ID A0A240U640_9BURK Unreviewed; 664 AA.
AC A0A240U640;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:ART53315.1};
GN ORFNames=CBP34_18850 {ECO:0000313|EMBL:ART53315.1};
OS Acidovorax carolinensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=553814 {ECO:0000313|EMBL:ART53315.1, ECO:0000313|Proteomes:UP000194432};
RN [1] {ECO:0000313|EMBL:ART53315.1, ECO:0000313|Proteomes:UP000194432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA3 {ECO:0000313|EMBL:ART53315.1};
RA Singleton D.R., Lee J., Dickey A.N., Stroud A., Scholl E.H., Wright F.A.,
RA Aitken M.D.;
RT "Polyphasic characterization of four soil-derived phenanthrene-degrading
RT Acidovorax strains and proposal of Acidovorax phenanthrenivorans sp. nov.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP021361; ART53315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A240U640; -.
DR KEGG; acin:CBP34_18850; -.
DR Proteomes; UP000194432; Chromosome.
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 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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000194432};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 339..391
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 396..625
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 415..449
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 664 AA; 69916 MW; C33B8E1AA54F0AEA CRC64;
MSLLHRLGLL HKFMILGTIG LMMSALPMFL YVSKSLQSIA AARHESVGAA PALVLNKVVQ
LMQVHRGLSA GMLGGDEALA ARRPAAREAL EKTMGEVAAS FAAAQVPAAQ TSAWAQAQQT
WKTLEQAVAA RSLQSGQSTA QHTQLIASIM LINEGLLHAY GLETDPDADT HALIQASLVH
APMLGEKLGV LRAQGSGFLG RGELPAQDKG QLLMLRQRVT ELQVQTMRSF DRALELNPQF
RQSLGGKTQE LQGLITQSLQ LLEGEVINAT EFKLPAKDYF DHFTRTIEAL NALNTQAAGN
LTQALNNRVA DLQQSLLWVA VALVATLSLT TGMALVFVRS MTQPLAQAVQ LSRAVAQGDL
SGGPIAHGTN EVGQLLAALL QMRQQLTDVV RNVRGGSESV ATASIQIAQG NTDLSARTES
QASALEETAA SMEQLNATVR QNAESAQQAS QLAASASTVA VQGGEVVAQV VDTMHGINAS
SQKIADIIGV IDSIAFQTNI LALNAAVEAA RAGEQGRGFA VVASEVRSLA GRSAEAAREI
KSLISASVER VAQGSALVDR AGATMSEVVG AIRRVTDIVG EISAASHEQS LGVAQVGEAV
TQMDQVTQQN AALVEEMAAA ASSLKSQAQD LVQVVSVFQL EEEFGGNRPG QATLQRARPS
LQIQ
//
