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Protein

Methyl-accepting chemotaxis protein III

Gene

trg

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Mediates taxis to the sugars ribose and galactose via an interaction with the periplasmic ribose- or galactose-binding proteins.
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.

GO - Molecular functioni

  • transmembrane signaling receptor activity Source: EcoCyc

GO - Biological processi

  • chemotaxis Source: EcoCyc
  • signal transduction Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Biological processi

Chemotaxis

Enzyme and pathway databases

BioCyciEcoCyc:TRG-MONOMER.
ECOL316407:JW1417-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-accepting chemotaxis protein III
Short name:
MCP-III
Alternative name(s):
Ribose and galactose chemoreceptor protein
Gene namesi
Name:trg
Ordered Locus Names:b1421, JW1417
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11018. trg.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2323CytoplasmicSequence analysisAdd
BLAST
Transmembranei24 – 4421HelicalSequence analysisAdd
BLAST
Topological domaini45 – 201157PeriplasmicSequence analysisAdd
BLAST
Transmembranei202 – 22221HelicalSequence analysisAdd
BLAST
Topological domaini223 – 546324CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 546546Methyl-accepting chemotaxis protein IIIPRO_0000110540Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei305 – 3051Glutamate methyl ester (Glu)2 Publications
Modified residuei312 – 3121Glutamate methyl ester (Gln)2 Publications
Modified residuei319 – 3191Glutamate methyl ester (Gln)2 Publications
Modified residuei501 – 5011Glutamate methyl ester (Glu)2 Publications
Modified residuei510 – 5101Glutamate methyl ester (Glu)1 Publication

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP05704.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
frlDP455435EBI-557436,EBI-562037

Protein-protein interaction databases

BioGridi4261384. 311 interactions.
DIPiDIP-11027N.
IntActiP05704. 5 interactions.
MINTiMINT-1228342.
STRINGi511145.b1421.

Structurei

3D structure databases

ProteinModelPortaliP05704.
SMRiP05704. Positions 226-528.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini224 – 27653HAMPPROSITE-ProRule annotationAdd
BLAST
Domaini281 – 510230Methyl-accepting transducerPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HAMP domain.PROSITE-ProRule annotation
Contains 1 methyl-accepting transducer domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C8Q. Bacteria.
COG0840. LUCA.
HOGENOMiHOG000148074.
InParanoidiP05704.
KOiK05876.
OMAiNRHLQQM.
OrthoDBiEOG6G4VQG.
PhylomeDBiP05704.

Family and domain databases

Gene3Di1.20.120.30. 1 hit.
InterProiIPR004090. Chemotax_Me-accpt_rcpt.
IPR003122. Chemotax_Me-accpt_rcpt_lig-bd.
IPR004091. Chemotax_Me-accpt_rcpt_Me-site.
IPR003660. HAMP_dom.
IPR004089. MCPsignal_dom.
[Graphical view]
PfamiPF00672. HAMP. 1 hit.
PF00015. MCPsignal. 1 hit.
PF02203. TarH. 1 hit.
[Graphical view]
PRINTSiPR00260. CHEMTRNSDUCR.
SMARTiSM00304. HAMP. 1 hit.
SM00283. MA. 1 hit.
SM00319. TarH. 1 hit.
[Graphical view]
SUPFAMiSSF47170. SSF47170. 1 hit.
PROSITEiPS00538. CHEMOTAXIS_TRANSDUC_1. 1 hit.
PS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
PS50885. HAMP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05704-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTTPSQRLG FLHHIRLVPL FACILGGILV LFALSSALAG YFLWQADRDQ
60 70 80 90 100
RDVTAEIEIR TGLANSSDFL RSARINMIQA GAASRIAEME AMKRNIAQAE
110 120 130 140 150
SEIKQSQQGY RAYQNRPVKT PADEALDTEL NQRFQAYITG MQPMLKYAKN
160 170 180 190 200
GMFEAIINHE SEQIRPLDNA YTDILNKAVK IRSTRANQLA ELAHQRTRLG
210 220 230 240 250
GMFMIGAFVL ALVMTLITFM VLRRIVIRPL QHAAQRIEKI ASGDLTMNDE
260 270 280 290 300
PAGRNEIGRL SRHLQQMQHS LGMTVGTVRQ GAEEIYRGTS EISAGNADLS
310 320 330 340 350
SRTEEQAAAI EQTAASMEQL TATVKQNADN AHHASKLAQE ASIKASDGGQ
360 370 380 390 400
TVSGVVKTMG AISTSSKKIS EITAVINSIA FQTNILALNA AVEAARAGEQ
410 420 430 440 450
GRGFAVVASE VRTLASRSAQ AAKEIEGLIS ESVRLIDLGS DEVATAGKTM
460 470 480 490 500
STIVDAVASV THIMQEIAAA SDEQSRGITQ VSQAISEMDK VTQQNASLVE
510 520 530 540
EASAAAVSLE EQAARLTEAV DVFRLHKHSV SAEPRGAGEP VSFATV
Length:546
Mass (Da):58,899
Last modified:November 1, 1997 - v3
Checksum:iFDB40374C0E83E7B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02073 Genomic DNA. Translation: AAA81329.2.
U00096 Genomic DNA. Translation: AAC74503.1.
AP009048 Genomic DNA. Translation: BAA15044.1.
PIRiH64893. QREC3M.
RefSeqiNP_415938.1. NC_000913.3.
WP_001098559.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74503; AAC74503; b1421.
BAA15044; BAA15044; BAA15044.
GeneIDi945995.
KEGGiecj:JW1417.
eco:b1421.
PATRICi32118128. VBIEscCol129921_1484.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02073 Genomic DNA. Translation: AAA81329.2.
U00096 Genomic DNA. Translation: AAC74503.1.
AP009048 Genomic DNA. Translation: BAA15044.1.
PIRiH64893. QREC3M.
RefSeqiNP_415938.1. NC_000913.3.
WP_001098559.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP05704.
SMRiP05704. Positions 226-528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261384. 311 interactions.
DIPiDIP-11027N.
IntActiP05704. 5 interactions.
MINTiMINT-1228342.
STRINGi511145.b1421.

