ID MCP1_ECOLI Reviewed; 551 AA.
AC P02942; P76817; Q2M5W1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 27-MAR-2024, entry version 200.
DE RecName: Full=Methyl-accepting chemotaxis protein I;
DE Short=MCP-I;
DE AltName: Full=Serine chemoreceptor protein;
GN Name=tsr; Synonyms=cheD; OrderedLocusNames=b4355, JW4318;
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=6402709; DOI=10.1038/301623a0;
RA Boyd A., Kendall K., Simon M.I.;
RT "Structure of the serine chemoreceptor in Escherichia coli.";
RL Nature 301:623-626(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
RC STRAIN=C;
RX PubMed=8384293; DOI=10.1007/bf00282806;
RA Roper D.I., Fawcett T., Cooper R.A.;
RT "The Escherichia coli C homoprotocatechuate degradative operon: hpc gene
RT order, direction of transcription and control of expression.";
RL Mol. Gen. Genet. 237:241-250(1993).
RN [6]
RP PROTEIN SEQUENCE OF 295-317 AND 483-507, AND METHYLATION.
RX PubMed=6213619; DOI=10.1016/s0021-9258(18)34030-4;
RA Kehry M.R., Dahlquist F.W.;
RT "The methyl-accepting chemotaxis proteins of Escherichia coli.
RT Identification of the multiple methylation sites on methyl-accepting
RT chemotaxis protein I.";
RL J. Biol. Chem. 257:10378-10386(1982).
RN [7]
RP METHYLATION AT GLN-297; GLU-304; GLN-311; GLU-493 AND GLU-502, AND
RP DEAMIDATION AT GLN-297 AND GLN-311.
RX PubMed=2033064; DOI=10.1016/s0021-9258(18)92884-x;
RA Rice M.S., Dahlquist F.W.;
RT "Sites of deamidation and methylation in Tsr, a bacterial chemotaxis
RT sensory transducer.";
RL J. Biol. Chem. 266:9746-9753(1991).
RN [8]
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 [9]
RP SUBCELLULAR LOCATION.
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 [10]
RP SUBCELLULAR LOCATION.
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 294-520.
RX PubMed=10466731; DOI=10.1038/23512;
RA Kim K.K., Yokota H., Kim S.-H.;
RT "Four-helical-bundle structure of the cytoplasmic domain of a serine
RT chemotaxis receptor.";
RL Nature 400:787-792(1999).
CC -!- FUNCTION: Receptor for the attractant L-serine and related amino acids.
CC Is also responsible for chemotaxis away from a wide range of
CC repellents, including leucine, indole, and weak acids.
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 {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:22380631}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:22380631}. Note=Found
CC predominantly at cell poles.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; V00373; CAA23676.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U14003; AAA97252.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77311.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78345.1; -; Genomic_DNA.
DR EMBL; S56952; AAB25802.1; -; Genomic_DNA.
DR PIR; E65250; QRECS.
DR RefSeq; NP_418775.1; NC_000913.3.
DR RefSeq; WP_000919536.1; NZ_LN832404.1.
DR PDB; 1QU7; X-ray; 2.60 A; A/B=294-520.
DR PDB; 2D4U; X-ray; 1.95 A; A/B=25-190.
DR PDB; 3ATP; X-ray; 2.50 A; A/B=25-190.
DR PDB; 3ZX6; X-ray; 2.65 A; A/B=264-551.
DR PDB; 6S1K; EM; 8.38 A; E/F/G/H/I/J/K/L/M/N/O/P=1-551.
DR PDB; 8C5V; EM; 12.00 A; I/J/K/L/M/N/O/P/Q/R/S/T=1-516.
DR PDBsum; 1QU7; -.
DR PDBsum; 2D4U; -.
DR PDBsum; 3ATP; -.
DR PDBsum; 3ZX6; -.
DR PDBsum; 6S1K; -.
DR PDBsum; 8C5V; -.
DR AlphaFoldDB; P02942; -.
DR SMR; P02942; -.
DR BioGRID; 4261744; 203.
DR BioGRID; 853162; 1.
DR DIP; DIP-11046N; -.
DR IntAct; P02942; 4.
DR MINT; P02942; -.
DR STRING; 511145.b4355; -.
DR PaxDb; 511145-b4355; -.
DR EnsemblBacteria; AAC77311; AAC77311; b4355.
DR GeneID; 948884; -.
DR KEGG; ecj:JW4318; -.
DR KEGG; eco:b4355; -.
