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Database: UniProt
Entry: A0A1I6D8L2_9RHOB
LinkDB: A0A1I6D8L2_9RHOB
Original site: A0A1I6D8L2_9RHOB 
ID   A0A1I6D8L2_9RHOB        Unreviewed;       285 AA.
AC   A0A1I6D8L2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Small-conductance mechanosensitive channel {ECO:0000256|RuleBase:RU369025};
GN   ORFNames=SAMN04515673_102412 {ECO:0000313|EMBL:SFR01738.1};
OS   Poseidonocella sedimentorum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Poseidonocella.
OX   NCBI_TaxID=871652 {ECO:0000313|EMBL:SFR01738.1, ECO:0000313|Proteomes:UP000199302};
RN   [1] {ECO:0000313|EMBL:SFR01738.1, ECO:0000313|Proteomes:UP000199302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMM 9023,NRIC 0796,JCM 17311,KCTC 23692
RC   {ECO:0000313|Proteomes:UP000199302};
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; FOYI01000002; SFR01738.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6D8L2; -.
DR   STRING; 871652.SAMN04515673_102412; -.
DR   OrthoDB; 9814206at2; -.
DR   Proteomes; UP000199302; 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:SF1; 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:UP000199302};
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..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369025"
FT   TRANSMEM        67..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369025"
FT   TRANSMEM        96..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369025"
FT   DOMAIN          70..111
FT                   /note="Mechanosensitive ion channel transmembrane helices
FT                   2/3"
FT                   /evidence="ECO:0000259|Pfam:PF21088"
FT   DOMAIN          113..178
FT                   /note="Mechanosensitive ion channel MscS"
FT                   /evidence="ECO:0000259|Pfam:PF00924"
FT   DOMAIN          187..267
FT                   /note="Mechanosensitive ion channel MscS C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21082"
SQ   SEQUENCE   285 AA;  31013 MW;  66029C15257BD9CE CRC64;
     MEEQFEAALE FFDDNRETFL IVQGLVVNIF AALVIFIVGL VVSGWVKRRI LRLGARTRHF
     DPTLANFLAN VARYAVLALA LIFVLSRFGI ETTSLAALIG AAGLAIGLAL QGTLSHLASG
     VMLVAFRPIQ IGQFVEAAGQ SGTVSNISLF TTELTTVDNV QLILPNGEVW GNVIKNYSAH
     PTRRCDLVVG VSYDADLKRA ETILWELIRA DARVLAEPEP FCKVTNLGDS SVDFTLRLWC
     SADDLWGLKF DMTRAIKDAF DANGIGIPFP TRTLVVEKGQ AVGAD
//
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