ID Q2SVL0_BURTA Unreviewed; 605 AA. AC Q2SVL0; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 80. DE SubName: Full=Methyl-accepting chemotaxis domain protein {ECO:0000313|EMBL:ABC37240.1}; GN OrderedLocusNames=BTH_I2522 {ECO:0000313|EMBL:ABC37240.1}; 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:ABC37240.1, ECO:0000313|Proteomes:UP000001930}; RN [1] {ECO:0000313|EMBL:ABC37240.1, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000086; ABC37240.1; -; Genomic_DNA. DR AlphaFoldDB; Q2SVL0; -. DR KEGG; bte:BTH_I2522; -. DR HOGENOM; CLU_000445_107_16_4; -. DR Proteomes; UP000001930; Chromosome I. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. 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; 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; PF00015; MCPsignal; 1. DR SMART; SM00304; HAMP; 1. 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 37..55 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 258..278 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 279..336 FT /note="HAMP" FT /evidence="ECO:0000259|PROSITE:PS50885" FT DOMAIN 341..570 FT /note="Methyl-accepting transducer" FT /evidence="ECO:0000259|PROSITE:PS50111" SQ SEQUENCE 605 AA; 65190 MW; BC686994E29CCD89 CRC64; MPLIQRASPR SIYRGRRVAP KPENIVGFLN TFSLRRYASL LLGLLAVAAV AIGFCQWRLD VANRRVAHAY QQRYVSTQLA NELRRSSDDL TRLARTYVAT GDAKWEQQYN EVLAIRSGKA PRPLDYDRIY WDFRAADEPM RPGHGETISL QDMMKRAGFT DEEFAKLHDA EQNSNDLVKT ETIAMNLVKG LTPDDAGNFT KQGPPDLDKA RSLMFDANYH RFKAKIMHPI DDFLKLLDAR TEGAIASAQA TAQTWKTVSA GVAIGALACF ALMLHALFRR VIAGLEVAAS TAGRVAAGDL TSHFDADRVD PQAKNEISRV MRSLQTMNDG LVRIVSDVRS GTDAIATVSH EIMAGNNDLS ARTEQQAASL QETAASMSEL TATVKLNLEN ARQANMIGSD AVSTVEQGAV SVEHLVTTVN AISASSGKIA DIISLIEGIA FQTNILALNA AVEAARAGEQ GRGFAVVASE VRSLAQRSSA AAKEIKDLIE TSIDTVRDGV SKADEVGRHI VEVKRAIRRV ADLVGEITSA SEEQSRGIEQ VDAAVSQMDR VTQQNAALVE QAAAASKAMD DQAGNLRAAA SIFKLPGGAG LHDHAQPGAS GRFAT //