UniProtKB - P0C0S1 (MSCS_ECOLI)
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- BLAST>sp|P0C0S1|MSCS_ECOLI Small-conductance mechanosensitive channel OS=Escherichia coli (strain K12) OX=83333 GN=mscS PE=1 SV=1 MEDLNVVDSINGAGSWLVANQALLLSYAVNIVAALAIIIVGLIIARMISNAVNRLMISRK IDATVADFLSALVRYGIIAFTLIAALGRVGVQTASVIAVLGAAGLAVGLALQGSLSNLAA GVLLVMFRPFRAGEYVDLGGVAGTVLSVQIFSTTMRTADGKIIVIPNGKIIAGNIINFSR EPVRRNEFIIGVAYDSDIDQVKQILTNIIQSEDRILKDREMTVRLNELGASSINFVVRVW SNSGDLQNVYWDVLERIKREFDAAGISFPYPQMDVNFKRVKEDKAA
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Small-conductance mechanosensitive channel
mscS
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.4"Pressure-sensitive ion channel in Escherichia coli."
Martinac B., Buechner M., Delcour A.H., Adler J., Kung C.
Proc. Natl. Acad. Sci. U.S.A. 84:2297-2301(1987) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.5"Characterization of mechanosensitive channels in Escherichia coli cytoplasmic membrane by whole-cell patch clamp recording."
Cui C., Smith D.O., Adler J.
J. Membr. Biol. 144:31-42(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SENSITIVITY TO OSMOTIC AND VOLTAGE DIFFERENCES ACROSS THE CYTOPLASMIC MEMBRANE. - Ref.6"Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: identification of genes required for MscS activity."
Levina N., Toetemeyer S., Stokes N.R., Louis P., Jones M.A., Booth I.R.
EMBO J. 18:1730-1737(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, PHYSIOLOGICAL ROLE. - Ref.7"Purification of the small mechanosensitive channel of Escherichia coli (MscS): the subunit structure, conduction, and gating characteristics in liposomes."
Sukharev S.
Biophys. J. 83:290-298(2002) [PubMed] [Europe PMC] [Abstract]Cited for: LIPOSOME RECONSTITUTION, FUNCTION. - Ref.8"Functional design of bacterial mechanosensitive channels. Comparisons and contrasts illuminated by random mutagenesis."
Okada K., Moe P.C., Blount P.
J. Biol. Chem. 277:27682-27688(2002) [PubMed] [Europe PMC] [Abstract]Cited for: LIPOSOME RECONSTITUTION, FUNCTION, MUTAGENESIS OF VAL-40. - Ref.9"C termini of the Escherichia coli mechanosensitive ion channel (MscS) move apart upon the channel opening."
Koprowski P., Kubalski A.
J. Biol. Chem. 278:11237-11245(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CROSS-LINKING OF THE C-TERMINI INHIBITS CHANNEL OPENING, DOMAIN, FUNCTION, SUBCELLULAR LOCATION. - Ref.10"The closed structure of the MscS mechanosensitive channel. Cross-linking of single cysteine mutants."
Miller S., Edwards M.D., Ozdemir C., Booth I.R.
J. Biol. Chem. 278:32246-32250(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT IN THE CLOSED STATE, MUTAGENESIS OF SER-58 AND SER-267, DOMAIN. - Ref.15"Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel."
Bass R.B., Strop P., Barclay M., Rees D.C.
Science 298:1582-1587(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS) OF 27-280 PROBABLY IN THE OPEN STATE, SUBUNIT, FUNCTION, TOPOLOGY, DOMAIN. - Ref.16"Conformational state of the MscS mechanosensitive channel in solution revealed by pulsed electron-electron double resonance (PELDOR) spectroscopy."
Pliotas C., Ward R., Branigan E., Rasmussen A., Hagelueken G., Huang H., Black S.S., Booth I.R., Schiemann O., Naismith J.H.
Proc. Natl. Acad. Sci. U.S.A. 109:E2675-E2682(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (4.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY. - Ref.17"Structure and molecular mechanism of an anion-selective mechanosensitive channel of small conductance."
Zhang X., Wang J., Feng Y., Ge J., Li W., Sun W., Iscla I., Yu J., Blount P., Li Y., Yang M.
Proc. Natl. Acad. Sci. U.S.A. 109:18180-18185(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 272-286, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ALA-158. - Ref.19"The role of lipids in mechanosensation."
