UniProtKB - P0A903 (BAMC_ECOLI)
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- BLAST>sp|P0A903|BAMC_ECOLI Outer membrane protein assembly factor BamC OS=Escherichia coli (strain K12) OX=83333 GN=bamC PE=1 SV=1 MAYSVQKSRLAKVAGVSLVLLLAACSSDSRYKRQVSGDEAYLEAAPLAELHAPAGMILPV TSGDYAIPVTNGSGAVGKALDIRPPAQPLALVSGARTQFTGDTASLLVENGRGNTLWPQV VSVLQAKNYTITQRDDAGQTLTTDWVQWNRLDEDEQYRGRYQISVKPQGYQQAVTVKLLN LEQAGKPVADAASMQRYSTEMMNVISAGLDKSATDAANAAQNRASTTMDVQSAADDTGLP MLVVRGPFNVVWQRLPAALEKVGMKVTDSTRSQGNMAVTYKPLSDSDWQELGASDPGLAS GDYKLQVGDLDNRSSLQFIDPKGHTLTQSQNDALVAVFQAAFSK
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Outer membrane protein assembly factor BamC
bamC
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Reconstitution of outer membrane protein assembly from purified components."
Hagan C.L., Kim S., Kahne D.
Science 328:890-892(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT. - Ref.11"The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of beta-barrel assembly."
Hagan C.L., Kahne D.
Biochemistry 50:7444-7446(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT. - Ref.12"BamE modulates the Escherichia coli beta-barrel assembly machine component BamA."
Rigel N.W., Schwalm J., Ricci D.P., Silhavy T.J.
J. Bacteriol. 194:1002-1008(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.18"Lateral opening in the intact beta-barrel assembly machinery captured by cryo-EM."
Iadanza M.G., Higgins A.J., Schiffrin B., Calabrese A.N., Brockwell D.J., Ashcroft A.E., Radford S.E., Ranson N.A.
Nat. Commun. 7:12865-12865(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS) OF 25-189 IN LATERAL OPEN BAM COMPLEX, FUNCTION, REACTION MECHANISM, SUBUNIT, MASS SPECTROMETRY, LIPIDATION. - Ref.19"Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins."
Han L., Zheng J., Wang Y., Yang X., Liu Y., Sun C., Cao B., Zhou H., Ni D., Lou J., Zhao Y., Huang Y.
Nat. Struct. Mol. Biol. 23:192-196(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.56 ANGSTROMS) OF 33-88 IN LATERAL CLOSED BAM COMPLEX, SUBUNIT, SUBCELLULAR LOCATION. - Ref.20"Structural basis of outer membrane protein insertion by the BAM complex."
Gu Y., Li H., Dong H., Zeng Y., Zhang Z., Paterson N.G., Stansfeld P.J., Wang Z., Zhang Y., Wang W., Dong C.
Nature 531:64-69(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN LATERAL CLOSED BAM COMPLEX AND LATERAL OPEN BAMACDE SUBCOMPLEX, SUBUNIT, SUBCELLULAR LOCATION. - Ref.21"The structure of the beta-barrel assembly machinery complex."
Bakelar J., Buchanan S.K., Noinaj N.
Science 351:180-186(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.39 ANGSTROMS) OF 25-344 OF LATERAL OPEN BAMACDE COMPLEX, SUBUNIT.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- Gram-negative-bacterium-type cell outer membrane assembly Source: EcoliWiki <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG10658-MONOMER |
Protein family/group databases
Transport Classification Database More...TCDBi | 1.B.33.1.3 the outer membrane protein insertion porin (bam complex) (ompip) family |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Outer membrane protein assembly factor BamCUniRule annotation<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:bamCUniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Synonyms:dapX, nlpB Ordered Locus Names:b2477, JW2462 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Escherichia coli (strain K12) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 83333 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Escherichia coli strain K12 genome database More...EcoGenei | EG10658 bamC |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
- Cell outer membrane UniRule annotation
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
3 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, SUBCELLULAR LOCATION. - Ref.19"Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins."
Han L., Zheng J., Wang Y., Yang X., Liu Y., Sun C., Cao B., Zhou H., Ni D., Lou J., Zhao Y., Huang Y.
Nat. Struct. Mol. Biol. 23:192-196(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.56 ANGSTROMS) OF 33-88 IN LATERAL CLOSED BAM COMPLEX, SUBUNIT, SUBCELLULAR LOCATION. - Ref.20"Structural basis of outer membrane protein insertion by the BAM complex."
Gu Y., Li H., Dong H., Zeng Y., Zhang Z., Paterson N.G., Stansfeld P.J., Wang Z., Zhang Y., Wang W., Dong C.
Nature 531:64-69(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN LATERAL CLOSED BAM COMPLEX AND LATERAL OPEN BAMACDE SUBCOMPLEX, SUBUNIT, SUBCELLULAR LOCATION.
