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Methyl-accepting chemotaxis protein III (MCP-III) (Ribose and galactose chemoreceptor protein)

 MCP3_ECOLI              Reviewed;         546 AA.
P05704; P77448;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 3.
28-MAR-2018, entry version 157.
RecName: Full=Methyl-accepting chemotaxis protein III;
Short=MCP-III;
AltName: Full=Ribose and galactose chemoreceptor protein;
Name=trg; OrderedLocusNames=b1421, JW1417;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6374654; DOI=10.1073/pnas.81.11.3287;
Bollinger J., Park C., Harayama S., Hazelbauer G.L.;
"Structure of the Trg protein: homologies with and differences from
other sensory transducers of Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 81:3287-3291(1984).
[2]
SEQUENCE REVISION.
Hazelbauer G.L.;
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
DEAMIDATION AT GLN-312 AND GLN-319, AND METHYLATION AT GLU-305;
GLN-312; GLN-319; GLU-501 AND GLU-510.
PubMed=6300110;
Kehry M.R., Engstrom P., Dahlquist F.W., Hazelbauer G.L.;
"Multiple covalent modifications of Trg, a sensory transducer of
Escherichia coli.";
J. Biol. Chem. 258:5050-5055(1983).
[7]
SUBCELLULAR LOCATION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[8]
SUBCELLULAR LOCATION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=22380631; DOI=10.1111/j.1365-2958.2012.08021.x;
Li G., Young K.D.;
"Isolation and identification of new inner membrane-associated
proteins that localize to cell poles in Escherichia coli.";
Mol. Microbiol. 84:276-295(2012).
-!- FUNCTION: Mediates taxis to the sugars ribose and galactose via an
interaction with the periplasmic ribose- or galactose-binding
proteins.
-!- FUNCTION: Chemotactic-signal transducers respond to changes in the
concentration of attractants and repellents in the environment,
transduce a signal from the outside to the inside of the cell, and
facilitate sensory adaptation through the variation of the level
of methylation. Attractants increase the level of methylation
while repellents decrease the level of methylation, the methyl
groups are added by the methyltransferase CheR and removed by the
methylesterase CheB.
-!- INTERACTION:
P45543:frlD; NbExp=5; IntAct=EBI-557436, EBI-562037;
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:22380631}; Multi-
pass membrane protein {ECO:0000269|PubMed:15919996,
ECO:0000269|PubMed:22380631}. Note=Found predominantly at cell
poles.
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EMBL; K02073; AAA81329.2; -; Genomic_DNA.
EMBL; U00096; AAC74503.1; -; Genomic_DNA.
EMBL; AP009048; BAA15044.1; -; Genomic_DNA.
PIR; H64893; QREC3M.
RefSeq; NP_415938.1; NC_000913.3.
RefSeq; WP_001098559.1; NZ_LN832404.1.
ProteinModelPortal; P05704; -.
SMR; P05704; -.
BioGrid; 4261384; 396.
DIP; DIP-11027N; -.
IntAct; P05704; 5.
STRING; 316385.ECDH10B_1549; -.
PaxDb; P05704; -.
PRIDE; P05704; -.
EnsemblBacteria; AAC74503; AAC74503; b1421.
EnsemblBacteria; BAA15044; BAA15044; BAA15044.
GeneID; 945995; -.
KEGG; ecj:JW1417; -.
KEGG; eco:b1421; -.
PATRIC; fig|1411691.4.peg.849; -.
EchoBASE; EB1011; -.
EcoGene; EG11018; trg.
eggNOG; ENOG4105C8Q; Bacteria.
eggNOG; COG0840; LUCA.
HOGENOM; HOG000148074; -.
InParanoid; P05704; -.
KO; K05876; -.
OMA; LQPMLKY; -.
PhylomeDB; P05704; -.
BioCyc; EcoCyc:TRG-MONOMER; -.
PRO; PR:P05704; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005887; C:integral component of plasma membrane; IMP:CAFA.
GO; GO:0098561; C:methyl accepting chemotaxis protein complex; IMP:CAFA.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
GO; GO:0004888; F:transmembrane signaling receptor activity; IMP:EcoCyc.
GO; GO:0006935; P:chemotaxis; IMP:EcoCyc.
GO; GO:0007165; P:signal transduction; IMP:EcoCyc.
CDD; cd06225; HAMP; 1.
CDD; cd00181; Tar_Tsr_LBD; 1.
InterPro; IPR035440; 4HB_MCP_dom_sf.
InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
InterPro; IPR004091; Chemotax_Me-accpt_rcpt_Me-site.
InterPro; IPR003660; HAMP_dom.
InterPro; IPR004089; MCPsignal_dom.
InterPro; IPR003122; Tar_rcpt_lig-bd.
Pfam; PF00672; HAMP; 1.
Pfam; PF00015; MCPsignal; 1.
Pfam; PF02203; TarH; 1.
PRINTS; PR00260; CHEMTRNSDUCR.
SMART; SM00304; HAMP; 1.
SMART; SM00283; MA; 1.
SMART; SM00319; TarH; 1.
SUPFAM; SSF47170; SSF47170; 1.
PROSITE; PS00538; CHEMOTAXIS_TRANSDUC_1; 1.
PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PROSITE; PS50885; HAMP; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Chemotaxis; Complete proteome;
Membrane; Methylation; Reference proteome; Transducer; Transmembrane;
Transmembrane helix.
CHAIN 1 546 Methyl-accepting chemotaxis protein III.
/FTId=PRO_0000110540.
TOPO_DOM 1 23 Cytoplasmic. {ECO:0000255}.
TRANSMEM 24 44 Helical. {ECO:0000255}.
TOPO_DOM 45 201 Periplasmic. {ECO:0000255}.
TRANSMEM 202 222 Helical. {ECO:0000255}.
TOPO_DOM 223 546 Cytoplasmic. {ECO:0000255}.
DOMAIN 224 276 HAMP. {ECO:0000255|PROSITE-
ProRule:PRU00102}.
DOMAIN 281 510 Methyl-accepting transducer.
{ECO:0000255|PROSITE-ProRule:PRU00284}.
MOD_RES 305 305 Glutamate methyl ester (Glu).
{ECO:0000269|PubMed:6300110,
ECO:0000269|PubMed:6374654}.
MOD_RES 312 312 Glutamate methyl ester (Gln).
{ECO:0000269|PubMed:6300110,
ECO:0000269|PubMed:6374654}.
MOD_RES 319 319 Glutamate methyl ester (Gln).
{ECO:0000269|PubMed:6300110,
ECO:0000269|PubMed:6374654}.
MOD_RES 501 501 Glutamate methyl ester (Glu).
{ECO:0000269|PubMed:6300110,
ECO:0000269|PubMed:6374654}.
MOD_RES 510 510 Glutamate methyl ester (Glu).
{ECO:0000269|PubMed:6300110}.
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


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