Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0C0S1 (MSCS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Small-conductance mechanosensitive channel
Gene names
Name:mscS
Synonyms:yggB
Ordered Locus Names:b2924, JW2891
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Homoheptamer. Ref.10 Ref.12 Ref.15

Subcellular location

Cell inner membrane; Multi-pass membrane protein Ref.12.

Sequence similarities

Belongs to the MscS (TC 1.A.23) family. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 286286Small-conductance mechanosensitive channel
PRO_0000110238

Regions

Topological domain1 – 2828Periplasmic Probable
Transmembrane29 – 5729Helical
Topological domain58 – 6710Cytoplasmic Probable
Transmembrane68 – 9124Helical
Topological domain92 – 954Periplasmic Probable
Transmembrane96 – 11318Helical
Topological domain114 – 286173Cytoplasmic Probable

Experimental info

Mutagenesis401V → C, G or N: No detectable phenotype. Ref.8 Ref.14
Mutagenesis401V → 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). Ref.8 Ref.14
Mutagenesis581S → 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. Ref.10 Ref.14
Mutagenesis266 – 28621ISFPY…EDKAA → HHHHHHLE: Normal levels of channels are expressed; they recover more slowly than wild-type cells after desensitization. Ref.14
Mutagenesis266 – 28621ISFPY…EDKAA → LE: Fewer channels present in the membrane, they require slightly more pressure to open and do not recover after desensitization. Ref.14
Mutagenesis2671S → C: Provides biochemical evidence for heptameric structure upon cross-linking. Ref.10 Ref.14

Secondary structure

................................. 286
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C0S1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: FF00AD64F795E9FE

FASTA28630,896
        10         20         30         40         50         60 
MEDLNVVDSI NGAGSWLVAN QALLLSYAVN IVAALAIIIV GLIIARMISN AVNRLMISRK 

        70         80         90        100        110        120 
IDATVADFLS ALVRYGIIAF TLIAALGRVG VQTASVIAVL GAAGLAVGLA LQGSLSNLAA 

       130        140        150        160        170        180 
GVLLVMFRPF RAGEYVDLGG VAGTVLSVQI FSTTMRTADG KIIVIPNGKI IAGNIINFSR 

       190        200        210        220        230        240 
EPVRRNEFII GVAYDSDIDQ VKQILTNIIQ SEDRILKDRE MTVRLNELGA SSINFVVRVW 

       250        260        270        280 
SNSGDLQNVY WDVLERIKRE FDAAGISFPY PQMDVNFKRV KEDKAA 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"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: 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]"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.
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14436 Genomic DNA. Translation: CAA32606.1.
U28377 Genomic DNA. Translation: AAA69091.1.
U00096 Genomic DNA. Translation: AAC75961.1.
AP009048 Genomic DNA. Translation: BAE76988.1.
PIRQQEC4A. S04735.
RefSeqNP_417399.1. NC_000913.3.
YP_491124.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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/G266-286[»]
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[»]
ProteinModelPortalP0C0S1.
SMRP0C0S1. Positions 27-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36192N.
IntActP0C0S1. 2 interactions.
STRING511145.b2924.

Protein family/group databases

TCDB1.A.23.2.1. the small conductance mechanosensitive ion channel (mscs) family.

Proteomic databases

PaxDbP0C0S1.
PRIDEP0C0S1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75961; AAC75961; b2924.
BAE76988; BAE76988; BAE76988.
GeneID12930244.
947416.
KEGGecj:Y75_p2855.
eco:b2924.
PATRIC32121262. VBIEscCol129921_3019.

Organism-specific databases

EchoBASEEB1149.
EcoGeneEG11160. mscS.

Phylogenomic databases

eggNOGCOG0668.
HOGENOMHOG000110050.
KOK03442.
OMAWANMAAG.
OrthoDBEOG61GG69.
PhylomeDBP0C0S1.
ProtClustDBPRK10334.

Enzyme and pathway databases

BioCycEcoCyc:EG11160-MONOMER.
ECOL316407:JW2891-MONOMER.

Gene expression databases

GenevestigatorP0C0S1.

Family and domain databases

InterProIPR010920. LSM_dom.
IPR011066. MscC_channel_C.
IPR006685. MscS_channel.
IPR006686. MscS_channel_CS.
IPR011014. MscS_channel_TM-2.
IPR008910. TM_helix.
[Graphical view]
PfamPF00924. MS_channel. 1 hit.
PF05552. TM_helix. 1 hit.
[Graphical view]
SUPFAMSSF50182. SSF50182. 1 hit.
SSF82689. SSF82689. 1 hit.
SSF82861. SSF82861. 1 hit.
PROSITEPS01246. UPF0003. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0C0S1.
PROP0C0S1.

Entry information

Entry nameMSCS_ECOLI
AccessionPrimary (citable) accession number: P0C0S1
Secondary accession number(s): P11666, Q2M9R8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene