UniProtKB - P0A937 (BAME_ECOLI)
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- BLAST>sp|P0A937|BAME_ECOLI Outer membrane protein assembly factor BamE OS=Escherichia coli (strain K12) OX=83333 GN=bamE PE=1 SV=1 MRCKTLTAAAAVLLMLTAGCSTLERVVYRPDINQGNYLTANDVSKIRVGMTQQQVAYALG TPLMSDPFGTNTWFYVFRQQPGHEGVTQQTLTLTFNSSGVLTNIDNKPALSGN
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Outer membrane protein assembly factor BamE
bamE
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.5"Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli."
Sklar J.G., Wu T., Gronenberg L.S., Malinverni J.C., Kahne D., Silhavy T.J.
Proc. Natl. Acad. Sci. U.S.A. 104:6400-6405(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. - Ref.6"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.7"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.8"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.10"Structural characterization of Escherichia coli BamE, a lipoprotein component of the beta-barrel assembly machinery complex."
Kim K.H., Kang H.S., Okon M., Escobar-Cabrera E., McIntosh L.P., Paetzel M.
Biochemistry 50:1081-1090(2011) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 21-113, FUNCTION, SUBUNIT. - Ref.12"Structural basis of outer membrane protein biogenesis in bacteria."
Albrecht R., Zeth K.
J. Biol. Chem. 286:27792-27803(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 34-113, SUBUNIT, FUNCTION. - Ref.13"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 24-110 IN LATERAL OPEN BAM COMPLEX, FUNCTION, REACTION MECHANISM, SUBUNIT, MASS SPECTROMETRY, DIACYLGLYCEROL AT CYS-20, PALMITOYLATION AT CYS-20. - Ref.14"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 20-113 IN LATERAL CLOSED BAM COMPLEX, SUBUNIT, SUBCELLULAR LOCATION. - Ref.15"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.16"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 20-113 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
- protein binding, bridging Source: EcoCyc <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: 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
- protein insertion into membrane 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
- response to antibiotic Source: EcoCyc <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG10952-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 BamEUniRule 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:bamEUniRule 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:smpA Ordered Locus Names:b2617, JW2598 |
| <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 | EG10952 bamE |
<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.5"Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli."
Sklar J.G., Wu T., Gronenberg L.S., Malinverni J.C., Kahne D., Silhavy T.J.
Proc. Natl. Acad. Sci. U.S.A. 104:6400-6405(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. - Ref.14"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 20-113 IN LATERAL CLOSED BAM COMPLEX, SUBUNIT, SUBCELLULAR LOCATION. - Ref.15"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.5"Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli."
Sklar J.G., Wu T., Gronenberg L.S., Malinverni J.C., Kahne D., Silhavy T.J.
Proc. Natl. Acad. Sci. U.S.A. 104:6400-6405(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. - Ref.13"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 24-110 IN LATERAL OPEN BAM COMPLEX, FUNCTION, REACTION MECHANISM, SUBUNIT, MASS SPECTROMETRY, DIACYLGLYCEROL AT CYS-20, PALMITOYLATION AT CYS-20.
<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
- integral component of cell outer membrane 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
- membrane Source: EcoliWiki <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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei
<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.5"Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli."
Sklar J.G., Wu T., Gronenberg L.S., Malinverni J.C., Kahne D., Silhavy T.J.
Proc. Natl. Acad. Sci. U.S.A. 104:6400-6405(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
<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 – 19 | 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 Add BLAST | 19 | |
| <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_0000032810 | 20 – 113 | Outer membrane protein assembly factor BamEAdd BLAST | 94 |
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 | 20 | N-palmitoyl cysteine1 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
| 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 | 20 | S-diacylglycerol cysteine1 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
| 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
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0A937 |
PRoteomics IDEntifications database More...PRIDEi | P0A937 |
<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.5"Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli."
Sklar J.G., Wu T., Gronenberg L.S., Malinverni J.C., Kahne D., Silhavy T.J.
Proc. Natl. Acad. Sci. U.S.A. 104:6400-6405(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. - Ref.6"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.7"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.9"Crystallization and preliminary X-ray data collection of the Escherichia coli lipoproteins BamC, BamD and BamE."
Albrecht R., Zeth K.
