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Protein

Small-conductance mechanosensitive channel

Gene

mscS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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. Contributes to normal resistance to hypoosmotic shock. 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.11 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • mechanosensitive ion channel activity Source: UniProtKB

GO - Biological processi

  • cellular water homeostasis Source: EcoCyc
  • ion transmembrane transport Source: UniProtKB
  • protein homooligomerization Source: UniProtKB

Keywordsi

Molecular functionIon channel
Biological processIon transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EG11160-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11160 mscS

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 30Periplasmic1 PublicationAdd BLAST30
Transmembranei31 – 52Helical2 PublicationsAdd BLAST22
Topological domaini53 – 67Cytoplasmic1 PublicationAdd BLAST15
Transmembranei68 – 88Helical2 PublicationsAdd BLAST21
Topological domaini89 – 90Periplasmic1 Publication2
Transmembranei91 – 111Helical2 PublicationsAdd BLAST21
Topological domaini112 – 286Cytoplasmic1 PublicationAdd BLAST175

GO - Cellular componenti

  • integral component of membrane Source: EcoCyc
  • integral component of plasma membrane Source: UniProtKB

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi40V → C, G or N: No detectable phenotype. 1 Publication1
Mutagenesisi40V → 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 Publication1
Mutagenesisi58S → 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 Publication1
Mutagenesisi158A → F: Decreased conductance, due to decreased diameter of the channel portal. 1 Publication1
Mutagenesisi266 – 286ISFPY…EDKAA → HHHHHHLE: Normal levels of channels are expressed; they recover more slowly than wild-type cells after desensitization. 1 PublicationAdd BLAST21
Mutagenesisi266 – 286ISFPY…EDKAA → LE: Fewer channels present in the membrane, they require slightly more pressure to open and do not recover after desensitization. 1 PublicationAdd BLAST21
Mutagenesisi267S → C: Provides biochemical evidence for heptameric structure upon cross-linking. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001102381 – 286Small-conductance mechanosensitive channelAdd BLAST286

Proteomic databases

PaxDbiP0C0S1
PRIDEiP0C0S1

Interactioni

Subunit structurei

Homoheptamer.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-554616,EBI-554616

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4259238, 255 interactors
DIPiDIP-36192N
IntActiP0C0S1, 2 interactors
STRINGi316385.ECDH10B_3099

Structurei

Secondary structure

1286
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi22 – 58Combined sources37
Helixi63 – 87Combined sources25
Turni88 – 90Combined sources3
Helixi93 – 127Combined sources35
Beta strandi135 – 140Combined sources6
Beta strandi142 – 148Combined sources7
Beta strandi150 – 156Combined sources7
Beta strandi162 – 166Combined sources5
Helixi167 – 172Combined sources6
Beta strandi175 – 192Combined sources18
Helixi198 – 211Combined sources14
Beta strandi221 – 228Combined sources8
Beta strandi233 – 242Combined sources10
Turni243 – 245Combined sources3
Helixi246 – 264Combined sources19
Beta strandi272 – 279Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5AJIX-ray2.99A/B/C/D/E/F/G1-286[»]
ProteinModelPortaliP0C0S1
SMRiP0C0S1
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0S1

Family & Domainsi

Domaini

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, and is probably influenced by freely exchangeable membrane lipids that bind in grooves and pockets between the transmembrane helices and enhance the stability of the closed channel conformation. In a hypoosmotic environment the membrane is stretched, and lipids may be pulled into the lipid bilayer and away from the protein, which is predicted to destabilize the closed conformation and promote channel gating.5 Publications

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105D64 Bacteria
COG0668 LUCA
HOGENOMiHOG000110050
InParanoidiP0C0S1
KOiK03442
OMAiIEDGIFN
PhylomeDBiP0C0S1

Family and domain databases

Gene3Di2.30.30.60, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF00924 MS_channel, 1 hit
PF05552 TM_helix, 1 hit
SUPFAMiSSF50182 SSF50182, 1 hit
SSF82689 SSF82689, 1 hit
SSF82861 SSF82861, 1 hit
PROSITEiView protein in PROSITE
PS01246 UPF0003, 1 hit

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:
EMBLi
GenBanki
DDBJi
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
WP_000389818.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75961; AAC75961; b2924
BAE76988; BAE76988; BAE76988
GeneIDi947416
KEGGiecj:JW2891
eco:b2924
PATRICifig|1411691.4.peg.3808

Similar proteinsi

Entry informationi

Entry nameiMSCS_ECOLI
AccessioniPrimary (citable) accession number: P0C0S1
Secondary accession number(s): P11666, Q2M9R8
Entry historyiIntegrated 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.
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

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