Pliotas C., Dahl A.C., Rasmussen T., Mahendran K.R., Smith T.K., Marius P., Gault J., Banda T., Rasmussen A., Miller S., Robinson C.V., Bayley H., Sansom M.S., Booth I.R., Naismith J.H.
Nat. Struct. Mol. Biol. 22:991-998(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS), FUNCTION, SUBUNIT, TOPOLOGY, DOMAIN.
<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
- mechanosensitive ion channel activity Source: UniProtKB <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>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
- cellular water homeostasis 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
- ion transmembrane transport Source: UniProtKB <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 homooligomerization Source: UniProtKB <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>Keywordsi
| Molecular function | Ion channel |
| Biological process | Ion transport, Transport |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG11160-MONOMER |
Protein family/group databases
Transport Classification Database More...TCDBi | 1.A.23.2.1 the small conductance mechanosensitive ion channel (mscs) 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: Small-conductance mechanosensitive channel |
| <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:mscS Synonyms:yggB Ordered Locus Names:b2924, JW2891 |
| <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 | EG11160 mscS |
<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 7 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.4"Pressure-sensitive ion channel in Escherichia coli."
Martinac B., Buechner M., Delcour A.H., Adler J., Kung C.
Proc. Natl. Acad. Sci. U.S.A. 84:2297-2301(1987) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.5"Characterization of mechanosensitive channels in Escherichia coli cytoplasmic membrane by whole-cell patch clamp recording."
Cui C., Smith D.O., Adler J.
J. Membr. Biol. 144:31-42(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SENSITIVITY TO OSMOTIC AND VOLTAGE DIFFERENCES ACROSS THE CYTOPLASMIC MEMBRANE. - Ref.6"Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: identification of genes required for MscS activity."
Levina N., Toetemeyer S., Stokes N.R., Louis P., Jones M.A., Booth I.R.
EMBO J. 18:1730-1737(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, PHYSIOLOGICAL ROLE. - Ref.9"C termini of the Escherichia coli mechanosensitive ion channel (MscS) move apart upon the channel opening."
Koprowski P., Kubalski A.
J. Biol. Chem. 278:11237-11245(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CROSS-LINKING OF THE C-TERMINI INHIBITS CHANNEL OPENING, DOMAIN, FUNCTION, SUBCELLULAR LOCATION. - Ref.12"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, SUBCELLULAR LOCATION. - Ref.16"Conformational state of the MscS mechanosensitive channel in solution revealed by pulsed electron-electron double resonance (PELDOR) spectroscopy."
Pliotas C., Ward R., Branigan E., Rasmussen A., Hagelueken G., Huang H., Black S.S., Booth I.R., Schiemann O., Naismith J.H.
Proc. Natl. Acad. Sci. U.S.A. 109:E2675-E2682(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (4.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY. - Ref.17"Structure and molecular mechanism of an anion-selective mechanosensitive channel of small conductance."
Zhang X., Wang J., Feng Y., Ge J., Li W., Sun W., Iscla I., Yu J., Blount P., Li Y., Yang M.
Proc. Natl. Acad. Sci. U.S.A. 109:18180-18185(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 272-286, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ALA-158.
<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.12"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, SUBCELLULAR LOCATION. - Ref.15"Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel."
Bass R.B., Strop P., Barclay M., Rees D.C.
Science 298:1582-1587(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS) OF 27-280 PROBABLY IN THE OPEN STATE, SUBUNIT, FUNCTION, TOPOLOGY, DOMAIN. - Ref.16"Conformational state of the MscS mechanosensitive channel in solution revealed by pulsed electron-electron double resonance (PELDOR) spectroscopy."
Pliotas C., Ward R., Branigan E., Rasmussen A., Hagelueken G., Huang H., Black S.S., Booth I.R., Schiemann O., Naismith J.H.
Proc. Natl. Acad. Sci. U.S.A. 109:E2675-E2682(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (4.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY. - Ref.18"Open and shut: crystal structures of the dodecylmaltoside solubilized mechanosensitive channel of small conductance from Escherichia coli and Helicobacter pylori at 4.4 A and 4.1 A resolutions."
Lai J.Y., Poon Y.S., Kaiser J.T., Rees D.C.
Protein Sci. 22:502-509(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (4.37 ANGSTROMS), SUBUNIT, TOPOLOGY. - Ref.19"The role of lipids in mechanosensation."
Pliotas C., Dahl A.C., Rasmussen T., Mahendran K.R., Smith T.K., Marius P., Gault J., Banda T., Rasmussen A., Miller S., Robinson C.V., Bayley H., Sansom M.S., Booth I.R., Naismith J.H.
