MCP2_ECOLI
ID MCP2_ECOLI Reviewed; 553 AA.
AC P07017; P76301;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Methyl-accepting chemotaxis protein II;
DE Short=MCP-II;
DE AltName: Full=Aspartate chemoreceptor protein;
GN Name=tar; Synonyms=cheM; OrderedLocusNames=b1886, JW1875;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6305515; DOI=10.1016/0092-8674(83)90442-7;
RA Krikos A., Mutoh N., Boyd A., Simon M.I.;
RT "Sensory transducers of E. coli are composed of discrete structural and
RT functional domains.";
RL Cell 33:615-622(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [7]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22380631; DOI=10.1111/j.1365-2958.2012.08021.x;
RA Li G., Young K.D.;
RT "Isolation and identification of new inner membrane-associated proteins
RT that localize to cell poles in Escherichia coli.";
RL Mol. Microbiol. 84:276-295(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 38-179.
RX PubMed=15299315; DOI=10.1107/s0907444994010498;
RA Bowie J.U., Pakula A.A., Simon M.I.;
RT "The three-dimensional structure of the aspartate receptor from Escherichia
RT coli.";
RL Acta Crystallogr. D 51:145-154(1995).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 38-180.
RX PubMed=9315712; DOI=10.1016/s0014-5793(97)01027-2;
RA Chi Y.-I., Yokota H., Kim S.-H.;
RT "Apo structure of the ligand-binding domain of aspartate receptor from
RT Escherichia coli and its comparison with ligand-bound or pseudoligand-bound
RT structures.";
RL FEBS Lett. 414:327-332(1997).
CC -!- FUNCTION: Receptor for the attractant L-aspartate and related amino and
CC dicarboxylic acids. Tar also mediates taxis to the attractant maltose
CC via an interaction with the periplasmic maltose binding protein. Tar
CC mediates taxis away from the repellents cobalt and nickel.
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 -!- INTERACTION:
CC P07017; P07363: cheA; NbExp=4; IntAct=EBI-1125130, EBI-1026773;
CC P07017; P0A964: cheW; NbExp=5; IntAct=EBI-1125130, EBI-1125947;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:22380631}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22380631}. Note=Found predominantly at cell poles.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; J01705; AAA23566.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74956.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15702.1; -; Genomic_DNA.
DR PIR; F64951; QRECM4.
DR RefSeq; NP_416400.1; NC_000913.3.
DR RefSeq; WP_001297437.1; NZ_SSZK01000001.1.
DR PDB; 2ASR; X-ray; 2.30 A; A=38-179.
DR PDB; 2L9G; NMR; -; A=214-232.
DR PDB; 4Z9H; X-ray; 1.45 A; A/B=26-193.
DR PDB; 4Z9I; X-ray; 1.57 A; A/B=26-193.
DR PDB; 4Z9J; X-ray; 1.78 A; A/B=26-193.
DR PDBsum; 2ASR; -.
DR PDBsum; 2L9G; -.
DR PDBsum; 4Z9H; -.
DR PDBsum; 4Z9I; -.
DR PDBsum; 4Z9J; -.
DR AlphaFoldDB; P07017; -.
DR BMRB; P07017; -.
DR SMR; P07017; -.
DR BioGRID; 4260381; 319.
DR DIP; DIP-10956N; -.
DR IntAct; P07017; 7.
DR STRING; 511145.b1886; -.
DR MoonProt; P07017; -.
DR PaxDb; P07017; -.
DR PRIDE; P07017; -.
DR EnsemblBacteria; AAC74956; AAC74956; b1886.
DR EnsemblBacteria; BAA15702; BAA15702; BAA15702.
DR GeneID; 66674223; -.
DR GeneID; 946399; -.
DR KEGG; ecj:JW1875; -.
DR KEGG; eco:b1886; -.
DR PATRIC; fig|511145.12.peg.1967; -.
DR EchoBASE; EB0981; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_16_6; -.
DR InParanoid; P07017; -.
DR OMA; SARMMMD; -.
DR PhylomeDB; P07017; -.
DR BioCyc; EcoCyc:TAR-MON; -.
DR EvolutionaryTrace; P07017; -.
DR PRO; PR:P07017; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0051286; C:cell tip; IDA:CACAO.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:CAFA.
DR GO; GO:0098561; C:methyl accepting chemotaxis protein complex; IDA:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:CAFA.
DR GO; GO:0043424; F:protein histidine kinase binding; IDA:EcoCyc.
DR GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IMP:EcoCyc.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:CAFA.
DR GO; GO:0006935; P:chemotaxis; IMP:EcoCyc.
DR GO; GO:0009593; P:detection of chemical stimulus; IDA:CAFA.
DR GO; GO:1901875; P:positive regulation of post-translational protein modification; IMP:CAFA.
DR GO; GO:0050920; P:regulation of chemotaxis; IDA:CAFA.
DR GO; GO:0007172; P:signal complex assembly; IDA:CAFA.
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_0000110538"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT TRANSMEM 7..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..190
FT /note="Periplasmic"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..553
FT /note="Cytoplasmic"
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 517..553
FT /note="Disordered"
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 164
FT /note="A -> R (in Ref. 1; AAA23566)"
FT /evidence="ECO:0000305"
FT HELIX 37..74
FT /evidence="ECO:0007829|PDB:4Z9H"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:4Z9H"
FT HELIX 86..109
FT /evidence="ECO:0007829|PDB:4Z9H"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4Z9H"
FT HELIX 117..142
FT /evidence="ECO:0007829|PDB:4Z9H"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:4Z9H"
FT HELIX 154..182
FT /evidence="ECO:0007829|PDB:4Z9H"
FT TURN 215..219
FT /evidence="ECO:0007829|PDB:2L9G"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:2L9G"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:2L9G"
SQ SEQUENCE 553 AA; 59944 MW; B8DC7F2229CE7DC8 CRC64;
MINRIRVVTL LVMVLGVFAL LQLISGSLFF SSLHHSQKSF VVSNQLREQQ GELTSTWDLM
LQTRINLSRS AVRMMMDSSN QQSNAKVELL DSARKTLAQA ATHYKKFKSM APLPEMVATS
RNIDEKYKNY YTALTELIDY LDYGNTGAYF AQPTQGMQNA MGEAFAQYAL SSEKLYRDIV
TDNADDYRFA QWQLAVIALV VVLILLVAWY GIRRMLLTPL AKIIAHIREI AGGNLANTLT
IDGRSEMGDL AQSVSHMQRS LTDTVTHVRE GSDAIYAGTR EIAAGNTDLS SRTEQQASAL
EETAASMEQL TATVKQNADN ARQASQLAQS ASDTAQHGGK VVDGVVKTMH EIADSSKKIA
DIISVIDGIA FQTNILALNA AVEAARAGEQ GRGFAVVAGE VRNLASRSAQ AAKEIKALIE
DSVSRVDTGS VLVESAGETM NNIVNAVTRV TDIMGEIASA SDEQSRGIDQ VALAVSEMDR
VTQQNASLVQ ESAAAAAALE EQASRLTQAV SAFRLAASPL TNKPQTPSRP ASEQPPAQPR
LRIAEQDPNW ETF