Acta Crystallogr. F 66:1586-1590(2010) [PubMed] [Europe PMC] [Abstract]Cited for: CRYSTALLIZATION, SUBUNIT. - Ref.10"Structural characterization of Escherichia coli BamE, a lipoprotein component of the beta-barrel assembly machinery complex."
Kim K.H., Kang H.S., Okon M., Escobar-Cabrera E., McIntosh L.P., Paetzel M.
Biochemistry 50:1081-1090(2011) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 21-113, FUNCTION, SUBUNIT. - Ref.11"Structure and function of BamE within the outer membrane and the beta-barrel assembly machine."
Knowles T.J., Browning D.F., Jeeves M., Maderbocus R., Rajesh S., Sridhar P., Manoli E., Emery D., Sommer U., Spencer A., Leyton D.L., Squire D., Chaudhuri R.R., Viant M.R., Cunningham A.F., Henderson I.R., Overduin M.
EMBO Rep. 12:123-128(2011) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 21-113, SUBUNIT. - Ref.12"Structural basis of outer membrane protein biogenesis in bacteria."
Albrecht R., Zeth K.
J. Biol. Chem. 286:27792-27803(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 34-113, SUBUNIT, FUNCTION. - Ref.13"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 24-110 IN LATERAL OPEN BAM COMPLEX, FUNCTION, REACTION MECHANISM, SUBUNIT, MASS SPECTROMETRY, DIACYLGLYCEROL AT CYS-20, PALMITOYLATION AT CYS-20. - Ref.14"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 20-113 IN LATERAL CLOSED BAM COMPLEX, SUBUNIT, SUBCELLULAR LOCATION. - Ref.15"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.16"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 20-113 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 | 14 | EBI-6391574,EBI-6391574 | ||
| bamD | P0AC02 | 3 | EBI-6391574,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 binding, bridging Source: EcoCyc <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 | 4259570, 145 interactors 849957, 1 interactor |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-1923 Bam complex |
Database of interacting proteins More...DIPi | DIP-10895N |
Protein interaction database and analysis system More...IntActi | P0A937, 5 interactors |
Molecular INTeraction database More...MINTi | P0A937 |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_2783 |
<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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 32 – 35 | 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 | 42 – 44 | 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 | 52 – 59 | 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 | 8 | |
| <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 | 63 – 65 | 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 | 68 – 70 | 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 | 71 – 76 | 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 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 | 82 – 84 | 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 | 85 – 87 | 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 | 90 – 95 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 99 – 107 | 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 | 9 | |
| <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 | 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 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P0A937 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0A937 |
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 | P0A937 |
<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 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 | ENOG4105YRI Bacteria COG2913 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000256181 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0A937 |
KEGG Orthology (KO) More...KOi | K06186 |
Identification of Orthologs from Complete Genome Data More...OMAi | QPGHEKV |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0A937 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.1450.10, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_00925 OM_assembly_BamE, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR026592 BamE IPR037873 BamE-like IPR007450 Lipoprotein_SmpA/OmlA |
The PANTHER Classification System More...PANTHERi | PTHR37482 PTHR37482, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF04355 SmpA_OmlA, 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
MRCKTLTAAA AVLLMLTAGC STLERVVYRP DINQGNYLTA NDVSKIRVGM
60 70 80 90 100
TQQQVAYALG TPLMSDPFGT NTWFYVFRQQ PGHEGVTQQT LTLTFNSSGV
110
LTNIDNKPAL SGN
<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
<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.13"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 24-110 IN LATERAL OPEN BAM COMPLEX, FUNCTION, REACTION MECHANISM, SUBUNIT, MASS SPECTROMETRY, DIACYLGLYCEROL AT CYS-20, PALMITOYLATION AT CYS-20.
<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.13"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 24-110 IN LATERAL OPEN BAM COMPLEX, FUNCTION, REACTION MECHANISM, SUBUNIT, MASS SPECTROMETRY, DIACYLGLYCEROL AT CYS-20, PALMITOYLATION AT CYS-20.
