UniProtKB - P06136 (FTSQ_ECOLI)
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- BLAST>sp|P06136|FTSQ_ECOLI Cell division protein FtsQ OS=Escherichia coli (strain K12) OX=83333 GN=ftsQ PE=1 SV=1 MSQAALNTRNSEEEVSSRRNNGTRLAGILFLLTVLTTVLVSGWVVLGWMEDAQRLPLSKL VLTGERHYTRNDDIRQSILALGEPGTFMTQDVNIIQTQIEQRLPWIKQVSVRKQWPDELK IHLVEYVPIARWNDQHMVDAEGNTFSVPPERTSKQVLPMLYGPEGSANEVLQGYREMGQM LAKDRFTLKEAAMTARRSWQLTLNNDIKLNLGRGDTMKRLARFVELYPVLQQQAQTDGKR ISYVDLRYDSGAAVGWAPLPPEESTQQQNQAQAEQQ
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Cell division protein FtsQ
ftsQ
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>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.17"Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins."
D'Ulisse V., Fagioli M., Ghelardini P., Paolozzi L.
Microbiology 153:124-138(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, DOMAIN, INTERACTION WITH FTSK; FTSW; FTSI AND FTSN. - Ref.18"Divisome under construction: distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins."
Gonzalez M.D., Beckwith J.
J. Bacteriol. 191:2815-2825(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, INTERACTION WITH FTSB.
<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
- cell division Source: EcoliWiki <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
- division septum assembly Source: EcoliWiki <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
- FtsZ-dependent cytokinesis 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
<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>Keywordsi
| Biological process | Cell cycle, Cell division |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG10342-MONOMER |
<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: Cell division protein FtsQUniRule 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:ftsQUniRule 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 Ordered Locus Names:b0093, JW0091 |
| <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 | EG10342 ftsQ |
<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 inner 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
8 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.8"The FtsQ protein of Escherichia coli: membrane topology, abundance, and cell division phenotypes due to overproduction and insertion mutations."
Carson M.J., Barondess J., Beckwith J.
J. Bacteriol. 173:2187-2195(1991) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TOPOLOGY. - Ref.9"Localization of cell division protein FtsQ by immunofluorescence microscopy in dividing and nondividing cells of Escherichia coli."
Buddelmeijer N., Aarsman M.E., Kolk A.H., Vicente M., Nanninga N.
J. Bacteriol. 180:6107-6116(1998) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, DOMAIN. - Ref.10"Septal localization of FtsQ, an essential cell division protein in Escherichia coli."
Chen J.C., Weiss D.S., Ghigo J.M., Beckwith J.
J. Bacteriol. 181:521-530(1999) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, DOMAIN. - Ref.11"Sec-dependent membrane protein insertion: sequential interaction of nascent FtsQ with SecY and YidC."
Urbanus M.L., Scotti P.A., Froderberg L., Saaf A., de Gier J.W., Brunner J., Samuelson J.C., Dalbey R.E., Oudega B., Luirink J.
EMBO Rep. 2:524-529(2001) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.12"FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division."
Chen J.C., Beckwith J.
Mol. Microbiol. 42:395-413(2001) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.13"ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the septal ring in Escherichia coli."
Hale C.A., de Boer P.A.J.
J. Bacteriol. 184:2552-2556(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.14"A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region."
Buddelmeijer N., Beckwith J.
Mol. Microbiol. 52:1315-1327(2004) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, INTERACTION WITH FTSL AND FTSB, SUBCELLULAR LOCATION. - Ref.16"Contribution of the FtsQ transmembrane segment to localization to the cell division site."
Scheffers D.J., Robichon C., Haan G.J., den Blaauwen T., Koningstein G., van Bloois E., Beckwith J., Luirink J.
J. Bacteriol. 189:7273-7280(2007) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF LEU-29; LEU-32 AND VAL-38.
<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
8 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.8"The FtsQ protein of Escherichia coli: membrane topology, abundance, and cell division phenotypes due to overproduction and insertion mutations."
Carson M.J., Barondess J., Beckwith J.
J. Bacteriol. 173:2187-2195(1991) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TOPOLOGY. - Ref.9"Localization of cell division protein FtsQ by immunofluorescence microscopy in dividing and nondividing cells of Escherichia coli."
Buddelmeijer N., Aarsman M.E., Kolk A.H., Vicente M., Nanninga N.
