MCP2_SALTY
ID MCP2_SALTY Reviewed; 553 AA.
AC P02941;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Methyl-accepting chemotaxis protein II;
DE Short=MCP-II;
DE AltName: Full=Aspartate chemoreceptor protein;
GN Name=tar; Synonyms=cheM; OrderedLocusNames=STM1919;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6302843; DOI=10.1126/science.6302843;
RA Russo A.F., Koshland D.E. Jr.;
RT "Separation of signal transduction and adaptation functions of the
RT aspartate receptor in bacterial sensing.";
RL Science 220:1016-1020(1983).
RN [2]
RP SEQUENCE REVISION TO 236 AND 498.
RA Stock A.;
RL Thesis (1986), University of Berkeley, United States.
RN [3]
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 26-188.
RX PubMed=1660187; DOI=10.1126/science.1660187;
RA Milburn M.V., Prive G.G., Milligan D.L., Scott W.G., Yeh J., Jancarik J.,
RA Koshland D.E. Jr., Kim S.-H.;
RT "Three-dimensional structures of the ligand-binding domain of the bacterial
RT aspartate receptor with and without a ligand.";
RL Science 254:1342-1347(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 36-180.
RX PubMed=8486661; DOI=10.1016/s0021-9258(18)98416-4;
RA Yeh J.I., Biemann H.-P., Pandit J., Koshland D.E. Jr., Kim S.-H.;
RT "The three-dimensional structure of the ligand-binding domain of a wild-
RT type bacterial chemotaxis receptor. Structural comparison to the cross-
RT linked mutant forms and conformational changes upon ligand binding.";
RL J. Biol. Chem. 268:9787-9792(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 26-180.
RX PubMed=8831788; DOI=10.1006/jmbi.1996.0507;
RA Yeh J.I., Biemann H.-P., Prive G.G., Pandit J., Koshland D.E. Jr.,
RA Kim S.-H.;
RT "High-resolution structures of the ligand binding domain of the wild-type
RT bacterial aspartate receptor.";
RL J. Mol. Biol. 262:186-201(1996).
CC -!- FUNCTION: Receptor for the attractant L-aspartate and related amino and
CC dicarboxylic acids. Tar mediates taxis away from the repellents cobalt
CC and nickel. Unlike in E.coli tar, it does not mediates maltose taxis.
CC -!- FUNCTION: Chemotactic-signal transducers respond to changes in the
CC concentration of attractants and repellents in the environment,
CC transduce a signal from the outside to the inside of the cell, and
CC facilitate sensory adaptation through the variation of the level of
CC methylation. Attractants increase the level of methylation while
CC repellents decrease the level of methylation, the methyl groups are
CC added by the methyltransferase CheR and removed by the methylesterase
CC CheB.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; J01809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE006468; AAL20835.1; -; Genomic_DNA.
DR PIR; A03441; QREBDT.
DR RefSeq; NP_460876.1; NC_003197.2.
DR RefSeq; WP_000483274.1; NC_003197.2.
DR PDB; 1JMW; X-ray; 1.90 A; A=36-180.
DR PDB; 1LIH; X-ray; 2.20 A; A=26-188.
DR PDB; 1VLS; X-ray; 1.85 A; A=36-180.
DR PDB; 1VLT; X-ray; 2.20 A; A/B=36-180.
DR PDB; 1WAS; X-ray; 2.70 A; A=36-180.
DR PDB; 1WAT; X-ray; 3.00 A; A/B=36-180.
DR PDB; 2LIG; X-ray; 2.00 A; A/B=26-188.
DR PDBsum; 1JMW; -.
DR PDBsum; 1LIH; -.
DR PDBsum; 1VLS; -.
DR PDBsum; 1VLT; -.
DR PDBsum; 1WAS; -.
DR PDBsum; 1WAT; -.
DR PDBsum; 2LIG; -.
DR AlphaFoldDB; P02941; -.
DR SMR; P02941; -.
DR DIP; DIP-61268N; -.
DR IntAct; P02941; 1.
DR STRING; 99287.STM1919; -.
DR DrugBank; DB02365; 1,10-Phenanthroline.
DR PaxDb; P02941; -.
DR EnsemblBacteria; AAL20835; AAL20835; STM1919.
DR GeneID; 1253440; -.
DR KEGG; stm:STM1919; -.
DR PATRIC; fig|99287.12.peg.2035; -.
DR HOGENOM; CLU_000445_107_16_6; -.
DR OMA; SARMMMD; -.
DR PhylomeDB; P02941; -.
DR BioCyc; SENT99287:STM1919-MON; -.
DR EvolutionaryTrace; P02941; -.
DR PHI-base; PHI:6983; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; cd00181; Tar_Tsr_LBD; 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 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; SSF47170; 1.
DR PROSITE; PS00538; CHEMOTAXIS_TRANSDUC_1; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Chemotaxis; Membrane;
KW Methylation; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..553
FT /note="Methyl-accepting chemotaxis protein II"
FT /id="PRO_0000110539"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..190
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..553
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 214..266
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 271..500
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 64..73
FT /note="The 3 Arg may form a positively charged pocket,
FT which binds the alpha-carboxyl group of the attractant AA"
FT REGION 532..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000250|UniProtKB:P02942"
FT MOD_RES 302
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250|UniProtKB:P02942"
FT MOD_RES 309
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000250|UniProtKB:P02942"
FT MOD_RES 491
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250|UniProtKB:P02942"
FT MOD_RES 500
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250|UniProtKB:P02942"
FT CONFLICT 246
FT /note="E -> G (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="T -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:2LIG"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1VLS"
FT HELIX 39..73
FT /evidence="ECO:0007829|PDB:1VLS"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:1WAT"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1VLS"
FT HELIX 89..109
FT /evidence="ECO:0007829|PDB:1VLS"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1VLS"
FT HELIX 117..142
FT /evidence="ECO:0007829|PDB:1VLS"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:1VLS"
FT HELIX 154..177
FT /evidence="ECO:0007829|PDB:1VLS"
SQ SEQUENCE 553 AA; 59614 MW; 5CEC8E707452760D CRC64;
MFNRIRVVTM LMMVLGVFAL LQLVSGGLLF SSLQHNQQGF VISNELRQQQ SELTSTWDLM
LQTRINLSRS AARMMMDASN QQSSAKTDLL QNAKTTLAQA AAHYANFKNM TPLPAMAEAS
ANVDEKYQRY QAALAELIQF LDNGNMDAYF AQPTQGMQNA LGEALGNYAR VSENLYRQTF
DQSAHDYRFA QWQLGVLAVV LVLILMVVWF GIRHALLNPL ARVITHIREI ASGDLTKTLT
VSGRNEIGEL AGTVEHMQRS LIDTVTQVRE GSDAIYSGTS EIAAGNTDLS SRTEQQASAL
EETAASMEQL TATVKQNADN ARQASQLAQS ASETARHGGK VVDGVVNTMH EIADSSKKIA
DIISVIDGIA FQTNILALNA AVEAARAGEQ GRGFAVVAGE VRNLASRSAQ AAKEIKALIE
DSVSRVDTGS VLVESAGETM TDIVNAVTRV TDIMGEIASA SDEQSRGIDQ VALAVSEMDR
VTQQNASLVQ ESAAAAAALE EQASRLTQAV SAFRLASRPL AVNKPEMRLS VNAQSGNTPQ
SLAARDDANW ETF
