MCP3_ECOLI
ID MCP3_ECOLI Reviewed; 546 AA.
AC P05704; P77448;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Methyl-accepting chemotaxis protein III;
DE Short=MCP-III;
DE AltName: Full=Ribose and galactose chemoreceptor protein;
GN Name=trg; OrderedLocusNames=b1421, JW1417;
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=6374654; DOI=10.1073/pnas.81.11.3287;
RA Bollinger J., Park C., Harayama S., Hazelbauer G.L.;
RT "Structure of the Trg protein: homologies with and differences from other
RT sensory transducers of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:3287-3291(1984).
RN [2]
RP SEQUENCE REVISION.
RA Hazelbauer G.L.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
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 [5]
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 [6]
RP DEAMIDATION AT GLN-312 AND GLN-319, AND METHYLATION AT GLU-305; GLN-312;
RP GLN-319; GLU-501 AND GLU-510.
RX PubMed=6300110; DOI=10.1016/s0021-9258(18)32536-5;
RA Kehry M.R., Engstrom P., Dahlquist F.W., Hazelbauer G.L.;
RT "Multiple covalent modifications of Trg, a sensory transducer of
RT Escherichia coli.";
RL J. Biol. Chem. 258:5050-5055(1983).
RN [7]
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 [8]
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).
CC -!- FUNCTION: Mediates taxis to the sugars ribose and galactose via an
CC interaction with the periplasmic ribose- or galactose-binding proteins.
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 P05704; P45543: frlD; NbExp=5; IntAct=EBI-557436, EBI-562037;
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; K02073; AAA81329.2; -; Genomic_DNA.
DR EMBL; U00096; AAC74503.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15044.1; -; Genomic_DNA.
DR PIR; H64893; QREC3M.
DR RefSeq; NP_415938.1; NC_000913.3.
DR RefSeq; WP_001098559.1; NZ_STEB01000005.1.
DR AlphaFoldDB; P05704; -.
DR SMR; P05704; -.
DR BioGRID; 4261384; 396.
DR BioGRID; 850357; 1.
DR DIP; DIP-11027N; -.
DR IntAct; P05704; 5.
DR STRING; 511145.b1421; -.
DR PaxDb; P05704; -.
DR PRIDE; P05704; -.
DR EnsemblBacteria; AAC74503; AAC74503; b1421.
DR EnsemblBacteria; BAA15044; BAA15044; BAA15044.
DR GeneID; 945995; -.
DR KEGG; ecj:JW1417; -.
DR KEGG; eco:b1421; -.
DR PATRIC; fig|1411691.4.peg.849; -.
DR EchoBASE; EB1011; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_16_6; -.
DR InParanoid; P05704; -.
DR OMA; AYQNRSV; -.
DR PhylomeDB; P05704; -.
DR BioCyc; EcoCyc:TRG-MON; -.
DR PRO; PR:P05704; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:CAFA.
DR GO; GO:0098561; C:methyl accepting chemotaxis protein complex; IMP:CAFA.
DR GO; GO:0005886; C:plasma membrane; 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:0006935; P:chemotaxis; IMP:EcoCyc.
DR GO; GO:0007165; P:signal transduction; IMP:EcoCyc.
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 Cell inner membrane; Cell membrane; Chemotaxis; Membrane; Methylation;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..546
FT /note="Methyl-accepting chemotaxis protein III"
FT /id="PRO_0000110540"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..201
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 224..276
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 281..510
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT MOD_RES 305
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:6300110,
FT ECO:0000269|PubMed:6374654"
FT MOD_RES 312
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000269|PubMed:6300110,
FT ECO:0000269|PubMed:6374654"
FT MOD_RES 319
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000269|PubMed:6300110,
FT ECO:0000269|PubMed:6374654"
FT MOD_RES 501
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:6300110,
FT ECO:0000269|PubMed:6374654"
FT MOD_RES 510
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:6300110"
SQ SEQUENCE 546 AA; 58899 MW; FDB40374C0E83E7B CRC64;
MNTTPSQRLG FLHHIRLVPL FACILGGILV LFALSSALAG YFLWQADRDQ RDVTAEIEIR
TGLANSSDFL RSARINMIQA GAASRIAEME AMKRNIAQAE SEIKQSQQGY RAYQNRPVKT
PADEALDTEL NQRFQAYITG MQPMLKYAKN GMFEAIINHE SEQIRPLDNA YTDILNKAVK
IRSTRANQLA ELAHQRTRLG GMFMIGAFVL ALVMTLITFM VLRRIVIRPL QHAAQRIEKI
ASGDLTMNDE PAGRNEIGRL SRHLQQMQHS LGMTVGTVRQ GAEEIYRGTS EISAGNADLS
SRTEEQAAAI EQTAASMEQL TATVKQNADN AHHASKLAQE ASIKASDGGQ TVSGVVKTMG
AISTSSKKIS EITAVINSIA FQTNILALNA AVEAARAGEQ GRGFAVVASE VRTLASRSAQ
AAKEIEGLIS ESVRLIDLGS DEVATAGKTM STIVDAVASV THIMQEIAAA SDEQSRGITQ
VSQAISEMDK VTQQNASLVE EASAAAVSLE EQAARLTEAV DVFRLHKHSV SAEPRGAGEP
VSFATV