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, SUBCELLULAR LOCATION. - Ref.18"Lateral opening in the intact beta-barrel assembly machinery captured by cryo-EM."
Iadanza M.G., Higgins A.J., Schiffrin B., Calabrese A.N., Brockwell D.J., Ashcroft A.E., Radford S.E., Ranson N.A.
Nat. Commun. 7:12865-12865(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS) OF 25-189 IN LATERAL OPEN BAM COMPLEX, FUNCTION, REACTION MECHANISM, SUBUNIT, MASS SPECTROMETRY, LIPIDATION.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti
- Bam protein complex Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cell surface Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell outer membrane, Membrane<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 24 | Add BLAST | 24 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000018027 | 25 – 344 | Outer membrane protein assembly factor BamCAdd BLAST | 320 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 25 | N-palmitoyl cysteineUniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi 1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 25 | S-diacylglycerol cysteineUniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi 1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Lipoprotein, PalmitateProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P0A903 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0A903 |
PRoteomics IDEntifications database More...PRIDEi | P0A903 |
2D gel databases
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P0A903 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli."
Wu T., Malinverni J., Ruiz N., Kim S., Silhavy T.J., Kahne D.
Cell 121:235-245(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.7"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, SUBCELLULAR LOCATION. - Ref.8"YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli."
Malinverni J.C., Werner J., Kim S., Sklar J.G., Kahne D., Misra R., Silhavy T.J.
Mol. Microbiol. 61:151-164(2006) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, INTERACTION WITH BAMD. - Ref.10"Reconstitution of outer membrane protein assembly from purified components."
Hagan C.L., Kim S., Kahne D.
Science 328:890-892(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT. - Ref.11"The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of beta-barrel assembly."
Hagan C.L., Kahne D.
Biochemistry 50:7444-7446(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT. - Ref.18"Lateral opening in the intact beta-barrel assembly machinery captured by cryo-EM."
Iadanza M.G., Higgins A.J., Schiffrin B., Calabrese A.N., Brockwell D.J., Ashcroft A.E., Radford S.E., Ranson N.A.
Nat. Commun. 7:12865-12865(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS) OF 25-189 IN LATERAL OPEN BAM COMPLEX, FUNCTION, REACTION MECHANISM, SUBUNIT, MASS SPECTROMETRY, LIPIDATION. - Ref.19"Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins."
Han L., Zheng J., Wang Y., Yang X., Liu Y., Sun C., Cao B., Zhou H., Ni D., Lou J., Zhao Y., Huang Y.
Nat. Struct. Mol. Biol. 23:192-196(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.56 ANGSTROMS) OF 33-88 IN LATERAL CLOSED BAM COMPLEX, SUBUNIT, SUBCELLULAR LOCATION. - Ref.20"Structural basis of outer membrane protein insertion by the BAM complex."
Gu Y., Li H., Dong H., Zeng Y., Zhang Z., Paterson N.G., Stansfeld P.J., Wang Z., Zhang Y., Wang W., Dong C.
Nature 531:64-69(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN LATERAL CLOSED BAM COMPLEX AND LATERAL OPEN BAMACDE SUBCOMPLEX, SUBUNIT, SUBCELLULAR LOCATION. - Ref.21"The structure of the beta-barrel assembly machinery complex."
Bakelar J., Buchanan S.K., Noinaj N.
Science 351:180-186(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.39 ANGSTROMS) OF 25-344 OF LATERAL OPEN BAMACDE COMPLEX, SUBUNIT.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| itself | 2 | EBI-1129043,EBI-1129043 | ||
| bamD | P0AC02 | 4 | EBI-1129043,EBI-1128087 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 4262898, 311 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-1923 Bam complex |
Database of interacting proteins More...DIPi | DIP-39898N |
Protein interaction database and analysis system More...IntActi | P0A903, 7 interactors |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_2643 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 30 – 33 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 37 – 39 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 40 – 43 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 77 – 79 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 96 – 100 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 103 – 108 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 109 – 112 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 116 – 126 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 131 – 135 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 136 – 138 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 140 – 143 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 146 – 148 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 153 – 155 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 157 – 168 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 171 – 183 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 186 – 188 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 191 – 208 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 230 – 234 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 235 – 237 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 240 – 246 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 248 – 261 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 264 – 270 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 271 – 273 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 275 – 280 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 285 – 291 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 300 – 310 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 313 – 319 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 321 – 323 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 328 – 344 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 17 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P0A903 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0A903 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P0A903 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Crystallographic analysis of the C-terminal domain of the Escherichia coli lipoprotein BamC."
Kim K.H., Aulakh S., Tan W., Paetzel M.
