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P0C0S1

- MSCS_ECOLI

UniProt

P0C0S1 - MSCS_ECOLI

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Protein

Small-conductance mechanosensitive channel

Gene

mscS

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. The channel is sensitive to voltage; as the membrane is depolarized, less tension is required to open the channel and vice versa. The channel is characterized by short bursts of activity that last for a few seconds.
The channel pore is formed by TM3 and the loop between TM2 and TM3. After a sharp turn at Gly-113, an alpha-helix (residues 114-127) is oriented nearly parallel to the plane of the putative lipid bilayer. On the intracellular side of the channel, the permeation pathway of MscS does not connect directly to the cytoplasm but instead opens to a large chamber that is connected to the cytoplasm. This chamber resembles a molecular filter that could serve to prescreen large molecules before they are allowed passage to the transmembrane pore. The TM1 and TM2 helices appear to be likely candidates for mediating the tension and voltage sensitivities of MscS. Gating requires large rearrangements of at least the C-terminus.

GO - Molecular functioni

  1. mechanically-gated ion channel activity Source: EcoCyc

GO - Biological processi

  1. cellular water homeostasis Source: EcoCyc
  2. ion transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EG11160-MONOMER.
ECOL316407:JW2891-MONOMER.
RETL1328306-WGS:GSTH-1410-MONOMER.

Protein family/group databases

TCDBi1.A.23.2.1. the small conductance mechanosensitive ion channel (mscs) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Small-conductance mechanosensitive channel
Gene namesi
Name:mscS
Synonyms:yggB
Ordered Locus Names:b2924, JW2891
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11160. mscS.

Subcellular locationi

Cell inner membrane 1 Publication; Multi-pass membrane protein 1 Publication

GO - Cellular componenti

  1. integral component of membrane Source: EcoCyc
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401V → C, G or N: No detectable phenotype. 1 Publication
Mutagenesisi40 – 401V → 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
Mutagenesisi58 – 581S → 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
Mutagenesisi266 – 28621ISFPY…EDKAA → HHHHHHLE: Normal levels of channels are expressed; they recover more slowly than wild-type cells after desensitization. 1 PublicationAdd
BLAST
Mutagenesisi266 – 28621ISFPY…EDKAA → LE: Fewer channels present in the membrane, they require slightly more pressure to open and do not recover after desensitization. 1 PublicationAdd
BLAST
Mutagenesisi267 – 2671S → C: Provides biochemical evidence for heptameric structure upon cross-linking. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 286286Small-conductance mechanosensitive channelPRO_0000110238Add
BLAST

Proteomic databases

PaxDbiP0C0S1.
PRIDEiP0C0S1.

Expressioni

Gene expression databases

GenevestigatoriP0C0S1.

Interactioni

Subunit structurei

Homoheptamer.3 Publications

Protein-protein interaction databases

DIPiDIP-36192N.
IntActiP0C0S1. 2 interactions.
STRINGi511145.b2924.

Structurei

Secondary structure

1
286
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 283
Helixi30 – 5930
Helixi63 – 8725
Turni88 – 903
Helixi96 – 11116
Helixi113 – 12513
Beta strandi135 – 1406
Beta strandi142 – 1487
Beta strandi150 – 1567
Beta strandi162 – 1665
Helixi167 – 1715
Beta strandi175 – 19218
Helixi198 – 21114
Beta strandi221 – 2288
Beta strandi230 – 24213
Turni243 – 2453
Helixi246 – 26419
Beta strandi274 – 2796

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OAUX-ray3.70A/B/C/D/E/F/G1-286[»]
2VV5X-ray3.45A/B/C/D/E/F/G1-286[»]
3UDCX-ray3.36A/B/C/D/E/F/G272-286[»]
4AGEX-ray4.84A/B/C/D/E/F/G1-286[»]
4AGFX-ray4.70A/B/C/D/E/F/G1-286[»]
4HWAX-ray4.37A/B/C/D/E/F/G1-286[»]
ProteinModelPortaliP0C0S1.
SMRiP0C0S1. Positions 27-280.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0S1.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2828Periplasmic1 PublicationAdd
BLAST
Topological domaini58 – 6710Cytoplasmic1 Publication
Topological domaini92 – 954Periplasmic1 Publication
Topological domaini114 – 286173Cytoplasmic1 PublicationAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei29 – 5729HelicalAdd
BLAST
Transmembranei68 – 9124HelicalAdd
BLAST
Transmembranei96 – 11318HelicalAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0668.
HOGENOMiHOG000110050.
InParanoidiP0C0S1.
KOiK03442.
OMAiILYISEY.
OrthoDBiEOG61GG69.
PhylomeDBiP0C0S1.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR011066. MscC_channel_C.
IPR006685. MscS_channel.
IPR006686. MscS_channel_CS.
IPR011014. MscS_channel_TM-2.
IPR008910. TM_helix.
[Graphical view]
PfamiPF00924. MS_channel. 1 hit.
PF05552. TM_helix. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.
SSF82689. SSF82689. 1 hit.
SSF82861. SSF82861. 1 hit.
PROSITEiPS01246. UPF0003. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C0S1-1 [UniParc]FASTAAdd to Basket

