ID L0GZE4_9GAMM Unreviewed; 511 AA.
AC L0GZE4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Small-conductance mechanosensitive channel {ECO:0000256|RuleBase:RU369025};
GN ORFNames=Thimo_1914 {ECO:0000313|EMBL:AGA90679.1};
OS Thioflavicoccus mobilis 8321.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thioflavicoccus.
OX NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA90679.1, ECO:0000313|Proteomes:UP000010816};
RN [1] {ECO:0000313|EMBL:AGA90679.1, ECO:0000313|Proteomes:UP000010816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8321 {ECO:0000313|EMBL:AGA90679.1,
RC ECO:0000313|Proteomes:UP000010816};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z., Imhoff J.,
RA Thiel V., Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of chromosome of Thioflavicoccus mobilis 8321.";
RL Submitted (SEP-2011) 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}.
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DR EMBL; CP003051; AGA90679.1; -; Genomic_DNA.
DR RefSeq; WP_015280820.1; NC_019940.1.
DR AlphaFoldDB; L0GZE4; -.
DR STRING; 765912.Thimo_1914; -.
DR KEGG; tmb:Thimo_1914; -.
DR PATRIC; fig|765912.4.peg.1874; -.
DR eggNOG; COG0664; Bacteria.
DR eggNOG; COG0668; Bacteria.
DR HOGENOM; CLU_032479_1_0_6; -.
DR OrthoDB; 9775207at2; -.
DR Proteomes; UP000010816; Chromosome.
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:UP000010816};
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..29
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369025"
FT TRANSMEM 41..67
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369025"
FT TRANSMEM 87..108
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369025"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369025"
FT DOMAIN 358..474
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
SQ SEQUENCE 511 AA; 56354 MW; 31E0AA2D2640257B CRC64;
MIFLEDLTAR YWPFFLAASL LFLLWRLGGH SLQGRGLARR FPLLMALADL LMIPLLVAVF
GGLVKLAATG VGLSGFDGKA VRTGTLVVGY LISGWLLAHL IELMLLARAD DKISERVPKL
VVGLVYGALM LLGLGLLLWL QGYSFTGIWV STGVAAAVLG LALQRTLGDL FSGIALGIER
PFKLGDWIEL ADGTVGQVID LNWRATWLRG WDNSTHVIPN SQMAGQPLKN LHDEQHLFAP
WYFVKIPAEV DPRFATALIL DAALRCESVL KVPHPVVRLA DASSIPYSYM VWVHLKNYPA
MFRGREELYR EIHWALRQAG ISLAPEVNEL RMRRADAVNA EPPTIFLALK ALDVGGLLTE
AELDQLAAGG AYRYYDCGRV ILSEGTLSDA FYVIAGGLVE AAITLPDGTR KVTEVLGTGD
YFGITSMLTT NPSYLEMRAQ SDVTLIRIDL DCVRALLAAR PELAERFARI VKERLDAAEA
VRVASRQPTR RLSLRDIRER IDGLVVRKTR A
//