Nat. Struct. Mol. Biol. 22:991-998(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS), FUNCTION, SUBUNIT, TOPOLOGY, DOMAIN.
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 – 30 | Periplasmic1 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
| 30 | |
| <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 | 31 – 52 | Helical2 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
| 22 | |
| <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 | 53 – 67 | Cytoplasmic1 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
| 15 | |
| <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 | 68 – 88 | Helical2 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
| 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 | 89 – 90 | Periplasmic1 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
| 2 | |
| <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 | 91 – 111 | Helical2 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
| 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 | 112 – 286 | Cytoplasmic1 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
| 175 |
<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
- integral component of 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
- integral component of plasma membrane Source: UniProtKB <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 | 40 | V → C, G or N: No detectable phenotype. 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 | 40 | V → D or K: Normal growth stops, without cell death, due to increased membrane permeability to potassium ions and protons (permeability tested only for D substitutions). 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 | 58 | S → C: Readily forms disulfide bonds with cross-linkers, suggesting that individual S-58 are only 3 Angstroms apart in the closed state, versus 33 Angstroms apart in the open state crystal structure. 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 | 158 | A → F: Decreased conductance, due to decreased diameter of the channel portal. 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 | 266 – 286 | ISFPY…EDKAA → HHHHHHLE: Normal levels of channels are expressed; they recover more slowly than wild-type cells after desensitization. 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
| 21 | |
| <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 | 266 – 286 | ISFPY…EDKAA → LE: Fewer channels present in the membrane, they require slightly more pressure to open and do not recover after desensitization. 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
| 21 | |
| <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 | 267 | S → C: Provides biochemical evidence for heptameric structure upon cross-linking. 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_0000110238 | 1 – 286 | Small-conductance mechanosensitive channelAdd BLAST | 286 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0C0S1 |
PRoteomics IDEntifications database More...PRIDEi | P0C0S1 |
<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.10"The closed structure of the MscS mechanosensitive channel. Cross-linking of single cysteine mutants."
Miller S., Edwards M.D., Ozdemir C., Booth I.R.
J. Biol. Chem. 278:32246-32250(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT IN THE CLOSED STATE, MUTAGENESIS OF SER-58 AND SER-267, DOMAIN. - Ref.12"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, SUBCELLULAR LOCATION. - Ref.15"Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel."
Bass R.B., Strop P., Barclay M., Rees D.C.
Science 298:1582-1587(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS) OF 27-280 PROBABLY IN THE OPEN STATE, SUBUNIT, FUNCTION, TOPOLOGY, DOMAIN. - Ref.16"Conformational state of the MscS mechanosensitive channel in solution revealed by pulsed electron-electron double resonance (PELDOR) spectroscopy."
Pliotas C., Ward R., Branigan E., Rasmussen A., Hagelueken G., Huang H., Black S.S., Booth I.R., Schiemann O., Naismith J.H.
Proc. Natl. Acad. Sci. U.S.A. 109:E2675-E2682(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (4.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY. - Ref.17"Structure and molecular mechanism of an anion-selective mechanosensitive channel of small conductance."
Zhang X., Wang J., Feng Y., Ge J., Li W., Sun W., Iscla I., Yu J., Blount P., Li Y., Yang M.
Proc. Natl. Acad. Sci. U.S.A. 109:18180-18185(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 272-286, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ALA-158. - Ref.18"Open and shut: crystal structures of the dodecylmaltoside solubilized mechanosensitive channel of small conductance from Escherichia coli and Helicobacter pylori at 4.4 A and 4.1 A resolutions."
Lai J.Y., Poon Y.S., Kaiser J.T., Rees D.C.
Protein Sci. 22:502-509(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (4.37 ANGSTROMS), SUBUNIT, TOPOLOGY. - Ref.19"The role of lipids in mechanosensation."
Pliotas C., Dahl A.C., Rasmussen T., Mahendran K.R., Smith T.K., Marius P., Gault J., Banda T., Rasmussen A., Miller S., Robinson C.V., Bayley H., Sansom M.S., Booth I.R., Naismith J.H.
Nat. Struct. Mol. Biol. 22:991-998(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS), FUNCTION, SUBUNIT, TOPOLOGY, DOMAIN.
