MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint anonymous-2014q-2 Subunit CydX of Escherichia coli cytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site in vitro In vitro affinity techniques affinity technology affinity techniques ms participant Identification by mass spectrometry ms participant friedrich@bio.chemie.uni-freiburg.de 2014 imex curation Hoeser J., Hong S., Gehmann G., Gennis R.B., Friedrich T. FEBS Lett. (0014-5793) Only protein-protein interactions anonymous-2014v-1 Subunit CydX of Escherichia coli cytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column ms participant Identification by mass spectrometry ms participant friedrich@bio.chemie.uni-freiburg.de 2014 imex curation Hoeser J., Hong S., Gehmann G., Gennis R.B., Friedrich T. FEBS Lett. (0014-5793) Only protein-protein interactions cydb_ecoli Cytochrome bd-I ubiquinol oxidase subunit 2 cydB cyd-2 b0734 JW0723 Cytochrome d ubiquinol oxidase subunit II Cytochrome bd-I oxidase subunit II protein protein ecoli Escherichia coli (strain K12) MIDYEVLRFIWWLLVGVLLIGFAVTDGFDMGVGMLTRFLGRNDTERRIMINSIAPHWDGNQVWLITAGGALFAAWPMVYAAAFSGFYVAMILVLASLFFRPVGFDYRSKIEETRWRNMWDWGIFIGSFVPPLVIGVAFGNLLQGVPFNVDEYLRLYYTGNFFQLLNPFGLLAGVVSVGMIITQGATYLQMRTVGELHLRTRATAQVAALVTLVCFALAGVWVMYGIDGYVVKSTMDHYAASNPLNKEVVREAGAWLVNFNNTPILWAIPALGVVLPLLTILTARMDKAAWAFVFSSLTLACIILTAGIAMFPFVMPSSTMMNASLTMWDATSSQLTLNVMTWVAVVLVPIILLYTAWCYWKMFGRITKEDIERNTHSLY cyda_ecoli Cytochrome bd-I ubiquinol oxidase subunit 1 cydA cyd-1 b0733 Cytochrome d ubiquinol oxidase subunit I Cytochrome bd-I oxidase subunit I JW0722 protein protein ecoli Escherichia coli (strain K12) MLDIVELSRLQFALTAMYHFLFVPLTLGMAFLLAIMETVYVLSGKQIYKDMTKFWGKLFGINFALGVATGLTMEFQFGTNWSYYSHYVGDIFGAPLAIEGLMAFFLESTFVGLFFFGWDRLGKVQHMCVTWLVALGSNLSALWILVANGWMQNPIASDFNFETMRMEMVSFSELVLNPVAQVKFVHTVASGYVTGAMFILGISAWYMLKGRDFAFAKRSFAIAASFGMAAVLSVIVLGDESGYEMGDVQKTKLAAIEAEWETQPAPAAFTLFGIPDQEEETNKFAIQIPYALGIIATRSVDTPVIGLKELMVQHEERIRNGMKAYSLLEQLRSGSTDQAVRDQFNSMKKDLGYGLLLKRYTPNVADATEAQIQQATKDSIPRVAPLYFAFRIMVACGFLLLAIIALSFWSVIRNRIGEKKWLLRAALYGIPLPWIAVEAGWFVAEYGRQPWAIGEVLPTAVANSSLTAGDLIFSMVLICGLYTLFLVAELFLMFKFARLGPSSLKTGRYHFEQSSTTTQPAR cydx_ecoli Cytochrome bd-I ubiquinol oxidase subunit X cydX Cytochrome bd-I oxidase subunit X Cytochrome d ubiquinol oxidase subunit X ybgT JW0724 b4515 protein protein ecoli Escherichia coli (strain K12) MWYFAWILGTLLACSFGVITALALEHVESGKAGQEDI cyda-cydb-1 1521185 n/a cydB 1521187 ms participant Identification by mass spectrometry ms participant unspecified role unspecified role prey prey subcellular prep subcellular preparation subcellular prep over-expressed over expressed level over-expressed n/a cydA 1521188 ms participant Identification by mass spectrometry ms participant unspecified role unspecified role bait bait subcellular prep subcellular preparation subcellular prep over-expressed over expressed level over-expressed his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false association association false false false f1 sf1 The gel of the preparation of the bd oxidase from strain CBO/pET28 cydAhisBX obtained by affinity- and size-exclusion chromatography showed two major bands at approximately 54 and 30 kDa. Mass spectrometric analysis revealed that the 54 kDa band corresponds to CydA (sequence coverage: 37%, overall score: 9865) and the 30 kDa to CydB (sequence coverage: 11%, overall score: 3576). The relatively low sequence coverage is typical for membrane proteins. No band with an apparent molecular mass of 4 kDa was detectable in the CBB-stained gel. However, silver staining revealed the presence of several other bands (Fig. 1). Bands from hydrophobic proteins, degradation products of CydA and CydB, were detected at about 20 and 8 kDa. Most interestingly, only the preparation of the bd oxidase from strain CBO/pET28 cydAhisBX showed an additional band at approximately 5 kDa (Fig. 1). This band corresponds to CydX as revealed by mass spectrometry (sequence coverage: 67%, overall score: 724). cyda-cydb-1 1521185 n/a cydX 1521189 ms participant Identification by mass spectrometry ms participant unspecified role unspecified role prey prey subcellular prep subcellular preparation subcellular prep over-expressed over expressed level over-expressed n/a cydB 1521187 ms participant Identification by mass spectrometry ms participant unspecified role unspecified role prey prey subcellular prep subcellular preparation subcellular prep over-expressed over expressed level over-expressed n/a cydA 1521188 ms participant Identification by mass spectrometry ms participant unspecified role unspecified role bait bait subcellular prep subcellular preparation subcellular prep over-expressed over expressed level over-expressed his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false association association false false false f1 sf2 The gel of the preparation of the bd oxidase from strain CBO/pET28 cydAhisBX obtained by affinity- and size-exclusion chromatography showed two major bands at approximately 54 and 30 kDa. Mass spectrometric analysis revealed that the 54 kDa band corresponds to CydA (sequence coverage: 37%, overall score: 9865) and the 30 kDa to CydB (sequence coverage: 11%, overall score: 3576). The relatively low sequence coverage is typical for membrane proteins. No band with an apparent molecular mass of 4 kDa was detectable in the CBB-stained gel. However, silver staining revealed the presence of several other bands (Fig. 1). Bands from hydrophobic proteins, degradation products of CydA and CydB, were detected at about 20 and 8 kDa. Most interestingly, only