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Small-conductance mechanosensitive channel

 MSCS_ECOLI              Reviewed;         286 AA.
P0C0S1; P11666; Q2M9R8;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 1.
28-MAR-2018, entry version 116.
RecName: Full=Small-conductance mechanosensitive channel;
Name=mscS; Synonyms=yggB; OrderedLocusNames=b2924, JW2891;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / CS520;
PubMed=2546007; DOI=10.1111/j.1365-2958.1989.tb00221.x;
Alefounder P.R., Perham R.N.;
"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.";
Mol. Microbiol. 3:723-732(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=K12 / AW405;
PubMed=2436228; DOI=10.1073/pnas.84.8.2297;
Martinac B., Buechner M., Delcour A.H., Adler J., Kung C.;
"Pressure-sensitive ion channel in Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 84:2297-2301(1987).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND SENSITIVITY TO OSMOTIC AND VOLTAGE
DIFFERENCES ACROSS THE CYTOPLASMIC MEMBRANE.
STRAIN=K12;
PubMed=7595939; DOI=10.1007/BF00238414;
Cui C., Smith D.O., Adler J.;
"Characterization of mechanosensitive channels in Escherichia coli
cytoplasmic membrane by whole-cell patch clamp recording.";
J. Membr. Biol. 144:31-42(1995).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND PHYSIOLOGICAL ROLE.
STRAIN=K12 / MJF379;
PubMed=10202137; DOI=10.1093/emboj/18.7.1730;
Levina N., Toetemeyer S., Stokes N.R., Louis P., Jones M.A.,
Booth I.R.;
"Protection of Escherichia coli cells against extreme turgor by
activation of MscS and MscL mechanosensitive channels: identification
of genes required for MscS activity.";
EMBO J. 18:1730-1737(1999).
[7]
LIPOSOME RECONSTITUTION, AND FUNCTION.
STRAIN=K12 / AW405;
PubMed=12080120; DOI=10.1016/S0006-3495(02)75169-2;
Sukharev S.;
"Purification of the small mechanosensitive channel of Escherichia
coli (MscS): the subunit structure, conduction, and gating
characteristics in liposomes.";
Biophys. J. 83:290-298(2002).
[8]
LIPOSOME RECONSTITUTION, FUNCTION, AND MUTAGENESIS OF VAL-40.
STRAIN=K12 / MJF379;
PubMed=12015316; DOI=10.1074/jbc.M202497200;
Okada K., Moe P.C., Blount P.;
"Functional design of bacterial mechanosensitive channels. Comparisons
and contrasts illuminated by random mutagenesis.";
J. Biol. Chem. 277:27682-27688(2002).
[9]
CROSS-LINKING OF THE C-TERMINI INHIBITS CHANNEL OPENING, DOMAIN,
FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=K12 / MJF379;
PubMed=12551944; DOI=10.1074/jbc.M212073200;
Koprowski P., Kubalski A.;
"C termini of the Escherichia coli mechanosensitive ion channel (MscS)
move apart upon the channel opening.";
J. Biol. Chem. 278:11237-11245(2003).
[10]
SUBUNIT IN THE CLOSED STATE, MUTAGENESIS OF SER-58 AND SER-267, AND
DOMAIN.
PubMed=12767977; DOI=10.1074/jbc.M303188200;
Miller S., Edwards M.D., Ozdemir C., Booth I.R.;
"The closed structure of the MscS mechanosensitive channel. Cross-
linking of single cysteine mutants.";
J. Biol. Chem. 278:32246-32250(2003).
[11]
C-TERMINAL DELETIONS.
PubMed=15304354; DOI=10.1016/j.febslet.2004.07.045;
Schumann U., Edwards M.D., Li C., Booth I.R.;
"The conserved carboxy-terminus of the MscS mechanosensitive channel
is not essential but increases stability and activity.";
FEBS Lett. 572:233-237(2004).