<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 | 5 | EBI-554616,EBI-554616 |
<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 | 4259238, 255 interactors |
Database of interacting proteins More...DIPi | DIP-36192N |
Protein interaction database and analysis system More...IntActi | P0C0S1, 2 interactors |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_3099 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 22 – 58 | 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 | 37 | |
| <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 | 63 – 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 | 25 | |
| <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 | 88 – 90 | 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 | 93 – 127 | 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 | 35 | |
| <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 | 135 – 140 | 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 | 142 – 148 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 150 – 156 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 162 – 166 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 167 – 172 | 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 | 175 – 192 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 198 – 211 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 221 – 228 | 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 | 233 – 242 | 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 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 | 243 – 245 | 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 | 246 – 264 | 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 | 19 | |
| <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 | 272 – 279 | 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
| 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 |
| 2OAU | X-ray | 3.70 | A/B/C/D/E/F/G | 1-286 | [»] | |
| 2VV5 | X-ray | 3.45 | A/B/C/D/E/F/G | 1-286 | [»] | |
| 3UDC | X-ray | 3.36 | A/B/C/D/E/F/G | 272-286 | [»] | |
| 4AGE | X-ray | 4.84 | A/B/C/D/E/F/G | 1-286 | [»] | |
| 4AGF | X-ray | 4.70 | A/B/C/D/E/F/G | 1-286 | [»] | |
| 4HWA | X-ray | 4.37 | A/B/C/D/E/F/G | 1-286 | [»] | |
| 5AJI | X-ray | 2.99 | A/B/C/D/E/F/G | 1-286 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P0C0S1 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0C0S1 | |||||
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 | P0C0S1 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"C termini of the Escherichia coli mechanosensitive ion channel (MscS) move apart upon the channel opening."
Koprowski P., Kubalski A.
J. Biol. Chem. 278:11237-11245(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CROSS-LINKING OF THE C-TERMINI INHIBITS CHANNEL OPENING, DOMAIN, FUNCTION, SUBCELLULAR LOCATION. - Ref.10"The closed structure of the MscS mechanosensitive channel. Cross-linking of single cysteine mutants."
Miller S., Edwards M.D., Ozdemir C., Booth I.R.
J. Biol. Chem. 278:32246-32250(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT IN THE CLOSED STATE, MUTAGENESIS OF SER-58 AND SER-267, DOMAIN. - Ref.15"Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel."
Bass R.B., Strop P., Barclay M., Rees D.C.
Science 298:1582-1587(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS) OF 27-280 PROBABLY IN THE OPEN STATE, SUBUNIT, FUNCTION, TOPOLOGY, DOMAIN. - Ref.17"Structure and molecular mechanism of an anion-selective mechanosensitive channel of small conductance."
Zhang X., Wang J., Feng Y., Ge J., Li W., Sun W., Iscla I., Yu J., Blount P., Li Y., Yang M.
Proc. Natl. Acad. Sci. U.S.A. 109:18180-18185(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 272-286, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ALA-158. - Ref.19"The role of lipids in mechanosensation."
Pliotas C., Dahl A.C., Rasmussen T., Mahendran K.R., Smith T.K., Marius P., Gault J., Banda T., Rasmussen A., Miller S., Robinson C.V., Bayley H., Sansom M.S., Booth I.R., Naismith J.H.
Nat. Struct. Mol. Biol. 22:991-998(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS), FUNCTION, SUBUNIT, TOPOLOGY, DOMAIN.
