4PKS|rcsb pdb:4PKT|rcsb pdb:4PKU|rcsb pdb:4PKV|rcsb pdb:4PKW|rcsb pdb:4WF6|rcsb pdb:4XM6|rcsb pdb:4XM7|rcsb pdb:4XM8|rcsb pdb:5D1S|rcsb pdb:5D1T|rcsb pdb:5D1U|rcsb pdb:6PSN|rcsb pdb:6WJJ|rcsb pdb:6ZXJ|rcsb pdb:6ZXK|rcsb pdb:6ZXL|reactome:R-HSA-5210891	-	-	-	caution:A paper describing the plasmid pET22b-PA indicates that PA is only 735 residues long but the Uniprot entry is 764 residues. This paper does not specify the length.|comment:"The plasmid pET22b-PA does not contain the sequence coding for the signal peptide. Thus the mutations described in the paper (asp512lys and lys199glu&arg468ala&arg470asp) are mapped to residues 29 residues later in the Uniprot entry."|comment:They first examined LFN bound to the heptameric pre-pore, but because of the inherent tendency of these complexes to aggregate at high concentrations, they turned to a dimeric formof PA as an alternative binding partner for LFN. When two mutated,oligomerization-deficient forms of PA are combined in the presence of LFN, a ternary complex is formed containing one molecule of each species.|comment:PA was activated by incubation with trypsin at a final trypsin.|comment:"Four discrete sites in LFN (i.e. residues 95�120, DX site 1; 137�147,  DX site 2; 177�189, DX site 3; and 223�235, DX site 4) became significantly more protected from solvent exchange in the presence of PA."|figure legend:2 and 3|comment:Mapping all of the binding-defective mutants onto the four sites on the structure of LFN revealed the breadth of the binding surface defined by residues in DX sites 2 and 3. The distance between the most distal bindingdefective mutants, Asp-182 on DX site 3 to Glu-135 on DX site 2, was seen to be 40 A.|comment:The mutations in LFN listed above are those the authors specify as causing a defect in binding, however, from Fig. 3 A it seems that some of the other mutations did cause a decrease in binding.|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2006/08/02	2014/10/16	rogid:xLr/ydN4I0qJ46G/8A3JfZqAbyE1392	rogid:HvuMhoQb9eCHIox5O6RIVFknPMc1392	intact-crc:DDBD8E26E7F78C17|rigid:yQkONnbu+JsZD96VDnfbI1JXzBg	false	sufficient binding region:30-764..764|mutation:541-541|mutation:228-228,497-497,499-499	mutation decreasing interaction:173-173|mutation decreasing interaction:176-176|35s radiolabel:?-?|mutation decreasing interaction:169-169|sufficient binding region:34-296|mutation decreasing interaction:139-139|mutation decreasing interaction:141-141|mutation decreasing interaction:168-168|mutation decreasing interaction:168-168|mutation decreasing interaction:169-169	2	1	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)