Acta Crystallogr. F 67:1350-1358(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 224-343, DOMAIN. - Ref.16"Crystal structure of beta-barrel assembly machinery BamCD protein complex."
Kim K.H., Aulakh S., Paetzel M.
J. Biol. Chem. 286:39116-39121(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 26-344, INTERACTION WITH BAMD, DOMAIN. - Ref.17"Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set."
Warner L.R., Varga K., Lange O.F., Baker S.L., Baker D., Sousa M.C., Pardi A.
J. Mol. Biol. 411:83-95(2011) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 101-344, DOMAIN. - Ref.18"Lateral opening in the intact beta-barrel assembly machinery captured by cryo-EM."
Iadanza M.G., Higgins A.J., Schiffrin B., Calabrese A.N., Brockwell D.J., Ashcroft A.E., Radford S.E., Ranson N.A.
Nat. Commun. 7:12865-12865(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS) OF 25-189 IN LATERAL OPEN BAM COMPLEX, FUNCTION, REACTION MECHANISM, SUBUNIT, MASS SPECTROMETRY, LIPIDATION. - Ref.19"Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins."
Han L., Zheng J., Wang Y., Yang X., Liu Y., Sun C., Cao B., Zhou H., Ni D., Lou J., Zhao Y., Huang Y.
Nat. Struct. Mol. Biol. 23:192-196(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.56 ANGSTROMS) OF 33-88 IN LATERAL CLOSED BAM COMPLEX, SUBUNIT, SUBCELLULAR LOCATION. - Ref.20"Structural basis of outer membrane protein insertion by the BAM complex."
Gu Y., Li H., Dong H., Zeng Y., Zhang Z., Paterson N.G., Stansfeld P.J., Wang Z., Zhang Y., Wang W., Dong C.
Nature 531:64-69(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN LATERAL CLOSED BAM COMPLEX AND LATERAL OPEN BAMACDE SUBCOMPLEX, SUBUNIT, SUBCELLULAR LOCATION. - Ref.21"The structure of the beta-barrel assembly machinery complex."
Bakelar J., Buchanan S.K., Noinaj N.
Science 351:180-186(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.39 ANGSTROMS) OF 25-344 OF LATERAL OPEN BAMACDE COMPLEX, SUBUNIT.
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4107EG0 Bacteria COG3317 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000123040 |
KEGG Orthology (KO) More...KOi | K07287 |
Identification of Orthologs from Complete Genome Data More...OMAi | YTVVWDR |
Family and domain databases
HAMAP database of protein families More...HAMAPi | MF_00924 OM_assembly_BamC, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR014524 BamC IPR010653 NlpB/DapX |
Pfam protein domain database More...Pfami | View protein in Pfam PF06804 Lipoprotein_18, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF026343 NlpB, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51257 PROKAR_LIPOPROTEIN, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
10 20 30 40 50
MAYSVQKSRL AKVAGVSLVL LLAACSSDSR YKRQVSGDEA YLEAAPLAEL
60 70 80 90 100
HAPAGMILPV TSGDYAIPVT NGSGAVGKAL DIRPPAQPLA LVSGARTQFT
110 120 130 140 150
GDTASLLVEN GRGNTLWPQV VSVLQAKNYT ITQRDDAGQT LTTDWVQWNR
160 170 180 190 200
LDEDEQYRGR YQISVKPQGY QQAVTVKLLN LEQAGKPVAD AASMQRYSTE
210 220 230 240 250
MMNVISAGLD KSATDAANAA QNRASTTMDV QSAADDTGLP MLVVRGPFNV
260 270 280 290 300
VWQRLPAALE KVGMKVTDST RSQGNMAVTY KPLSDSDWQE LGASDPGLAS
310 320 330 340
GDYKLQVGDL DNRSSLQFID PKGHTLTQSQ NDALVAVFQA AFSK
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 219 | A → R in M33928 (PubMed:2120198).Curated | 1 |
<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.18"Lateral opening in the intact beta-barrel assembly machinery captured by cryo-EM."
Iadanza M.G., Higgins A.J., Schiffrin B., Calabrese A.N., Brockwell D.J., Ashcroft A.E., Radford S.E., Ranson N.A.
Nat. Commun. 7:12865-12865(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS) OF 25-189 IN LATERAL OPEN BAM COMPLEX, FUNCTION, REACTION MECHANISM, SUBUNIT, MASS SPECTROMETRY, LIPIDATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.18"Lateral opening in the intact beta-barrel assembly machinery captured by cryo-EM."
Iadanza M.G., Higgins A.J., Schiffrin B., Calabrese A.N., Brockwell D.J., Ashcroft A.E., Radford S.E., Ranson N.A.
Nat. Commun. 7:12865-12865(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS) OF 25-189 IN LATERAL OPEN BAM COMPLEX, FUNCTION, REACTION MECHANISM, SUBUNIT, MASS SPECTROMETRY, LIPIDATION.