« Hide

        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
Length:286
Mass (Da):30,896
Last modified:December 6, 2005 - v1
Checksum:iFF00AD64F795E9FE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links 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.
PIRiS04735. QQEC4A.
RefSeqiNP_417399.1. NC_000913.3.
YP_491124.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75961; AAC75961; b2924.
BAE76988; BAE76988; BAE76988.
GeneIDi12930244.
947416.
KEGGiecj:Y75_p2855.
eco:b2924.
PATRICi32121262. VBIEscCol129921_3019.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links 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 .
PIRi S04735. QQEC4A.
RefSeqi NP_417399.1. NC_000913.3.
YP_491124.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P0C0S1.
SMRi P0C0S1. Positions 27-280.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-36192N.
IntActi P0C0S1. 2 interactions.
STRINGi 511145.b2924.

Protein family/group databases

TCDBi 1.A.23.2.1. the small conductance mechanosensitive ion channel (mscs) family.

Proteomic databases

PaxDbi P0C0S1.
PRIDEi P0C0S1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75961 ; AAC75961 ; b2924 .
BAE76988 ; BAE76988 ; BAE76988 .
GeneIDi 12930244.
947416.
KEGGi ecj:Y75_p2855.
eco:b2924.
PATRICi 32121262. VBIEscCol129921_3019.

Organism-specific databases

EchoBASEi EB1149.
EcoGenei EG11160. mscS.

Phylogenomic databases

eggNOGi COG0668.
HOGENOMi HOG000110050.
InParanoidi P0C0S1.
KOi K03442.
OMAi ILYISEY.
OrthoDBi EOG61GG69.
PhylomeDBi P0C0S1.

Enzyme and pathway databases

BioCyci EcoCyc:EG11160-MONOMER.
ECOL316407:JW2891-MONOMER.
RETL1328306-WGS:GSTH-1410-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0C0S1.
PROi P0C0S1.

Gene expression databases

Genevestigatori P0C0S1.

Family and domain databases

InterProi IPR010920. LSM_dom.
IPR011066. MscC_channel_C.
IPR006685. MscS_channel.
IPR006686. MscS_channel_CS.
IPR011014. MscS_channel_TM-2.
IPR008910. TM_helix.
[Graphical view ]
Pfami PF00924. MS_channel. 1 hit.
PF05552. TM_helix. 1 hit.
[Graphical view ]
SUPFAMi SSF50182. SSF50182. 1 hit.
SSF82689. SSF82689. 1 hit.
SSF82861. SSF82861. 1 hit.
PROSITEi PS01246. UPF0003. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli."
    Alefounder P.R., Perham R.N.
    Mol. Microbiol. 3:723-732(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / CS520.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: CHARACTERIZATION.
    Strain: K12 / AW405.
  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: SENSITIVITY TO OSMOTIC AND VOLTAGE DIFFERENCES ACROSS THE CYTOPLASMIC MEMBRANE.
    Strain: K12.
  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: CHARACTERIZATION, PHYIOLOGICAL ROLE.
    Strain: K12 / MJF379.
  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.
    Strain: K12 / AW405.
  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, MUTAGENESIS OF VAL-40.
    Strain: K12 / MJF379.
  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.
    Strain: K12 / MJF379.
  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.
  11. "The conserved carboxy-terminus of the MscS mechanosensitive channel is not essential but increases stability and activity."
    Schumann U., Edwards M.D., Li C., Booth I.R.
    FEBS Lett. 572:233-237(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: C-TERMINAL DELETIONS.
  12. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BL21-DE3.
  13. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  14. "Pivotal role of the glycine-rich TM3 helix in gating the MscS mechanosensitive channel."
    Edwards M.D., Li Y., Kim S., Miller S., Bartlett W., Black S., Dennison S., Iscla I., Blount P., Bowie J.U., Booth I.R.
    Nat. Struct. Mol. Biol. 12:113-119(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CONSERVED GLY AND ALA RESIDUES IN TM3, PRESENTATION OF MODELS OF THE CLOSED STATE CHANNEL AND CLOSED TO OPEN STATE TRANSITIONS.
    Strain: K12 / MJF431.
  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.
    Strain: K12.

Entry informationi

Entry nameiMSCS_ECOLI
AccessioniPrimary (citable) accession number: P0C0S1
Secondary accession number(s): P11666, Q2M9R8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: October 29, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3