ID   MSCS_HELPX              Reviewed;         274 AA.
AC   T0DVE4;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Small-conductance mechanosensitive channel;
GN   Name=mscS; ORFNames=N203_05530 {ECO:0000312|EMBL:EPZ73970.1};
OS   Helicobacter pylori (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=210;
RN   [1] {ECO:0000312|EMBL:EPZ73970.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UM084 {ECO:0000312|EMBL:EPZ73970.1};
RX   PubMed=24051312; DOI=10.1128/genomea.00687-13;
RA   Rehvathy V., Tan M.H., Gunaletchumy S.P., Teh X., Wang S., Baybayan P.,
RA   Singh S., Ashby M., Kaakoush N.O., Mitchell H.M., Croft L.J., Goh K.L.,
RA   Loke M.F., Vadivelu J.;
RT   "Multiple genome sequences of Helicobacter pylori strains of diverse
RT   disease and antibiotic resistance backgrounds from malaysia.";
RL   Genome Announc. 1:E00687-E00713(2013).
RN   [2] {ECO:0007744|PDB:4HW9}
RP   X-RAY CRYSTALLOGRAPHY (4.14 ANGSTROMS), TOPOLOGY, AND SUBUNIT.
RX   PubMed=23339071; DOI=10.1002/pro.2222;
RA   Lai J.Y., Poon Y.S., Kaiser J.T., Rees D.C.;
RT   "Open and shut: crystal structures of the dodecylmaltoside solubilized
RT   mechanosensitive channel of small conductance from Escherichia coli and
RT   Helicobacter pylori at 4.4 A and 4.1 A resolutions.";
RL   Protein Sci. 22:502-509(2013).
CC   -!- FUNCTION: Mechanosensitive channel that participates in the regulation
CC       of osmotic pressure changes within the cell, opening in response to
CC       stretch forces in the membrane lipid bilayer, without the need for
CC       other proteins. Contributes to normal resistance to hypoosmotic shock.
CC       Forms an ion channel of 1.0 nanosiemens conductance with a slight
CC       preference for anions. {ECO:0000250|UniProtKB:P0C0S1}.
CC   -!- SUBUNIT: Homoheptamer. {ECO:0000269|PubMed:23339071}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P0C0S1}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:23339071}.
CC   -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}.
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DR   EMBL; AUSO01000002; EPZ73970.1; -; Genomic_DNA.
DR   RefSeq; WP_021304837.1; NZ_RJHH01000009.1.
DR   PDB; 4HW9; X-ray; 4.14 A; A/B/C/D/E/F/G=1-272.
DR   PDBsum; 4HW9; -.
DR   AlphaFoldDB; T0DVE4; -.
DR   SMR; T0DVE4; -.
DR   STRING; 1345592.CBOM010000016_gene1203; -.
DR   EnsemblBacteria; EPZ73970; EPZ73970; N203_05530.
DR   PATRIC; fig|1355530.3.peg.203; -.
DR   eggNOG; COG0668; Bacteria.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008381; F:mechanosensitive ion channel activity; IEA:InterPro.
DR   Gene3D; 2.30.30.60; -; 1.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR045275; MscS_archaea/bacteria_type.
DR   InterPro; IPR006685; MscS_channel.
DR   InterPro; IPR011066; MscS_channel_C.
DR   InterPro; IPR011014; MscS_channel_TM-2.
DR   InterPro; IPR023408; MscS_dom_sf.
DR   PANTHER; PTHR30221; PTHR30221; 1.
DR   Pfam; PF00924; MS_channel; 1.
DR   SUPFAM; SSF50182; SSF50182; 1.
DR   SUPFAM; SSF82689; SSF82689; 1.
DR   SUPFAM; SSF82861; SSF82861; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Ion channel;
KW   Ion transport; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..274
FT                   /note="Small-conductance mechanosensitive channel"
FT                   /id="PRO_0000440565"
FT   TOPO_DOM        1..21
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:23339071"
FT   TRANSMEM        22..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:23339071"
FT   TOPO_DOM        45..56
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:23339071"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:23339071"
FT   TOPO_DOM        78..79
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:23339071"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:23339071"
FT   TOPO_DOM        101..274
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:23339071"
SQ   SEQUENCE   274 AA;  30402 MW;  2CA167714FDD34E6 CRC64;
     MDEIKTLLVD FFPQAKHFGI ILIKAVIVFC IGFYFSFFLR NKTMKLLSKK DEILANFVAQ
     VTFILILIIT TIIALSTLGV QTTSIITVLG TVGIAVALAL KDYLSSIAGG IILIILHPFK
     KGDIIEISGL EGKVEALNFF NTSLRLHDGR LAVLPNRSVA NSNIINSNNT ACRRIEWVCG
     VGYGSDIELV HKTIKDVIDT MEKIDKNMPT FIGITDFGSS SLNFTIRVWA KIEDGIFNVR
     SELIERIKNA LDANHIEIPF NKLDIAIKNQ DSSK