ID V4JC00_9GAMM Unreviewed; 514 AA.
AC V4JC00;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Small-conductance mechanosensitive channel {ECO:0000256|RuleBase:RU369025};
GN ORFNames=N838_17155 {ECO:0000313|EMBL:ESQ12014.1};
OS Thiohalocapsa sp. PB-PSB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiohalocapsa.
OX NCBI_TaxID=1385625 {ECO:0000313|EMBL:ESQ12014.1, ECO:0000313|Proteomes:UP000017935};
RN [1] {ECO:0000313|EMBL:ESQ12014.1, ECO:0000313|Proteomes:UP000017935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilbanks E.G., Jaekel U., Salman V., Humphrey P.T., Eisen J.A.,
RA Facciotti M.T., Buckley D.H., Zinder S.H., Druschel G.K., Fike D.A.,
RA Orphan V.J.;
RT "A sulfurous symbiosis: microscale sulfur cycling in the pink berry
RT consortia of the Sippewissett salt marsh.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family.
CC {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:ESQ12014.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AVFR01001042; ESQ12014.1; -; Genomic_DNA.
DR AlphaFoldDB; V4JC00; -.
DR PATRIC; fig|1385625.5.peg.6358; -.
DR Proteomes; UP000017935; 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 CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.287.1260; -; 1.
DR Gene3D; 2.30.30.60; -; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR010920; LSM_dom_sf.
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; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR30221; SMALL-CONDUCTANCE MECHANOSENSITIVE CHANNEL; 1.
DR PANTHER; PTHR30221:SF1; SMALL-CONDUCTANCE MECHANOSENSITIVE CHANNEL; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00924; MS_channel_2nd; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF82689; Mechanosensitive channel protein MscS (YggB), C-terminal domain; 1.
DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 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:UP000017935};
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 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369025"
FT TRANSMEM 46..69
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369025"
FT TRANSMEM 81..100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369025"
FT TRANSMEM 120..139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369025"
FT TRANSMEM 145..163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369025"
FT DOMAIN 354..457
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
SQ SEQUENCE 514 AA; 56995 MW; E5E6445E0580C211 CRC64;
MPQFIDSLAW DYWHLLLAAL MVYMAWHIGA HVVGERPLMN HFPRTAALLN VLMLPLSVIV
AGSLLRVANR KLGIPELDEE LSALTLLCTY LSTAWALARV VDVSLELKAE EEHGERVPKL
AVGLIYVLLL LLGLAVFLWQ QGYSFAGVWV STGVAAGVLG LALQKTLGDL FSGIALGLER
PFRLGDWIEL KDGTVGQVTD LNWRATRLRG WDNATHVIPN SSLASQSIRN LHGDDHLYAP
WYFIQIPADV DPRFANALLL QAAMRCESVL NFPNPIVRLA DASSLPYSYM VWVHLKNYPA
MFRGREELYR EIHRGLREAG IEVAPQVHEM RTRRASTIDS GLPTISLALK GLDFAGNLTD
EEIAQLAARS QYRYFDTGHV ILGETATSDA FYLIAGGLVD ARIRLPNGKL KVVETLVPGK
YFGITEMLVT EPSLLEFVAN TDVTLIRIDL DCVTDIISAR PELAEILSAV IKERLEAAEA
ARAASQQPTK RLTLTDIRLG VERRMRGPVW PPTP
//
