UniProtKB - P0C0S1 (MSCS_ECOLI)
Protein
Small-conductance mechanosensitive channel
Gene
mscS
Organism
Escherichia coli (strain K12)
Status
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 function | Ion channel |
Biological process | Ion transport, Transport |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11160-MONOMER |
Protein family/group databases
TCDBi | 1.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 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
- Cell inner membrane 7 Publications; Multi-pass membrane protein 5 Publications
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 30 | Periplasmic1 PublicationAdd BLAST | 30 | |
Transmembranei | 31 – 52 | Helical2 PublicationsAdd BLAST | 22 | |
Topological domaini | 53 – 67 | Cytoplasmic1 PublicationAdd BLAST | 15 | |
Transmembranei | 68 – 88 | Helical2 PublicationsAdd BLAST | 21 | |
Topological domaini | 89 – 90 | Periplasmic1 Publication | 2 | |
Transmembranei | 91 – 111 | Helical2 PublicationsAdd BLAST | 21 | |
Topological domaini | 112 – 286 | Cytoplasmic1 PublicationAdd BLAST | 175 |
GO - Cellular componenti
- integral component of membrane Source: EcoCyc
- integral component of plasma membrane Source: UniProtKB
Keywords - Cellular componenti
Cell inner membrane, Cell membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 40 | V → C, G or N: No detectable phenotype. 1 Publication | 1 | |
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 | 1 | |
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 | 1 | |
Mutagenesisi | 158 | A → F: Decreased conductance, due to decreased diameter of the channel portal. 1 Publication | 1 | |
Mutagenesisi | 266 – 286 | ISFPY…EDKAA → HHHHHHLE: Normal levels of channels are expressed; they recover more slowly than wild-type cells after desensitization. 1 PublicationAdd BLAST | 21 | |
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 PublicationAdd BLAST | 21 | |
Mutagenesisi | 267 | S → C: Provides biochemical evidence for heptameric structure upon cross-linking. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000110238 | 1 – 286 | Small-conductance mechanosensitive channelAdd BLAST | 286 |
Proteomic databases
jPOSTi | P0C0S1 |
PaxDbi | P0C0S1 |
PRIDEi | P0C0S1 |
Interactioni
Subunit structurei
Homoheptamer.
7 PublicationsBinary interactionsi
P0C0S1
With | #Exp. | IntAct |
---|---|---|
itself | 5 | EBI-554616,EBI-554616 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4259238, 255 interactors |
DIPi | DIP-36192N |
IntActi | P0C0S1, 2 interactors |
STRINGi | 511145.b2924 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0C0S1 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0C0S1 |
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 helixPhylogenomic databases
eggNOGi | COG0668, Bacteria |
HOGENOMi | CLU_037945_1_1_6 |
InParanoidi | P0C0S1 |
PhylomeDBi | P0C0S1 |
Family and domain databases
Gene3Di | 2.30.30.60, 1 hit |
InterProi | View protein in InterPro IPR010920, LSM_dom_sf IPR006685, MscS_channel IPR011066, MscS_channel_C IPR006686, MscS_channel_CS IPR011014, MscS_channel_TM-2 IPR023408, MscS_dom_sf IPR008910, TM_helix |
Pfami | View protein in Pfam PF00924, MS_channel, 1 hit PF05552, TM_helix, 1 hit |
SUPFAMi | SSF50182, SSF50182, 1 hit SSF82689, SSF82689, 1 hit SSF82861, SSF82861, 1 hit |
PROSITEi | View protein in PROSITE PS01246, UPF0003, 1 hit |
i Sequence
Sequence statusi: Complete.
P0C0S1-1 [UniParc]FASTAAdd to basket
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: 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 |
PIRi | S04735, QQEC4A |
RefSeqi | NP_417399.1, NC_000913.3 WP_000389818.1, NZ_STEB01000001.1 |
Genome annotation databases
EnsemblBacteriai | AAC75961; AAC75961; b2924 BAE76988; BAE76988; BAE76988 |
GeneIDi | 48134130 947416 |
KEGGi | ecj:JW2891 eco:b2924 |
PATRICi | fig|1411691.4.peg.3808 |
Similar proteinsi
Cross-referencesi
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 |
PIRi | S04735, QQEC4A |
RefSeqi | NP_417399.1, NC_000913.3 WP_000389818.1, NZ_STEB01000001.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links 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 | [»] | |
6PWN | electron microscopy | 3.10 | A/B/C/D/E/F/G | 1-286 | [»] | |
6PWO | electron microscopy | 3.40 | A/B/C/D/E/F/G | 1-286 | [»] | |
6PWP | electron microscopy | 4.10 | A/B/C/D/E/F/G | 1-286 | [»] | |
6RLD | electron microscopy | 2.93 | A/B/C/D/E/F/G | 1-286 | [»] | |
6UZH | electron microscopy | 3.30 | A/B/C/D/E/F/G | 1-286 | [»] | |
SMRi | P0C0S1 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4259238, 255 interactors |
DIPi | DIP-36192N |
IntActi | P0C0S1, 2 interactors |
STRINGi | 511145.b2924 |
Protein family/group databases
TCDBi | 1.A.23.2.1, the small conductance mechanosensitive ion channel (mscs) family |
Proteomic databases
jPOSTi | P0C0S1 |
PaxDbi | P0C0S1 |
PRIDEi | P0C0S1 |
Genome annotation databases
EnsemblBacteriai | AAC75961; AAC75961; b2924 BAE76988; BAE76988; BAE76988 |
GeneIDi | 48134130 947416 |
KEGGi | ecj:JW2891 eco:b2924 |
PATRICi | fig|1411691.4.peg.3808 |
Organism-specific databases
EchoBASEi | EB1149 |
Phylogenomic databases
eggNOGi | COG0668, Bacteria |
HOGENOMi | CLU_037945_1_1_6 |
InParanoidi | P0C0S1 |
PhylomeDBi | P0C0S1 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11160-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P0C0S1 |
PROi | PR:P0C0S1 |
Family and domain databases
Gene3Di | 2.30.30.60, 1 hit |
InterProi | View protein in InterPro IPR010920, LSM_dom_sf IPR006685, MscS_channel IPR011066, MscS_channel_C IPR006686, MscS_channel_CS IPR011014, MscS_channel_TM-2 IPR023408, MscS_dom_sf IPR008910, TM_helix |
Pfami | View protein in Pfam PF00924, MS_channel, 1 hit PF05552, TM_helix, 1 hit |
SUPFAMi | SSF50182, SSF50182, 1 hit SSF82689, SSF82689, 1 hit SSF82861, SSF82861, 1 hit |
PROSITEi | View protein in PROSITE PS01246, UPF0003, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | MSCS_ECOLI | |
Accessioni | P0C0S1Primary (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: | December 2, 2020 | |
This is version 132 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families