[12]
SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BL21-DE3;
PubMed=16079137; DOI=10.1074/jbc.M506479200;
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
von Heijne G., Daley D.O.;
"Protein complexes of the Escherichia coli cell envelope.";
J. Biol. Chem. 280:34409-34419(2005).
[13]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[14]
3D-STRUCTURE MODELING, MUTAGENESIS OF CONSERVED GLY AND ALA RESIDUES
IN TM3, AND PRESENTATION OF MODELS OF THE CLOSED STATE CHANNEL AND
CLOSED TO OPEN STATE TRANSITIONS.
STRAIN=K12 / MJF431;
PubMed=15665866; DOI=10.1038/nsmb895;
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.;
"Pivotal role of the glycine-rich TM3 helix in gating the MscS
mechanosensitive channel.";
Nat. Struct. Mol. Biol. 12:113-119(2005).
[15]
X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS) OF 27-280 PROBABLY IN THE OPEN
STATE, SUBUNIT, FUNCTION, TOPOLOGY, AND DOMAIN.
STRAIN=K12;
PubMed=12446901; DOI=10.1126/science.1077945;
Bass R.B., Strop P., Barclay M., Rees D.C.;
"Crystal structure of Escherichia coli MscS, a voltage-modulated and
mechanosensitive channel.";
Science 298:1582-1587(2002).
[16]
X-RAY CRYSTALLOGRAPHY (4.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR
LOCATION, AND TOPOLOGY.
PubMed=23012406; DOI=10.1073/pnas.1202286109;
Pliotas C., Ward R., Branigan E., Rasmussen A., Hagelueken G.,
Huang H., Black S.S., Booth I.R., Schiemann O., Naismith J.H.;
"Conformational state of the MscS mechanosensitive channel in solution
revealed by pulsed electron-electron double resonance (PELDOR)
spectroscopy.";
Proc. Natl. Acad. Sci. U.S.A. 109:E2675-E2682(2012).
[17]
X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 272-286, FUNCTION, SUBUNIT,
SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF ALA-158.
PubMed=23074248; DOI=10.1073/pnas.1207977109;
Zhang X., Wang J., Feng Y., Ge J., Li W., Sun W., Iscla I., Yu J.,
Blount P., Li Y., Yang M.;
"Structure and molecular mechanism of an anion-selective
mechanosensitive channel of small conductance.";
Proc. Natl. Acad. Sci. U.S.A. 109:18180-18185(2012).
[18]
X-RAY CRYSTALLOGRAPHY (4.37 ANGSTROMS), SUBUNIT, AND TOPOLOGY.
PubMed=23339071; DOI=10.1002/pro.2222;
Lai J.Y., Poon Y.S., Kaiser J.T., Rees D.C.;
"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.";
Protein Sci. 22:502-509(2013).
[19]
X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS), FUNCTION, SUBUNIT, TOPOLOGY,
AND DOMAIN.
PubMed=26551077; DOI=10.1038/nsmb.3120;
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.;
"The role of lipids in mechanosensation.";
Nat. Struct. Mol. Biol. 22:991-998(2015).
-!- 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. 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. {ECO:0000269|PubMed:10202137,
ECO:0000269|PubMed:12015316, ECO:0000269|PubMed:12080120,
ECO:0000269|PubMed:12446901, ECO:0000269|PubMed:12551944,
ECO:0000269|PubMed:12767977, ECO:0000269|PubMed:23012406,
ECO:0000269|PubMed:23074248, ECO:0000269|PubMed:2436228,
ECO:0000269|PubMed:26551077, ECO:0000269|PubMed:7595939}.
-!- SUBUNIT: Homoheptamer. {ECO:0000269|PubMed:12446901,
ECO:0000269|PubMed:12767977, ECO:0000269|PubMed:16079137,
ECO:0000269|PubMed:23012406, ECO:0000269|PubMed:23074248,
ECO:0000269|PubMed:23339071, ECO:0000269|PubMed:26551077}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-554616, EBI-554616;
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:10202137, ECO:0000269|PubMed:12551944,
ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:23012406,
ECO:0000269|PubMed:23074248, ECO:0000269|PubMed:2436228,
ECO:0000269|PubMed:7595939}; Multi-pass membrane protein
{ECO:0000269|PubMed:12446901, ECO:0000269|PubMed:16079137,
ECO:0000269|PubMed:23012406, ECO:0000269|PubMed:23339071,
ECO:0000269|PubMed:26551077}.