J. Bacteriol. 180:6107-6116(1998) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, DOMAIN. - Ref.10"Septal localization of FtsQ, an essential cell division protein in Escherichia coli."
Chen J.C., Weiss D.S., Ghigo J.M., Beckwith J.
J. Bacteriol. 181:521-530(1999) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, DOMAIN. - Ref.11"Sec-dependent membrane protein insertion: sequential interaction of nascent FtsQ with SecY and YidC."
Urbanus M.L., Scotti P.A., Froderberg L., Saaf A., de Gier J.W., Brunner J., Samuelson J.C., Dalbey R.E., Oudega B., Luirink J.
EMBO Rep. 2:524-529(2001) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.12"FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division."
Chen J.C., Beckwith J.
Mol. Microbiol. 42:395-413(2001) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.13"ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the septal ring in Escherichia coli."
Hale C.A., de Boer P.A.J.
J. Bacteriol. 184:2552-2556(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.14"A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region."
Buddelmeijer N., Beckwith J.
Mol. Microbiol. 52:1315-1327(2004) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, INTERACTION WITH FTSL AND FTSB, SUBCELLULAR LOCATION. - Ref.16"Contribution of the FtsQ transmembrane segment to localization to the cell division site."
Scheffers D.J., Robichon C., Haan G.J., den Blaauwen T., Koningstein G., van Bloois E., Beckwith J., Luirink J.
J. Bacteriol. 189:7273-7280(2007) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF LEU-29; LEU-32 AND VAL-38.
Note: Localizes to the division septum. Localization requires FtsZ, FtsA, ZipA and FtsK, but not FtsL, FtsI and FtsN. Insertion into the membrane requires YidC and the Sec translocase.
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 1 – 27 | CytoplasmicUniRule 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 | 27 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 28 – 48 | HelicalUniRule 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 | 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 49 – 276 | PeriplasmicUniRule 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 | 228 |
<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
- cell division site 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 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
- integral component of plasma 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
- plasma 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
<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 inner membrane, Cell 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
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 29 | L → R: No change in activity. Correctly assembled, interacts with FtsB and FtsL, but fails to localize efficiently to the cell division site; when associated with R-32. Does not insert into the membrane and lack of activity; when associated with R-32 and P-38. 1 Publication <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/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 32 | L → R: No change in activity. Correctly assembled, interacts with FtsB and FtsL, but fails to localize efficiently to the cell division site; when associated with R-29. Does not insert into the membrane and lack of activity; when associated with R-29 and P-38. 1 Publication <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/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 38 | V → P: No change in activity. Does not insert into the membrane and lack of activity; when associated with R-29 and R-32. 1 Publication <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/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 91 | D → K or Q: Does not affect localization. 1 Publication <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/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 113 | K → D: Impairs localization. 1 Publication <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/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 125 | E → K: Impairs localization. 1 Publication <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/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 237 | D → N: Localizes to mid-cell, but is unable to form a functional complex with FtsL/FtsB. 1 Publication <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 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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000160580 | 1 – 276 | Cell division protein FtsQAdd BLAST | 276 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P06136 |
PRoteomics IDEntifications database More...PRIDEi | P06136 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<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.19"Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli."
Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J., Walker G.C.
Mol. Cell 36:845-860(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION BY HYDROXYUREA.
<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>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
4 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.14"A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region."
Buddelmeijer N., Beckwith J.
Mol. Microbiol. 52:1315-1327(2004) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, INTERACTION WITH FTSL AND FTSB, SUBCELLULAR LOCATION. - Ref.15"Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis."
Karimova G., Dautin N., Ladant D.
J. Bacteriol. 187:2233-2243(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FTSL; FTSA; FTSI; FTSN; FTSX AND YMGF. - Ref.17"Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins."
D'Ulisse V., Fagioli M., Ghelardini P., Paolozzi L.
Microbiology 153:124-138(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, DOMAIN, INTERACTION WITH FTSK; FTSW; FTSI AND FTSN. - Ref.18"Divisome under construction: distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins."
Gonzalez M.D., Beckwith J.