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X57402 Genomic DNA Translation: CAA40661.1 M33928 Genomic DNA No translation available. U00096 Genomic DNA Translation: AAC75530.2 AP009048 Genomic DNA Translation: BAA16354.1 |
Protein sequence database of the Protein Information Resource More...PIRi | D65023 |
NCBI Reference Sequences More...RefSeqi | NP_416972.4, NC_000913.3 WP_001297320.1, NZ_LN832404.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC75530; AAC75530; b2477 BAA16354; BAA16354; BAA16354 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 946954 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW2462 eco:b2477 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.4262 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P0A903 | Outer membrane protein assembly factor BamC | 344 | |||
| Outer membrane protein assembly factor BamC | 344 | ||||
| Outer membrane protein assembly factor BamC | 344 | ||||
| Outer membrane protein assembly factor BamC | 344 | ||||
| Outer membrane protein assembly factor BamC | 344 | ||||
| +112 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P0A903 | Outer membrane protein assembly factor BamC | 344 | |||
| Outer membrane protein assembly factor BamC | 344 | ||||
| Outer membrane protein assembly factor BamC | 344 | ||||
| Outer membrane protein assembly factor BamC | 344 | ||||
| Outer membrane protein assembly factor BamC | 344 | ||||
| +686 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P0A903 | Outer membrane protein assembly factor BamC | 344 | |||
| Outer membrane protein assembly factor BamC | 344 | ||||
| Outer membrane protein assembly factor BamC | 344 | ||||
| Outer membrane protein assembly factor BamC | 344 | ||||
| Outer membrane protein assembly factor BamC | 344 | ||||
| +1534 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X57402 Genomic DNA Translation: CAA40661.1 M33928 Genomic DNA No translation available. U00096 Genomic DNA Translation: AAC75530.2 AP009048 Genomic DNA Translation: BAA16354.1 |
Protein sequence database of the Protein Information Resource More...PIRi | D65023 |
NCBI Reference Sequences More...RefSeqi | NP_416972.4, NC_000913.3 WP_001297320.1, NZ_LN832404.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2LAE | NMR | - | A | 101-344 | [»] | |
| 2LAF | NMR | - | A | 101-344 | [»] | |
| 2YH5 | X-ray | 1.25 | A | 226-344 | [»] | |
| 2YH6 | X-ray | 1.55 | A/B/C/D | 101-212 | [»] | |
| 3SNS | X-ray | 1.50 | A | 224-343 | [»] | |
| 3TGO | X-ray | 2.90 | C/D | 26-344 | [»] | |
| 5AYW | X-ray | 3.56 | C | 33-88 | [»] | |
| 5D0O | X-ray | 2.90 | C | 1-344 | [»] | |
| 5D0Q | X-ray | 3.50 | C/G | 1-344 | [»] | |
| 5EKQ | X-ray | 3.39 | C | 25-344 | [»] | |
| 5LJO | electron microscopy | 4.90 | C | 25-189 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P0A903 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0A903 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 4262898, 311 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-1923 Bam complex |
Database of interacting proteins More...DIPi | DIP-39898N |
Protein interaction database and analysis system More...IntActi | P0A903, 7 interactors |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_2643 |
Protein family/group databases
Transport Classification Database More...TCDBi | 1.B.33.1.3 the outer membrane protein insertion porin (bam complex) (ompip) family |
2D gel databases
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P0A903 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P0A903 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0A903 |
PRoteomics IDEntifications database More...PRIDEi | P0A903 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 946954 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC75530; AAC75530; b2477 BAA16354; BAA16354; BAA16354 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 946954 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW2462 eco:b2477 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.4262 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB0652 |
Escherichia coli strain K12 genome database More...EcoGenei | EG10658 bamC |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4107EG0 Bacteria COG3317 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000123040 |
KEGG Orthology (KO) More...KOi | K07287 |
Identification of Orthologs from Complete Genome Data More...OMAi | YTVVWDR |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG10658-MONOMER |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P0A903 |
Protein Ontology More...PROi | PR:P0A903 |
Family and domain databases
HAMAP database of protein families More...HAMAPi | MF_00924 OM_assembly_BamC, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR014524 BamC IPR010653 NlpB/DapX |
Pfam protein domain database More...Pfami | View protein in Pfam PF06804 Lipoprotein_18, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF026343 NlpB, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51257 PROKAR_LIPOPROTEIN, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | BAMC_ECOLI | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P0A903Primary (citable) accession number: P0A903 Secondary accession number(s): P21167, P76564 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 19, 2005 |
| Last sequence update: | July 19, 2005 | |
| Last modified: | June 20, 2018 | |
| This is version 115 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
