ID A0A1H7N378_9RHOB Unreviewed; 455 AA.
AC A0A1H7N378;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Small-conductance mechanosensitive channel {ECO:0000256|RuleBase:RU369025};
GN ORFNames=SAMN04488526_2152 {ECO:0000313|EMBL:SEL17923.1};
OS Jannaschia helgolandensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=188906 {ECO:0000313|EMBL:SEL17923.1, ECO:0000313|Proteomes:UP000199283};
RN [1] {ECO:0000313|EMBL:SEL17923.1, ECO:0000313|Proteomes:UP000199283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14858 {ECO:0000313|EMBL:SEL17923.1,
RC ECO:0000313|Proteomes:UP000199283};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}. 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}.
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DR EMBL; FNZQ01000003; SEL17923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7N378; -.
DR STRING; 188906.SAMN04488526_2152; -.
DR Proteomes; UP000199283; 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; 3.30.1340.30; -; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR InterPro; IPR007055; BON_dom.
DR InterPro; IPR010920; LSM_dom_sf.
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 PANTHER; PTHR30221; SMALL-CONDUCTANCE MECHANOSENSITIVE CHANNEL; 1.
DR PANTHER; PTHR30221:SF1; SMALL-CONDUCTANCE MECHANOSENSITIVE CHANNEL; 1.
DR Pfam; PF04972; BON; 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; SSF50182; Sm-like ribonucleoproteins; 1.
DR PROSITE; PS50914; BON; 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:UP000199283};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..455
FT /note="Small-conductance mechanosensitive channel"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011783226"
FT TRANSMEM 130..155
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369025"
FT TRANSMEM 176..193
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369025"
FT TRANSMEM 199..218
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369025"
FT DOMAIN 44..110
FT /note="BON"
FT /evidence="ECO:0000259|PROSITE:PS50914"
FT REGION 397..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 49124 MW; 1AA164929B0F7298 CRC64;
MCIVLESVAM FRTALLFLCL ASPTFAQEPV QPSGTISTAQ DSLGDAAIDR RIEAIIAELD
GYDGVSVDVR EGIVTFSGEV VEAAAVPRLD EIAARVDGVV AIENDVTETT DVATRLDPVL
ERFQDRIGQF ISYLPLLLIA ILVGGLVMVA GFALARWERP WHSLAPNAFI AEIYRVVLRL
VFVIAGVVVA LDILNATAIL TGLFGAAGIV GLAVGFAVRD TVENFIASIM LSLRQPFRPN
DVVDIEGSIG SVIRLTSRAT ILLDPNGNHV RLPNAFVFKA KIINYTRNDE RRFGFVLGID
PNDDLAEAKR IGLETLAGLE FVLTDPSPQV WVKDAGDSTV TVEFFAWLNQ RQADFNAARG
EALRVVMGAL TSAGIGMPEP TYRLNLTGGA LPVVDLPDSE SRPEALVMSE ADPAPPPEPL
RAEEVAPDRT IERMVEDERR TEGDADLLSP AAPRE
//
