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   27-MAR-2024, entry version 200.
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; Pseudomonadota; 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AH000879; 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   EMDB; EMD-3234; -.
DR   EMDB; EMD-6319; -.
DR   EMDB; EMD-6320; -.
DR   SMR; P07017; -.
DR   BioGRID; 4260381; 319.
DR   DIP; DIP-10956N; -.
DR   IntAct; P07017; 7.
DR   STRING; 511145.b1886; -.
DR   MoonProt; P07017; -.
DR   PaxDb; 511145-b1886; -.
DR   EnsemblBacteria; AAC74956; AAC74956; b1886.
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   OrthoDB; 9765776at2; -.
DR   PhylomeDB; P07017; -.
DR   BioCyc; EcoCyc:TAR-MONOMER; -.
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:0098561; C:methyl accepting chemotaxis protein complex; IDA:CAFA.
DR   GO; GO:0005886; C:plasma membrane; 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; IDA:EcoCyc.
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:0051260; P:protein homooligomerization; IMP:EcoCyc.
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; 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   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
//