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Database: UniProt
Entry: A0A1G3KET0_9SPHN
LinkDB: A0A1G3KET0_9SPHN
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ID   A0A1G3KET0_9SPHN        Unreviewed;       387 AA.
AC   A0A1G3KET0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Small-conductance mechanosensitive channel {ECO:0000256|RuleBase:RU369025};
GN   ORFNames=A3H25_08405 {ECO:0000313|EMBL:OHD03512.1};
OS   Sphingomonadales bacterium RIFCSPLOWO2_12_FULL_63_15.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales.
OX   NCBI_TaxID=1802170 {ECO:0000313|EMBL:OHD03512.1, ECO:0000313|Proteomes:UP000176465};
RN   [1] {ECO:0000313|EMBL:OHD03512.1, ECO:0000313|Proteomes:UP000176465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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: 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:OHD03512.1}.
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DR   EMBL; MIAK01000005; OHD03512.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G3KET0; -.
DR   Proteomes; UP000176465; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; 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:SF1; SMALL-CONDUCTANCE MECHANOSENSITIVE CHANNEL; 1.
DR   Pfam; PF21088; MS_channel_1st; 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   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        34..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369025"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369025"
FT   TRANSMEM        146..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369025"
FT   TRANSMEM        183..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369025"
FT   DOMAIN          157..197
FT                   /note="Mechanosensitive ion channel transmembrane helices
FT                   2/3"
FT                   /evidence="ECO:0000259|Pfam:PF21088"
FT   DOMAIN          199..261
FT                   /note="Mechanosensitive ion channel MscS"
FT                   /evidence="ECO:0000259|Pfam:PF00924"
FT   DOMAIN          271..355
FT                   /note="Mechanosensitive ion channel MscS C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21082"
SQ   SEQUENCE   387 AA;  42066 MW;  1424900FE845CC57 CRC64;
     MANTKTPADP VITVRPPDLG AMWRSTSDWL AVHYVQILIA IGVGVLIYLA LTALRGVGKR
     HKGTRGDPLG YANVLGRAAA RTTHFFMVMV AARLVAGYAD APAPLYKTIA FLFTIAAVWQ
     AALWAREIIL GLVERKTLAQ DGGGETLANA MGLIRLLVSV VLFAVATIVV LDNLGVNVTG
     LVAGLGIGGI AIGLAAQGIF SDLFAALSII FDKPFRRGET INYDMTTATV EKIGLKSTRL
     RAITGEKKVI SNANLLQKEI TSYFTLDHRR IKFAIGVIYQ TPPDVAEQIP EILKTIVTDL
     GANFVRSGFI SFGASSLDFE VEFDVYLPDW DAIYVIRHKV GLAILRQFNE RGIEFAYPTQ
     TSFTAAPDGR MVLPYPDVQA VRQVEKE
//
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