ID G4E159_9GAMM Unreviewed; 645 AA.
AC G4E159;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:EGZ50818.1};
GN ORFNames=ThisiDRAFT_0038 {ECO:0000313|EMBL:EGZ50818.1};
OS Thiorhodospira sibirica ATCC 700588.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thiorhodospira.
OX NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ50818.1};
RN [1] {ECO:0000313|EMBL:EGZ50818.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ50818.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J.,
RA Frigaard N.-U., Bryant D., Woyke T.;
RT "The draft genome of Thiorhodospira sibirica ATCC 700588.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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:EGZ50818.1}.
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DR EMBL; AGFD01000001; EGZ50818.1; -; Genomic_DNA.
DR AlphaFoldDB; G4E159; -.
DR STRING; 765914.ThisiDRAFT_0038; -.
DR eggNOG; COG0840; Bacteria.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.20.1440.210; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 279..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 300..355
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 351..413
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT DOMAIN 360..589
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 612..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 70289 MW; D25C57F1B4D7C7EC CRC64;
MNSAPGARAL RMNIRLKILT GFLAVLVILS ILGVTAIVNL NDIRAKFDGL VEATQVERYA
YRTIEEEKNY LLNEQDSSYQ QAMQNIDTII KALDTIDRHS RDADLLARSR EARRATLEYR
KGYEAGVAAL RANATAVTRM AENGQTVVTL AEQYYQNTQE SVALRVYITA LEIMNAEKEE
RLYRNREFYQ RMLVMRTQLD GYYNQLDPQG RDAQVNAARR ATEAYFEAAA TWIVNDDRLT
QEILPTMQRL GEDVIKLAFE AARDAADSMI ATQNLSNQVI ASGVVITIVL GILIGIILSN
MISKPLIYGV NFAKTIAEGD LTQRIEPQYL KRSDEIGDLA KALDEMVAQL QAMVMQVTDS
TAQVSSAAAE IAQGSSDLSQ RTEEQASAIE QTASSMEELT STVKESAKNA EQANELARVA
RHHAEQGGEV VDQAIVAMGA INASSRRIAD IISVIDEIAF QTNLLALNAA VEAARAGEQG
RGFAVVAGEV RNLAQRSADS AKEIKVLITD SVDKVQDGVE LVERSGATLK DIATAVKKVS
DIVAEMAAAS KEQAGGIEQV NKAIMQVDEV TQQNAALVEE TAAASQNMGQ QAQNLQEMMG
FFKLNAHTGA VPARTPAKTA ALPKPSPSHR QSASSERGGE EWQSF
//