J. Bacteriol. 191:2815-2825(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, INTERACTION WITH FTSB.
<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 | 6 | EBI-1130157,EBI-1130157 | ||
| ftsB | P0A6S5 | 10 | EBI-1130157,EBI-1113953 | |
| ftsI | P0AD68 | 5 | EBI-1130157,EBI-548564 | |
| ftsK | P46889 | 3 | EBI-1130157,EBI-550795 | |
| ftsL | P0AEN4 | 11 | EBI-1130157,EBI-1119082 | |
| ftsN | P29131 | 7 | EBI-1130157,EBI-1134233 | |
| ftsW | P0ABG4 | 3 | EBI-1130157,EBI-1214767 | |
| ymgF | P58034 | 3 | EBI-1130157,EBI-1214577 |
<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 | 4261112, 336 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-3099 FtsQBL complex |
Database of interacting proteins More...DIPi | DIP-9706N |
Protein interaction database and analysis system More...IntActi | P06136, 19 interactors |
Molecular INTeraction database More...MINTi | P06136 |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_0075 |
<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 | 59 – 64 | 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 | 71 – 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 | 9 | |
| <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 | 87 – 89 | 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 | 92 – 102 | 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 | 106 – 114 | 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 | 115 – 117 | 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 | 118 – 125 | 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 | 128 – 132 | 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 | 133 – 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 | 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 | 136 – 139 | 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 | 149 – 151 | 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 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 | 152 – 154 | 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 | 159 – 161 | 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 | 167 – 182 | 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 | 16 | |
| <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 | 190 – 193 | 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 | 195 – 197 | 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 | 199 – 202 | 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 | 204 – 206 | 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 | 208 – 214 | 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 | 216 – 236 | 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 | 21 | |
| <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 | 239 – 248 | 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 | 10 | |
| <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 | 251 – 258 | 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 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P06136 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P06136 |
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 | P06136 |
<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
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 55 – 126 | POTRAPROSITE-ProRule 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 | 72 |
<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.9"Localization of cell division protein FtsQ by immunofluorescence microscopy in dividing and nondividing cells of Escherichia coli."
Buddelmeijer N., Aarsman M.E., Kolk A.H., Vicente M., Nanninga N.
J. Bacteriol. 180:6107-6116(1998) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, DOMAIN. - Ref.10"Septal localization of FtsQ, an essential cell division protein in Escherichia coli."
Chen J.C., Weiss D.S., Ghigo J.M., Beckwith J.
J. Bacteriol. 181:521-530(1999) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, DOMAIN. - Ref.16"Contribution of the FtsQ transmembrane segment to localization to the cell division site."
Scheffers D.J., Robichon C., Haan G.J., den Blaauwen T., Koningstein G., van Bloois E., Beckwith J., Luirink J.
J. Bacteriol. 189:7273-7280(2007) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF LEU-29; LEU-32 AND VAL-38. - Ref.17"Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins."
D'Ulisse V., Fagioli M., Ghelardini P., Paolozzi L.
Microbiology 153:124-138(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, DOMAIN, INTERACTION WITH FTSK; FTSW; FTSI AND FTSN. - Ref.21"Structural and mutational analysis of the cell division protein FtsQ."
van den Ent F., Vinkenvleugel T.M., Ind A., West P., Veprintsev D., Nanninga N., den Blaauwen T., Lowe J.
Mol. Microbiol. 68:110-123(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 58-276, DOMAIN, MUTAGENESIS OF ASP-91; LYS-113; GLU-125 AND ASP-237.
<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
Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4105K7E Bacteria COG1589 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000255872 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P06136 |
KEGG Orthology (KO) More...KOi | K03589 |
Identification of Orthologs from Complete Genome Data More...OMAi | MARIQRF |
Database for complete collections of gene phylogenies More...PhylomeDBi | P06136 |
Family and domain databases
HAMAP database of protein families More...HAMAPi | MF_00911 FtsQ_subfam, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR005548 Cell_div_FtsQ/DivIB IPR026579 FtsQ IPR034746 POTRA IPR013685 POTRA_FtsQ_type |
The PANTHER Classification System More...PANTHERi | PTHR35851 PTHR35851, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF03799 FtsQ, 1 hit PF08478 POTRA_1, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51779 POTRA, 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.
