ID   CAR_HALS3               Reviewed;         452 AA.
AC   B0R9Z1; O93775;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Transducer protein Car;
DE   AltName: Full=Cytoplasmic arginine transducer protein;
GN   Name=car; Synonyms=htr11; OrderedLocusNames=OE_5243F;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OG   Plasmid PHS3.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP   DISRUPTION PHENOTYPE, AND GENE NAME.
RC   STRAIN=R1 / S9;
RX   PubMed=10064582; DOI=10.1093/emboj/18.5.1146;
RA   Storch K.F., Rudolph J., Oesterhelt D.;
RT   "Car: a cytoplasmic sensor responsible for arginine chemotaxis in the
RT   archaeon Halobacterium salinarum.";
RL   EMBO J. 18:1146-1158(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1; PLASMID=PHS3;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
RN   [3]
RP   METHYLATION.
RC   STRAIN=R1 / S9;
RX   PubMed=18514223; DOI=10.1016/j.jmb.2008.04.063;
RA   Koch M.K., Staudinger W.F., Siedler F., Oesterhelt D.;
RT   "Physiological sites of deamidation and methyl esterification in sensory
RT   transducers of Halobacterium salinarum.";
RL   J. Mol. Biol. 380:285-302(2008).
RN   [4]
RP   INTERACTION WITH CHEW2.
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=23171228; DOI=10.1186/1471-2180-12-272;
RA   Schlesner M., Miller A., Besir H., Aivaliotis M., Streif J., Scheffer B.,
RA   Siedler F., Oesterhelt D.;
RT   "The protein interaction network of a taxis signal transduction system in a
RT   halophilic archaeon.";
RL   BMC Microbiol. 12:272-272(2012).
CC   -!- FUNCTION: Mediates chemotaxis towards arginine. Probably transduces the
CC       signal to the histidine kinase CheA. {ECO:0000269|PubMed:10064582}.
CC   -!- SUBUNIT: Interacts with CheW2. {ECO:0000269|PubMed:23171228}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10064582}.
CC   -!- PTM: Methylated by CheR. {ECO:0000269|PubMed:18514223}.
CC   -!- DISRUPTION PHENOTYPE: Mutants lose the chemotactic response towards
CC       arginine, but they still respond to leucine.
CC       {ECO:0000269|PubMed:10064582}.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000305}.
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DR   EMBL; AJ132321; CAB38318.1; -; Genomic_DNA.
DR   EMBL; AM774418; CAP15586.1; -; Genomic_DNA.
DR   PIR; T44849; T44849.
DR   RefSeq; WP_012289648.1; NC_010368.1.
DR   AlphaFoldDB; B0R9Z1; -.
DR   SMR; B0R9Z1; -.
DR   EnsemblBacteria; CAP15586; CAP15586; OE_5243F.
DR   GeneID; 5954798; -.
DR   GeneID; 62888236; -.
DR   KEGG; hsl:OE_5243F; -.
DR   HOGENOM; CLU_000445_116_1_2; -.
DR   OMA; AFGEKTQ; -.
DR   PhylomeDB; B0R9Z1; -.
DR   Proteomes; UP000001321; Plasmid PHS3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd00130; PAS; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00283; MA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE   1: Evidence at protein level;
KW   Chemotaxis; Cytoplasm; Methylation; Plasmid; Transducer.
FT   CHAIN           1..452
FT                   /note="Transducer protein Car"
FT                   /id="PRO_0000428990"
FT   DOMAIN          47..121
FT                   /note="PAS"
FT   DOMAIN          180..416
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT   REGION          229..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   452 AA;  49099 MW;  9244D900D694681A CRC64;
     MDPASSDMGG EATGEHLADE LCEAYLGDNE DDGGDELQRL SRERDFWKHM FNQLVAEYPE
     GILITAADGT VTHWNERFSD HMKMARSDAL GEDASDVFST AEESETLPEA VVRTGDTVEE
     EEPHDVPTDS LCQYHGVPLR APTGDVVGSF GVVPDISEKV KNQRELHDLH ETVSSNVGEH
     LSELSESIDE VGSFAEETEA FAGEEIERME GVADEVSNQS ATIEEIASSA EEVSQASQRA
     QDRATEGEQT AETAIDRMGA VQESAERVND TIDGLTSQAD EMSEIIDAIN DIADQTNMLA
     LNASIEAARA GEKGEGFAVV ADEVKSLAEE SQERADEIEQ MIVEMVETTD QTADRIGQTT
     TEIEEAITAV RETLDSLQEI RKAVDETATG VKEVAGATDD HAASTEQVAA TTDEAVDKLT
     ELEDRLDNLS QIASEQHDRV AEIEDMVDEL VE