ID B6ENJ2_ALISL Unreviewed; 561 AA.
AC B6ENJ2;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Small-conductance mechanosensitive channel {ECO:0000256|RuleBase:RU369025};
GN OrderedLocusNames=VSAL_I1797 {ECO:0000313|EMBL:CAQ79482.1};
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275 {ECO:0000313|EMBL:CAQ79482.1, ECO:0000313|Proteomes:UP000001730};
RN [1] {ECO:0000313|EMBL:CAQ79482.1, ECO:0000313|Proteomes:UP000001730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238 {ECO:0000313|EMBL:CAQ79482.1,
RC ECO:0000313|Proteomes:UP000001730};
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(2008).
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; FM178379; CAQ79482.1; -; Genomic_DNA.
DR RefSeq; WP_012550383.1; NC_011312.1.
DR AlphaFoldDB; B6ENJ2; -.
DR KEGG; vsa:VSAL_I1797; -.
DR eggNOG; COG0668; Bacteria.
DR HOGENOM; CLU_026710_3_0_6; -.
DR Proteomes; UP000001730; Chromosome 1.
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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..561
FT /note="Small-conductance mechanosensitive channel"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002842487"
FT TRANSMEM 279..296
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369025"
FT TRANSMEM 317..340
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369025"
FT TRANSMEM 346..364
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369025"
FT DOMAIN 329..365
FT /note="Mechanosensitive ion channel transmembrane helices
FT 2/3"
FT /evidence="ECO:0000259|Pfam:PF21088"
FT DOMAIN 366..433
FT /note="Mechanosensitive ion channel MscS"
FT /evidence="ECO:0000259|Pfam:PF00924"
FT DOMAIN 439..521
FT /note="Mechanosensitive ion channel MscS C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21082"
FT COILED 16..46
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 561 AA; 63556 MW; 39565491D039D6AB CRC64;
MRYLLCFLLL FSSLTYANET QDIEQLQNIN AEIARLKQES ASFKGNDLAV IRVQQVEKNN
ELRIVLSELI NKHTAENTPL LVSEVEDQIR YADRSFLYLG KELKSKKDKI DTADVEHKLA
LQNTLNESRS YYYTSLSDQL QNYRWLNKLG KPNQAKVDAF KLVIDQKIKF LSASLSFDSS
REQLLADQLQ RSSDSEKSSL TLEHLFFQRK VTNSTDGLIK LINIADQLNI STTNYKRQVF
ATTGNLTEDI LSFPVMAAIL SNWITDGSNW LFKHAPDQLL KFFVFILIIF ATRLLARLTR
RVVLKAVVQP HLRMSKLMQD FFVSMSSKLI FFIGILIAFS KIGLDLAPVL TGFGVAGIII
GFALQDTLSN FASGMMLLIY RPFDVGDLVD AGGVSGKVSH MSLVNTTIKT FDNQIIILPN
SKIWGDVIKN VTHERLRRVD MVFGIGYEDS IEHAEKILAE IIDTHPAALK KPEPNIRVHT
LGASSVDFIV RPWVKTEDYW DVYWDVTREV KLRFDKEGIS IPFAQQDVHV HFAKKAKKPK
ATTGIAGKLS NVIDSVRSKD S
//