10 20 30 40 50
MSQAALNTRN SEEEVSSRRN NGTRLAGILF LLTVLTTVLV SGWVVLGWME
60 70 80 90 100
DAQRLPLSKL VLTGERHYTR NDDIRQSILA LGEPGTFMTQ DVNIIQTQIE
110 120 130 140 150
QRLPWIKQVS VRKQWPDELK IHLVEYVPIA RWNDQHMVDA EGNTFSVPPE
160 170 180 190 200
RTSKQVLPML YGPEGSANEV LQGYREMGQM LAKDRFTLKE AAMTARRSWQ
210 220 230 240 250
LTLNNDIKLN LGRGDTMKRL ARFVELYPVL QQQAQTDGKR ISYVDLRYDS
260 270
GAAVGWAPLP PEESTQQQNQ AQAEQQ
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 | M14029 Genomic DNA Translation: AAA23673.1 K02668 Genomic DNA Translation: AAA23816.1 X55034 Genomic DNA Translation: CAA38870.1 U00096 Genomic DNA Translation: AAC73204.1 AP009048 Genomic DNA Translation: BAB96661.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S10852 CEECQ |
NCBI Reference Sequences More...RefSeqi | NP_414635.1, NC_000913.3 WP_000075748.1, NZ_LN832404.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC73204; AAC73204; b0093 BAB96661; BAB96661; BAB96661 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 944823 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW0091 eco:b0093 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.2187 |
<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 | |
|---|---|---|---|---|---|
| P06136 | Cell division protein FtsQ | 276 | |||
| Cell division protein FtsQ | 276 | ||||
| Cell division protein FtsQ | 276 | ||||
| Cell division protein FtsQ | 276 | ||||
| Cell division protein FtsQ | 276 | ||||
| +24 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P06136 | Cell division protein FtsQ | 276 | |||
| Cell division protein FtsQ | 276 | ||||
| Cell division protein FtsQ | 276 | ||||
| Cell division protein FtsQ | 276 | ||||
| Cell division protein FtsQ | 276 | ||||
| +428 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P06136 | Cell division protein FtsQ | 276 | |||
| Cell division protein FtsQ | 276 | ||||
| Cell division protein FtsQ | 276 | ||||
| Cell division protein FtsQ | 276 | ||||
| Cell division protein FtsQ | 276 | ||||
| +1351 | |||||
<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 | M14029 Genomic DNA Translation: AAA23673.1 K02668 Genomic DNA Translation: AAA23816.1 X55034 Genomic DNA Translation: CAA38870.1 U00096 Genomic DNA Translation: AAC73204.1 AP009048 Genomic DNA Translation: BAB96661.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S10852 CEECQ |
NCBI Reference Sequences More...RefSeqi | NP_414635.1, NC_000913.3 WP_000075748.1, 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 |
| 2VH1 | X-ray | 2.70 | A/B | 58-276 | [»] | |
| 4UE4 | electron microscopy | 7.00 | B | 29-50 | [»] | |
| 4V6M | electron microscopy | 7.1 | Z | 22-103 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P06136 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P06136 | |||||
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 | 4261112, 336 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-3099 FtsQBL complex |
Database of interacting proteins More...DIPi | DIP-9706N |
Protein interaction database and analysis system More...IntActi | P06136, 19 interactors |
Molecular INTeraction database More...MINTi | P06136 |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_0075 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P06136 |
PRoteomics IDEntifications database More...PRIDEi | P06136 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC73204; AAC73204; b0093 BAB96661; BAB96661; BAB96661 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 944823 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW0091 eco:b0093 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.2187 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB0338 |
Escherichia coli strain K12 genome database More...EcoGenei | EG10342 ftsQ |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4105K7E Bacteria COG1589 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000255872 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P06136 |
KEGG Orthology (KO) More...KOi | K03589 |
Identification of Orthologs from Complete Genome Data More...OMAi | MARIQRF |
Database for complete collections of gene phylogenies More...PhylomeDBi | P06136 |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG10342-MONOMER |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P06136 |
Protein Ontology More...PROi | PR:P06136 |
Family and domain databases
HAMAP database of protein families More...HAMAPi | MF_00911 FtsQ_subfam, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR005548 Cell_div_FtsQ/DivIB IPR026579 FtsQ IPR034746 POTRA IPR013685 POTRA_FtsQ_type |
The PANTHER Classification System More...PANTHERi | PTHR35851 PTHR35851, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF03799 FtsQ, 1 hit PF08478 POTRA_1, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51779 POTRA, 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 | FTSQ_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 | P06136Primary (citable) accession number: P06136 | |
| <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: | January 1, 1988 |
| Last sequence update: | January 1, 1988 | |
| Last modified: | June 20, 2018 | |
| This is version 148 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
