ID MCPC_SALTY Reviewed; 547 AA.
AC Q02755;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 27-MAR-2024, entry version 149.
DE RecName: Full=Methyl-accepting chemotaxis citrate transducer;
DE AltName: Full=Citrate chemoreceptor protein;
GN Name=tcp; OrderedLocusNames=STM3577;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29595 / ST1;
RX PubMed=8419927; DOI=10.1073/pnas.90.1.217;
RA Yamamoto K., Imae Y.;
RT "Cloning and characterization of the Salmonella typhimurium-specific
RT chemoreceptor Tcp for taxis to citrate and from phenol.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:217-221(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Acts as a receptor for citrate and mediates taxis away from
CC phenol. Also mediates an attractant response to metal-citrate
CC complexes.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- PTM: Methylation level is increased by citrate and decreased by phenol.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; L06029; AAA27231.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22437.1; -; Genomic_DNA.
DR PIR; A47178; A47178.
DR RefSeq; NP_462478.1; NC_003197.2.
DR RefSeq; WP_000789683.1; NC_003197.2.
DR AlphaFoldDB; Q02755; -.
DR SMR; Q02755; -.
DR STRING; 99287.STM3577; -.
DR PaxDb; 99287-STM3577; -.
DR GeneID; 1255100; -.
DR KEGG; stm:STM3577; -.
DR PATRIC; fig|99287.12.peg.3780; -.
DR HOGENOM; CLU_000445_107_16_6; -.
DR OMA; DNVVNTM; -.
DR PhylomeDB; Q02755; -.
DR BioCyc; SENT99287:STM3577-MONOMER; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd11386; MCP_signal; 1.
DR CDD; cd19407; Tar_Tsr_sensor; 1.
DR Gene3D; 1.20.120.30; Aspartate receptor, ligand-binding domain; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR035440; 4HB_MCP_dom_sf.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR004091; Chemotax_Me-accpt_rcpt_Me-site.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR003122; Tar_rcpt_lig-bd.
DR PANTHER; PTHR43531:SF5; METHYL-ACCEPTING CHEMOTAXIS PROTEIN II; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF02203; TarH; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SMART; SM00319; TarH; 1.
DR SUPFAM; SSF47170; Aspartate receptor, ligand-binding domain; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS00538; CHEMOTAXIS_TRANSDUC_1; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Chemotaxis; Membrane; Methylation;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..547
FT /note="Methyl-accepting chemotaxis citrate transducer"
FT /id="PRO_0000110544"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..189
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 215..267
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 272..501
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 317..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 296
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000250"
FT MOD_RES 303
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250"
FT MOD_RES 310
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000250"
FT MOD_RES 492
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250"
FT MOD_RES 501
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 547 AA; 58950 MW; 8269F4EC4DB509D8 CRC64;
MKNIKVITGV IATLGIFSAL LLVTGILFYS AVSSDRLNFQ NASALSYQQQ ELGGSFQTLI
ETRVTINRVA IRMLKNQRDP ASLDAMNTLL TNAGASLNEA EKHFNNYVNS EAIAGKDPAL
DAQAEASFKQ MYDVLQQSIH YLKADNYAAY GNLDAQKAQD DMEQVYDQWL SQNAQLIKLA
SDQNQSSFTQ MQWTLGIILL IVLIVLAFIW LGLQRVLLRP LQRIMAHIQT IADGDLTHEI
EAEGRSEMGQ LAAGLKTMQQ SLIRTVSAVR DNADSIYTGA GEISAGSSDL SSRTEQQASA
LEETAASMEQ LTATVRQNTD NARQATGLAK TASETARKGG RVVDNVVSTM NDIAESSEKI
VDITSVIDGI AFQTNILALN AAVEAARAGE QGRGFAVVAG EVRTLASRSA QAAKEIKVLI
ENSVSRIDTG STQVREAGET MKEIVNAVTR VTDIMGEIAS ASDEQSKGIE QVAQAVSEMD
SVTQQNASLV EESAAAAAAL EDQANELRQA VAAFRIQKQP RREASPTTLS KGLTPQPAAE
QANWESF
//