-!- DOMAIN: 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.
{ECO:0000269|PubMed:12446901, ECO:0000269|PubMed:12551944,
ECO:0000269|PubMed:12767977, ECO:0000269|PubMed:23074248,
ECO:0000269|PubMed:26551077}.
-!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X14436; CAA32606.1; -; Genomic_DNA.
EMBL; U28377; AAA69091.1; -; Genomic_DNA.
EMBL; U00096; AAC75961.1; -; Genomic_DNA.
EMBL; AP009048; BAE76988.1; -; Genomic_DNA.
PIR; S04735; QQEC4A.
RefSeq; NP_417399.1; NC_000913.3.
RefSeq; WP_000389818.1; NZ_LN832404.1.
PDB; 2OAU; X-ray; 3.70 A; A/B/C/D/E/F/G=1-286.
PDB; 2VV5; X-ray; 3.45 A; A/B/C/D/E/F/G=1-286.
PDB; 3UDC; X-ray; 3.36 A; A/B/C/D/E/F/G=272-286.
PDB; 4AGE; X-ray; 4.84 A; A/B/C/D/E/F/G=1-286.
PDB; 4AGF; X-ray; 4.70 A; A/B/C/D/E/F/G=1-286.
PDB; 4HWA; X-ray; 4.37 A; A/B/C/D/E/F/G=1-286.
PDB; 5AJI; X-ray; 2.99 A; A/B/C/D/E/F/G=1-286.
PDBsum; 2OAU; -.
PDBsum; 2VV5; -.
PDBsum; 3UDC; -.
PDBsum; 4AGE; -.
PDBsum; 4AGF; -.
PDBsum; 4HWA; -.
PDBsum; 5AJI; -.
ProteinModelPortal; P0C0S1; -.
SMR; P0C0S1; -.
BioGrid; 4259238; 255.
DIP; DIP-36192N; -.
IntAct; P0C0S1; 2.
STRING; 316385.ECDH10B_3099; -.
TCDB; 1.A.23.2.1; the small conductance mechanosensitive ion channel (mscs) family.
PaxDb; P0C0S1; -.
PRIDE; P0C0S1; -.
EnsemblBacteria; AAC75961; AAC75961; b2924.
EnsemblBacteria; BAE76988; BAE76988; BAE76988.
GeneID; 947416; -.
KEGG; ecj:JW2891; -.
KEGG; eco:b2924; -.
PATRIC; fig|1411691.4.peg.3808; -.
EchoBASE; EB1149; -.
EcoGene; EG11160; mscS.
eggNOG; ENOG4105D64; Bacteria.
eggNOG; COG0668; LUCA.
HOGENOM; HOG000110050; -.
InParanoid; P0C0S1; -.
KO; K03442; -.
OMA; IEDGIFN; -.
PhylomeDB; P0C0S1; -.
BioCyc; EcoCyc:EG11160-MONOMER; -.
EvolutionaryTrace; P0C0S1; -.
PRO; PR:P0C0S1; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016021; C:integral component of membrane; IDA:EcoCyc.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008381; F:mechanosensitive ion channel activity; IDA:UniProtKB.
GO; GO:0009992; P:cellular water homeostasis; IMP:EcoCyc.
GO; GO:0034220; P:ion transmembrane transport; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
Gene3D; 2.30.30.60; -; 1.
InterPro; IPR010920; LSM_dom_sf.
InterPro; IPR011066; MscC_channel_C.
InterPro; IPR006685; MscS_channel.
InterPro; IPR006686; MscS_channel_CS.
InterPro; IPR011014; MscS_channel_TM-2.
InterPro; IPR023408; MscS_dom_sf.
InterPro; IPR008910; TM_helix.
Pfam; PF00924; MS_channel; 1.
Pfam; PF05552; TM_helix; 1.
SUPFAM; SSF50182; SSF50182; 1.
SUPFAM; SSF82689; SSF82689; 1.
SUPFAM; SSF82861; SSF82861; 1.
PROSITE; PS01246; UPF0003; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
Ion channel; Ion transport; Membrane; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 286 Small-conductance mechanosensitive
channel.