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 | U36840 Genomic DNA Translation: AAA79787.1 U00096 Genomic DNA Translation: AAC75666.2 AP009048 Genomic DNA Translation: BAA16502.1 X52620 Genomic DNA Translation: CAA36847.1 Sequence problems. |
Protein sequence database of the Protein Information Resource More...PIRi | S11646 T08630 |
NCBI Reference Sequences More...RefSeqi | NP_417107.2, NC_000913.3 WP_001203437.1, NZ_LN832404.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC75666; AAC75666; b2617 BAA16502; BAA16502; BAA16502 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 945583 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW2598 eco:b2617 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.4122 |
<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 | |
|---|---|---|---|---|---|
| P0A937 | Outer membrane protein assembly factor BamE | 113 | |||
| Outer membrane protein assembly factor BamE | 113 | ||||
| Outer membrane protein assembly factor BamE | 113 | ||||
| Outer membrane protein assembly factor BamE | 113 | ||||
| Outer membrane protein assembly factor BamE | 113 | ||||
| +192 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P0A937 | Outer membrane protein assembly factor BamE | 112 | |||
| Outer membrane protein assembly factor BamE | 112 | ||||
| Outer membrane protein assembly factor BamE | 112 | ||||
| Outer membrane protein assembly factor BamE | 112 | ||||
| Outer membrane protein assembly factor BamE | 112 | ||||
| +593 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P0A937 | Outer membrane protein assembly factor BamE | 112 | |||
| Outer membrane protein assembly factor BamE | 112 | ||||
| Outer membrane protein assembly factor BamE | 112 | ||||
| Outer membrane protein assembly factor BamE | 112 | ||||
| Outer membrane protein assembly factor BamE | 112 | ||||
| +1061 | |||||
<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 | U36840 Genomic DNA Translation: AAA79787.1 U00096 Genomic DNA Translation: AAC75666.2 AP009048 Genomic DNA Translation: BAA16502.1 X52620 Genomic DNA Translation: CAA36847.1 Sequence problems. |
Protein sequence database of the Protein Information Resource More...PIRi | S11646 T08630 |
NCBI Reference Sequences More...RefSeqi | NP_417107.2, NC_000913.3 WP_001203437.1, 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 |
| 2KM7 | NMR | - | A | 20-113 | [»] | |
| 2KXX | NMR | - | A | 21-113 | [»] | |
| 2YH9 | X-ray | 1.80 | A/B/C | 34-113 | [»] | |
| 5AYW | X-ray | 3.56 | E | 20-113 | [»] | |
| 5D0O | X-ray | 2.90 | E | 1-113 | [»] | |
| 5D0Q | X-ray | 3.50 | E/I | 1-113 | [»] | |
| 5EKQ | X-ray | 3.39 | E | 20-113 | [»] | |
| 5LJO | electron microscopy | 4.90 | E | 24-110 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P0A937 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0A937 | |||||
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 | 4259570, 145 interactors 849957, 1 interactor |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-1923 Bam complex |
Database of interacting proteins More...DIPi | DIP-10895N |
Protein interaction database and analysis system More...IntActi | P0A937, 5 interactors |
Molecular INTeraction database More...MINTi | P0A937 |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_2783 |
Protein family/group databases
Transport Classification Database More...TCDBi | 1.B.33.1.3 the outer membrane protein insertion porin (bam complex) (ompip) family |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0A937 |
PRoteomics IDEntifications database More...PRIDEi | P0A937 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC75666; AAC75666; b2617 BAA16502; BAA16502; BAA16502 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 945583 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW2598 eco:b2617 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.4122 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB0945 |
Escherichia coli strain K12 genome database More...EcoGenei | EG10952 bamE |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4105YRI Bacteria COG2913 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000256181 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0A937 |
KEGG Orthology (KO) More...KOi | K06186 |
Identification of Orthologs from Complete Genome Data More...OMAi | QPGHEKV |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0A937 |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG10952-MONOMER |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P0A937 |
Protein Ontology More...PROi | PR:P0A937 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.1450.10, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_00925 OM_assembly_BamE, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR026592 BamE IPR037873 BamE-like IPR007450 Lipoprotein_SmpA/OmlA |
The PANTHER Classification System More...PANTHERi | PTHR37482 PTHR37482, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF04355 SmpA_OmlA, 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 | BAME_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 | P0A937Primary (citable) accession number: P0A937 Secondary accession number(s): P23089 | |
| <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 107 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