the preparation of the bd oxidase from strain CBO/pET28 cydAhisBX showed an additional band at approximately 5 kDa (Fig. 1). This band corresponds to CydX as revealed by mass spectrometry (sequence coverage: 67%, overall score: 724). cydx-cyda 1521185 n/a cydX 1521189 predetermined predetermined participant predetermined unspecified role unspecified role bait bait subcellular prep subcellular preparation subcellular prep over-expressed over expressed level over-expressed strep tag strep tag strep tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false n/a cydA 1521188 ms participant Identification by mass spectrometry ms participant unspecified role unspecified role prey prey subcellular prep subcellular preparation subcellular prep over-expressed over expressed level over-expressed n/a cydB 1521187 ms participant Identification by mass spectrometry ms participant unspecified role unspecified role prey prey subcellular prep subcellular preparation subcellular prep over-expressed over expressed level over-expressed association association false false false f3a The gel of the preparation of the bd oxidase from strain CBO/pET28 cydAhisBX obtained by affinity- and size-exclusion chromatography showed two major bands at approximately 54 and 30 kDa. Mass spectrometric analysis revealed that the 54 kDa band corresponds to CydA (sequence coverage: 37%, overall score: 9865) and the 30 kDa to CydB (sequence coverage: 11%, overall score: 3576). The relatively low sequence coverage is typical for membrane proteins. No band with an apparent molecular mass of 4 kDa was detectable in the CBB-stained gel. However, silver staining revealed the presence of several other bands (Fig. 1). Bands from hydrophobic proteins, degradation products of CydA and CydB, were detected at about 20 and 8 kDa. Most interestingly, only the preparation of the bd oxidase from strain CBO/pET28 cydAhisBX showed an additional band at approximately 5 kDa (Fig. 1). This band corresponds to CydX as revealed by mass spectrometry (sequence coverage: 67%, overall score: 724). cyda-cydb-2 1521186 n/a cydX 1521189 ms participant Identification by mass spectrometry ms participant unspecified role unspecified role neutral component neutral component subcellular prep subcellular preparation subcellular prep n/a cydA 1521188 ms participant Identification by mass spectrometry ms participant unspecified role unspecified role neutral component neutral component subcellular prep subcellular preparation subcellular prep over-expressed over expressed level over-expressed his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false n/a cydB 1521187 ms participant Identification by mass spectrometry ms participant unspecified role unspecified role neutral component neutral component subcellular prep subcellular preparation subcellular prep over-expressed over expressed level over-expressed physical association physical association false false false f1 sf2 The gel of the preparation of the bd oxidase from strain CBO/pET28 cydAhisBX obtained by affinity- and size-exclusion chromatography showed two major bands at approximately 54 and 30 kDa. Mass spectrometric analysis revealed that the 54 kDa band corresponds to CydA (sequence coverage: 37%, overall score: 9865) and the 30 kDa to CydB (sequence coverage: 11%, overall score: 3576). The relatively low sequence coverage is typical for membrane proteins. No band with an apparent molecular mass of 4 kDa was detectable in the CBB-stained gel. However, silver staining revealed the presence of several other bands (Fig. 1). Bands from hydrophobic proteins, degradation products of CydA and CydB, were detected at about 20 and 8 kDa. Most interestingly, only the preparation of the bd oxidase from strain CBO/pET28 cydAhisBX showed an additional band at approximately 5 kDa (Fig. 1). This band corresponds to CydX as revealed by mass spectrometry (sequence coverage: 67%, overall score: 724). cyda-cydb-1 1521186 n/a cydB 1521187 ms participant Identification by mass spectrometry ms participant unspecified role unspecified role neutral component neutral component subcellular prep subcellular preparation subcellular prep over-expressed over expressed level over-expressed n/a cydA 1521188 ms participant Identification by mass spectrometry ms participant unspecified role unspecified role neutral component neutral component subcellular prep subcellular preparation subcellular prep over-expressed over expressed level over-expressed his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false association association false false false f1 sf2 The gel of the preparation of the bd oxidase from strain CBO/pET28 cydAhisBX obtained by affinity- and size-exclusion chromatography showed two major bands at approximately 54 and 30 kDa. Mass spectrometric analysis revealed that the 54 kDa band corresponds to CydA (sequence coverage: 37%, overall score: 9865) and the 30 kDa to CydB (sequence coverage: 11%, overall score: 3576). The relatively low sequence coverage is typical for membrane proteins. No band with an apparent molecular mass of 4 kDa was detectable in the CBB-stained gel. However, silver staining revealed the presence of several other bands (Fig. 1). Bands from hydrophobic proteins, degradation products of CydA and CydB, were detected at about 20 and 8 kDa. Most interestingly, only the preparation of the bd oxidase from strain CBO/pET28 cydAhisBX showed an additional band at approximately 5 kDa (Fig. 1). This band corresponds to CydX as revealed by mass spectrometry (sequence coverage: 67%, overall score: 724).