ID   Q2SXL8_BURTA            Unreviewed;       640 AA.
AC   Q2SXL8;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:ABC39455.1};
GN   OrderedLocusNames=BTH_I1799 {ECO:0000313|EMBL:ABC39455.1};
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:ABC39455.1, ECO:0000313|Proteomes:UP000001930};
RN   [1] {ECO:0000313|EMBL:ABC39455.1, 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).
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CP000086; ABC39455.1; -; Genomic_DNA.
DR   RefSeq; WP_009890089.1; NZ_CP008785.1.
DR   AlphaFoldDB; Q2SXL8; -.
DR   KEGG; bte:BTH_I1799; -.
DR   HOGENOM; CLU_000445_107_22_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; cd06225; HAMP; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_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   PRINTS; PR00260; CHEMTRNSDUCR.
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.
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        315..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          344..390
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          395..624
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   640 AA;  67324 MW;  3AD9F1504B3A36EA CRC64;
     MSKQLFGPGM RLMARMKLPR KLAILAVLFI VPLVAALYAT LAVALHAYAT TQGERDGITI
     LETTQDLLKA VQVRRGAGAS VLAGNEAMRA KFDAANASAD RLVATLKQQV RDTRRFDVVA
     LVEALASQYE KAAAGGLGTS AAALFDSHTD VIHSIFLFEK DLAVASQLGV DPDASNYHLI
     DSVLFALPGT AETVGVLRGK GSAALSGGSL GDADKRELAV RAGGLAEQMS VIRHHLERTK
     DTLGANALDG VDLGAVAAFQ RTAAALAHGG APVDAKTYFQ QGSDAIDALY RVHGALAQQL
     RERLAARAHA EQVKVAAILA LSVALVACAL YLFVAFAMST HEDVAQLSGC MRAVGDGDLR
     ARLAVRGGDE FAFIKRGFNA LLDVWAQTLS ETRRVADSVM VGSQQIAAGN LDLSGRTETQ
     AASLEQTAAS MEELTSTVRH NASNASHAST LSAEASERAA DTGRIMTHAV TLMTKIHDSS
     NRMAEIVSVI EGIAFQTNIL ALNAAVEAAR AGEQGKGFAV VAGEVRALAH RSAAAAKDVK
     ELIHESIRHV TDGSLLFQRA DDAIRSVNAS IRSVDTVVSE IAKASEQQSD GIEQVNAAIT
     QMDEVTQRNA ALVEESAAAS ASLREQAEHM GKLVGRFVLA
//