DR PATRIC; fig|1411691.4.peg.2331; -.
DR EchoBASE; EB1027; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_16_6; -.
DR InParanoid; P02942; -.
DR OMA; TTRIDFH; -.
DR OrthoDB; 9765776at2; -.
DR PhylomeDB; P02942; -.
DR BioCyc; EcoCyc:TSR-MONOMER; -.
DR EvolutionaryTrace; P02942; -.
DR PRO; PR:P02942; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0098561; C:methyl accepting chemotaxis protein complex; IMP:CAFA.
DR GO; GO:0005886; C:plasma membrane; IMP:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:CAFA.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0048870; P:cell motility; IMP:CACAO.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:CAFA.
DR GO; GO:0006935; P:chemotaxis; IMP:CACAO.
DR GO; GO:0009593; P:detection of chemical stimulus; IMP:CAFA.
DR GO; GO:0043113; P:receptor clustering; IMP:CAFA.
DR GO; GO:1902021; P:regulation of bacterial-type flagellum-dependent cell motility; IMP:CAFA.
DR GO; GO:0050920; P:regulation of chemotaxis; IMP:CAFA.
DR GO; GO:0032110; P:regulation of protein histidine kinase activity; IMP:CAFA.
DR GO; GO:0007172; P:signal complex assembly; IMP:CAFA.
DR GO; GO:0007165; P:signal transduction; IMP:CACAO.
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:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 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;
KW Direct protein sequencing; Membrane; Methylation; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..551
FT /note="Methyl-accepting chemotaxis protein I"
FT /id="PRO_0000110537"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..190
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..551
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 216..268
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 273..502
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 MOD_RES 297
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000269|PubMed:2033064,
FT ECO:0000269|PubMed:6402709"
FT MOD_RES 304
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:2033064,
FT ECO:0000269|PubMed:6402709"
FT MOD_RES 311
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000269|PubMed:2033064,
FT ECO:0000269|PubMed:6402709"
FT MOD_RES 493
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:2033064,
FT ECO:0000269|PubMed:6402709"
FT MOD_RES 502
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:2033064"
FT HELIX 25..78
FT /evidence="ECO:0007829|PDB:2D4U"
FT HELIX 87..110
FT /evidence="ECO:0007829|PDB:2D4U"
FT HELIX 119..144
FT /evidence="ECO:0007829|PDB:2D4U"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:2D4U"
FT HELIX 156..186
FT /evidence="ECO:0007829|PDB:2D4U"
FT HELIX 296..328
FT /evidence="ECO:0007829|PDB:1QU7"
FT HELIX 332..360
FT /evidence="ECO:0007829|PDB:1QU7"
FT HELIX 362..388
FT /evidence="ECO:0007829|PDB:1QU7"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:1QU7"
FT HELIX 393..438
FT /evidence="ECO:0007829|PDB:1QU7"
FT HELIX 441..448
FT /evidence="ECO:0007829|PDB:1QU7"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:1QU7"
FT HELIX 452..515
FT /evidence="ECO:0007829|PDB:1QU7"
SQ SEQUENCE 551 AA; 59443 MW; E8DB026029989B0F CRC64;
MLKRIKIVTS LLLVLAVFGL LQLTSGGLFF NALKNDKENF TVLQTIRQQQ STLNGSWVAL
LQTRNTLNRA GIRYMMDQNN IGSGSTVAEL MESASISLKQ AEKNWADYEA LPRDPRQSTA
AAAEIKRNYD IYHNALAELI QLLGAGKINE FFDQPTQGYQ DGFEKQYVAY MEQNDRLHDI
AVSDNNASYS QAMWILVGVM IVVLAVIFAV WFGIKASLVA PMNRLIDSIR HIAGGDLVKP
IEVDGSNEMG QLAESLRHMQ GELMRTVGDV RNGANAIYSG ASEIATGNND LSSRTEQQAA
SLEETAASME QLTATVKQNA ENARQASHLA LSASETAQRG GKVVDNVVQT MRDISTSSQK
IADIISVIDG IAFQTNILAL NAAVEAARAG EQGRGFAVVA GEVRNLAQRS AQAAREIKSL
IEDSVGKVDV GSTLVESAGE TMAEIVSAVT RVTDIMGEIA SASDEQSRGI DQVGLAVAEM
DRVTQQNAAL VEESAAAAAA LEEQASRLTE AVAVFRIQQQ QRETSAVVKT VTPAAPRKMA
VADSEENWET F
//
