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Database: UniProt
Entry: F1W0V6_9BURK
LinkDB: F1W0V6_9BURK
Original site: F1W0V6_9BURK 
ID   F1W0V6_9BURK            Unreviewed;       288 AA.
AC   F1W0V6;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Small-conductance mechanosensitive channel {ECO:0000256|RuleBase:RU369025};
GN   ORFNames=IMCC9480_3812 {ECO:0000313|EMBL:EGF31516.1};
OS   Oxalobacteraceae bacterium IMCC9480.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae.
OX   NCBI_TaxID=937450 {ECO:0000313|EMBL:EGF31516.1, ECO:0000313|Proteomes:UP000004494};
RN   [1] {ECO:0000313|EMBL:EGF31516.1, ECO:0000313|Proteomes:UP000004494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC9480 {ECO:0000313|EMBL:EGF31516.1,
RC   ECO:0000313|Proteomes:UP000004494};
RX   PubMed=21572000; DOI=10.1128/JB.05088-11;
RA   Oh H.M., Lee K., Jang Y., Kang I., Kim H.J., Kang T.W., Kim S.Y., Cho J.C.;
RT   "Genome sequence of strain IMCC9480, a xanthorhodopsin-bearing
RT   betaproteobacterium isolated from the Arctic Ocean.";
RL   J. Bacteriol. 193:3421-3421(2011).
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:0000256|RuleBase:RU369025}.
CC   -!- SUBUNIT: Homoheptamer. {ECO:0000256|RuleBase:RU369025}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|RuleBase:RU369025}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU369025}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family.
CC       {ECO:0000256|ARBA:ARBA00008017, ECO:0000256|RuleBase:RU369025}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU369025}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGF31516.1}.
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DR   EMBL; AEPR01000418; EGF31516.1; -; Genomic_DNA.
DR   AlphaFoldDB; F1W0V6; -.
DR   OrthoDB; 9809206at2; -.
DR   Proteomes; UP000004494; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008381; F:mechanosensitive monoatomic ion channel activity; IEA:InterPro.
DR   Gene3D; 1.10.287.1260; -; 1.
DR   Gene3D; 2.30.30.60; -; 1.
DR   Gene3D; 3.30.70.100; -; 1.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR049142; MS_channel_1st.
DR   InterPro; IPR049278; MS_channel_C.
DR   InterPro; IPR008910; MSC_TM_helix.
DR   InterPro; IPR045275; MscS_archaea/bacteria_type.
DR   InterPro; IPR023408; MscS_beta-dom_sf.
DR   InterPro; IPR006685; MscS_channel_2nd.
DR   InterPro; IPR011066; MscS_channel_C_sf.
DR   InterPro; IPR011014; MscS_channel_TM-2.
DR   PANTHER; PTHR30221; SMALL-CONDUCTANCE MECHANOSENSITIVE CHANNEL; 1.
DR   PANTHER; PTHR30221:SF8; SMALL-CONDUCTANCE MECHANOSENSITIVE CHANNEL; 1.
DR   Pfam; PF21088; MS_channel_1st; 1.
DR   Pfam; PF05552; MS_channel_1st_1; 1.
DR   Pfam; PF00924; MS_channel_2nd; 1.
DR   Pfam; PF21082; MS_channel_3rd; 1.
DR   SUPFAM; SSF82689; Mechanosensitive channel protein MscS (YggB), C-terminal domain; 1.
DR   SUPFAM; SSF82861; Mechanosensitive channel protein MscS (YggB), transmembrane region; 1.
DR   SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|RuleBase:RU369025};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Ion channel {ECO:0000256|RuleBase:RU369025};
KW   Ion transport {ECO:0000256|RuleBase:RU369025};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU369025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004494};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU369025};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU369025}; Transport {ECO:0000256|RuleBase:RU369025}.
FT   TRANSMEM        20..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369025"
FT   TRANSMEM        65..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369025"
FT   TRANSMEM        89..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369025"
FT   DOMAIN          64..105
FT                   /note="Mechanosensitive ion channel transmembrane helices
FT                   2/3"
FT                   /evidence="ECO:0000259|Pfam:PF21088"
FT   DOMAIN          107..172
FT                   /note="Mechanosensitive ion channel MscS"
FT                   /evidence="ECO:0000259|Pfam:PF00924"
FT   DOMAIN          186..259
FT                   /note="Mechanosensitive ion channel MscS C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21082"
SQ   SEQUENCE   288 AA;  31297 MW;  E56B5001B65D6FC2 CRC64;
     MNDQIKHLID ILTGYLLSYG INVIGAIVTL IIGTLVAGWV ARLIDQAMRR SSRIDPVFHF
     LPGKIVRVAI LIFTLVAVLN RFGVETTSLI AVLGAAGLAV GLALQGTLSN VAAGVMILFF
     RPFKIGDVVQ LDSQVYIIDA VGFFICKGHL PDGPAVFIPN SKIWGQTIVN LSVTDNDIRR
     IDEGYGIAYT DSIPTALAIL QQIAAADPRI LATPAPLIKV DKLGESSVNI LFRVWTSRSD
     WWDTKLDLVQ RCKEGLEAGG CSLPYPQRDV HHFHEAGPVR KTGMTVGE
//
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