<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>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 | ENOG4105D64 Bacteria COG0668 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000110050 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0C0S1 |
KEGG Orthology (KO) More...KOi | K03442 |
Identification of Orthologs from Complete Genome Data More...OMAi | IEDGIFN |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0C0S1 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.30.30.60, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR010920 LSM_dom_sf IPR011066 MscC_channel_C IPR006685 MscS_channel IPR006686 MscS_channel_CS IPR011014 MscS_channel_TM-2 IPR023408 MscS_dom_sf IPR008910 TM_helix |
Pfam protein domain database More...Pfami | View protein in Pfam PF00924 MS_channel, 1 hit PF05552 TM_helix, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50182 SSF50182, 1 hit SSF82689 SSF82689, 1 hit SSF82861 SSF82861, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS01246 UPF0003, 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
MEDLNVVDSI NGAGSWLVAN QALLLSYAVN IVAALAIIIV GLIIARMISN
60 70 80 90 100
AVNRLMISRK IDATVADFLS ALVRYGIIAF TLIAALGRVG VQTASVIAVL
110 120 130 140 150
GAAGLAVGLA LQGSLSNLAA GVLLVMFRPF RAGEYVDLGG VAGTVLSVQI
160 170 180 190 200
FSTTMRTADG KIIVIPNGKI IAGNIINFSR EPVRRNEFII GVAYDSDIDQ
210 220 230 240 250
VKQILTNIIQ SEDRILKDRE MTVRLNELGA SSINFVVRVW SNSGDLQNVY
260 270 280
WDVLERIKRE FDAAGISFPY PQMDVNFKRV KEDKAA
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 | X14436 Genomic DNA Translation: CAA32606.1 U28377 Genomic DNA Translation: AAA69091.1 U00096 Genomic DNA Translation: AAC75961.1 AP009048 Genomic DNA Translation: BAE76988.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S04735 QQEC4A |
NCBI Reference Sequences More...RefSeqi | NP_417399.1, NC_000913.3 WP_000389818.1, NZ_LN832404.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC75961; AAC75961; b2924 BAE76988; BAE76988; BAE76988 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 947416 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW2891 eco:b2924 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.3808 |
<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 | |
|---|---|---|---|---|---|
| P0C0S1 | Small-conductance mechanosensitive channel | 286 | |||
| Small-conductance mechanosensitive channel | 286 | ||||
| Mechanosensitive channel | 286 | ||||
| Small-conductance mechanosensitive channel | 286 | ||||
| Small-conductance mechanosensitive channel | 286 | ||||
| +504 | |||||
<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 | X14436 Genomic DNA Translation: CAA32606.1 U28377 Genomic DNA Translation: AAA69091.1 U00096 Genomic DNA Translation: AAC75961.1 AP009048 Genomic DNA Translation: BAE76988.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S04735 QQEC4A |
NCBI Reference Sequences More...RefSeqi | NP_417399.1, NC_000913.3 WP_000389818.1, 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 |
| 2OAU | X-ray | 3.70 | A/B/C/D/E/F/G | 1-286 | [»] | |
| 2VV5 | X-ray | 3.45 | A/B/C/D/E/F/G | 1-286 | [»] | |
| 3UDC | X-ray | 3.36 | A/B/C/D/E/F/G | 272-286 | [»] | |
| 4AGE | X-ray | 4.84 | A/B/C/D/E/F/G | 1-286 | [»] | |
| 4AGF | X-ray | 4.70 | A/B/C/D/E/F/G | 1-286 | [»] | |
| 4HWA | X-ray | 4.37 | A/B/C/D/E/F/G | 1-286 | [»] | |
| 5AJI | X-ray | 2.99 | A/B/C/D/E/F/G | 1-286 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P0C0S1 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0C0S1 | |||||
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 | 4259238, 255 interactors |
Database of interacting proteins More...DIPi | DIP-36192N |
Protein interaction database and analysis system More...IntActi | P0C0S1, 2 interactors |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_3099 |
Protein family/group databases
Transport Classification Database More...TCDBi | 1.A.23.2.1 the small conductance mechanosensitive ion channel (mscs) family |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0C0S1 |
PRoteomics IDEntifications database More...PRIDEi | P0C0S1 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC75961; AAC75961; b2924 BAE76988; BAE76988; BAE76988 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 947416 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW2891 eco:b2924 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.3808 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB1149 |
Escherichia coli strain K12 genome database More...EcoGenei | EG11160 mscS |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4105D64 Bacteria COG0668 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000110050 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0C0S1 |
KEGG Orthology (KO) More...KOi | K03442 |
Identification of Orthologs from Complete Genome Data More...OMAi | IEDGIFN |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0C0S1 |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG11160-MONOMER |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P0C0S1 |
Protein Ontology More...PROi | PR:P0C0S1 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.30.30.60, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR010920 LSM_dom_sf IPR011066 MscC_channel_C IPR006685 MscS_channel IPR006686 MscS_channel_CS IPR011014 MscS_channel_TM-2 IPR023408 MscS_dom_sf IPR008910 TM_helix |
Pfam protein domain database More...Pfami | View protein in Pfam PF00924 MS_channel, 1 hit PF05552 TM_helix, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50182 SSF50182, 1 hit SSF82689 SSF82689, 1 hit SSF82861 SSF82861, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS01246 UPF0003, 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 | MSCS_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 | P0C0S1Primary (citable) accession number: P0C0S1 Secondary accession number(s): P11666, Q2M9R8 | |
| <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: | December 6, 2005 |
| Last sequence update: | December 6, 2005 | |
| Last modified: | March 28, 2018 | |
| This is version 116 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