/FTId=PRO_0000110238.
TOPO_DOM 1 30 Periplasmic.
{ECO:0000305|PubMed:15919996}.
TRANSMEM 31 52 Helical. {ECO:0000269|PubMed:12446901,
ECO:0000269|PubMed:26551077}.
TOPO_DOM 53 67 Cytoplasmic.
{ECO:0000305|PubMed:15919996}.
TRANSMEM 68 88 Helical. {ECO:0000269|PubMed:12446901,
ECO:0000269|PubMed:26551077}.
TOPO_DOM 89 90 Periplasmic.
{ECO:0000305|PubMed:15919996}.
TRANSMEM 91 111 Helical. {ECO:0000269|PubMed:12446901,
ECO:0000269|PubMed:26551077}.
TOPO_DOM 112 286 Cytoplasmic.
{ECO:0000305|PubMed:15919996}.
MUTAGEN 40 40 V->C,G,N: No detectable phenotype.
{ECO:0000269|PubMed:12015316}.
MUTAGEN 40 40 V->D,K: Normal growth stops, without cell
death, due to increased membrane
permeability to potassium ions and
protons (permeability tested only for D
substitutions).
{ECO:0000269|PubMed:12015316}.
MUTAGEN 58 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.
{ECO:0000269|PubMed:12767977}.
MUTAGEN 158 158 A->F: Decreased conductance, due to
decreased diameter of the channel portal.
{ECO:0000269|PubMed:23074248}.
MUTAGEN 266 286 ISFPYPQMDVNFKRVKEDKAA->HHHHHHLE: Normal
levels of channels are expressed; they
recover more slowly than wild-type cells
after desensitization.
{ECO:0000269|PubMed:15665866}.
MUTAGEN 266 286 ISFPYPQMDVNFKRVKEDKAA->LE: Fewer channels
present in the membrane, they require
slightly more pressure to open and do not
recover after desensitization.
{ECO:0000269|PubMed:15665866}.
MUTAGEN 267 267 S->C: Provides biochemical evidence for
heptameric structure upon cross-linking.
{ECO:0000269|PubMed:12767977}.
HELIX 22 58 {ECO:0000244|PDB:5AJI}.
HELIX 63 87 {ECO:0000244|PDB:5AJI}.
TURN 88 90 {ECO:0000244|PDB:5AJI}.
HELIX 93 127 {ECO:0000244|PDB:5AJI}.
STRAND 135 140 {ECO:0000244|PDB:5AJI}.
STRAND 142 148 {ECO:0000244|PDB:5AJI}.
STRAND 150 156 {ECO:0000244|PDB:5AJI}.
STRAND 162 166 {ECO:0000244|PDB:5AJI}.
HELIX 167 172 {ECO:0000244|PDB:5AJI}.
STRAND 175 192 {ECO:0000244|PDB:5AJI}.
HELIX 198 211 {ECO:0000244|PDB:5AJI}.
STRAND 221 228 {ECO:0000244|PDB:5AJI}.
STRAND 233 242 {ECO:0000244|PDB:5AJI}.
TURN 243 245 {ECO:0000244|PDB:5AJI}.
HELIX 246 264 {ECO:0000244|PDB:5AJI}.
STRAND 272 279 {ECO:0000244|PDB:5AJI}.
SEQUENCE 286 AA; 30896 MW; FF00AD64F795E9FE CRC64;
MEDLNVVDSI NGAGSWLVAN QALLLSYAVN IVAALAIIIV GLIIARMISN AVNRLMISRK
IDATVADFLS ALVRYGIIAF TLIAALGRVG VQTASVIAVL GAAGLAVGLA LQGSLSNLAA
GVLLVMFRPF RAGEYVDLGG VAGTVLSVQI FSTTMRTADG KIIVIPNGKI IAGNIINFSR
EPVRRNEFII GVAYDSDIDQ VKQILTNIIQ SEDRILKDRE MTVRLNELGA SSINFVVRVW
SNSGDLQNVY WDVLERIKRE FDAAGISFPY PQMDVNFKRV KEDKAA


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