ID   Q2SVA5_BURTA            Unreviewed;       558 AA.
AC   Q2SVA5;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:ABC38770.1};
GN   OrderedLocusNames=BTH_I2629 {ECO:0000313|EMBL:ABC38770.1};
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS   CIP 106301 / E264).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC38770.1, ECO:0000313|Proteomes:UP000001930};
RN   [1] {ECO:0000313|EMBL:ABC38770.1, ECO:0000313|Proteomes:UP000001930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC   {ECO:0000313|Proteomes:UP000001930};
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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DR   EMBL; CP000086; ABC38770.1; -; Genomic_DNA.
DR   RefSeq; WP_011402437.1; NZ_CP008785.1.
DR   AlphaFoldDB; Q2SVA5; -.
DR   GeneID; 66546903; -.
DR   KEGG; bte:BTH_I2629; -.
DR   HOGENOM; CLU_000445_107_16_4; -.
DR   Proteomes; UP000001930; Chromosome I.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd11386; MCP_signal; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR024478; HlyB_4HB_MCP.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR   PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR   Pfam; PF12729; 4HB_MCP_1; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE   4: Predicted;
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        40..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        225..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          308..537
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   558 AA;  58553 MW;  483DCBAA906783AB CRC64;
     MKGVSLHGKH FLPDDAPGNR GRTPKPGKPR RARRAWSVKT TLRAAFALLL VGTLAVGLFS
     LAQISRLNSS IKSVYEQGHV ASRAAEEVRA SVLRASRAQK MLITATTARE RDDLGADIDK
     GLAAIGTELA TLQRHADGAA DDAARMKAFG AAVGTWSTHL RDFVKLVREQ PLDLSQMSWQ
     VGSQDVSLLV ETGKLEKLVD GLVDARGEAS KATLDASGAI FRESFAMLAA MTAALVVLAF
     VIAAWVVRRL GAQLGGEPAY AKEIAVSISR GDLSNAIRLD TRDRDSMLHA LRDMQEGLAG
     TVREISASAE AIASAAGEIA MGNLDLSQRT EQQAVALERT ATSMGQLTST VHQNAENARQ
     ASALAANASS VAEAGGSVVG RVVATMNEID ESAKSIRDII GVIESIAFQT NILALNAAVE
     AARAGEEGRG FSVVASEVRS LAQRSATAAK EIKALIGASV ERVANGAVLA QDAGRTMDEV
     VRAVKRVTDI MGEISAASNE QSSGIDAIER AVTQMDAGTQ QNAALVEEAA AAARSLDEQA
     QMLKAMVGRF HLPAHAVG
//