Proteomic databases

PaxDbiP05704.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74503; AAC74503; b1421.
BAA15044; BAA15044; BAA15044.
GeneIDi945995.
KEGGiecj:JW1417.
eco:b1421.
PATRICi32118128. VBIEscCol129921_1484.

Organism-specific databases

EchoBASEiEB1011.
EcoGeneiEG11018. trg.

Phylogenomic databases

eggNOGiENOG4105C8Q. Bacteria.
COG0840. LUCA.
HOGENOMiHOG000148074.
InParanoidiP05704.
KOiK05876.
OMAiNRHLQQM.
OrthoDBiEOG6G4VQG.
PhylomeDBiP05704.

Enzyme and pathway databases

BioCyciEcoCyc:TRG-MONOMER.
ECOL316407:JW1417-MONOMER.

Miscellaneous databases

PROiP05704.

Family and domain databases

Gene3Di1.20.120.30. 1 hit.
InterProiIPR004090. Chemotax_Me-accpt_rcpt.
IPR003122. Chemotax_Me-accpt_rcpt_lig-bd.
IPR004091. Chemotax_Me-accpt_rcpt_Me-site.
IPR003660. HAMP_dom.
IPR004089. MCPsignal_dom.
[Graphical view]
PfamiPF00672. HAMP. 1 hit.
PF00015. MCPsignal. 1 hit.
PF02203. TarH. 1 hit.
[Graphical view]
PRINTSiPR00260. CHEMTRNSDUCR.
SMARTiSM00304. HAMP. 1 hit.
SM00283. MA. 1 hit.
SM00319. TarH. 1 hit.
[Graphical view]
SUPFAMiSSF47170. SSF47170. 1 hit.
PROSITEiPS00538. CHEMOTAXIS_TRANSDUC_1. 1 hit.
PS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
PS50885. HAMP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the Trg protein: homologies with and differences from other sensory transducers of Escherichia coli."
    Bollinger J., Park C., Harayama S., Hazelbauer G.L.
    Proc. Natl. Acad. Sci. U.S.A. 81:3287-3291(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Hazelbauer G.L.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Multiple covalent modifications of Trg, a sensory transducer of Escherichia coli."
    Kehry M.R., Engstrom P., Dahlquist F.W., Hazelbauer G.L.
    J. Biol. Chem. 258:5050-5055(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEAMIDATION AT GLN-312 AND GLN-319, METHYLATION AT GLU-305; GLN-312; GLN-319; GLU-501 AND GLU-510.
  7. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  8. "Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli."
    Li G., Young K.D.
    Mol. Microbiol. 84:276-295(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiMCP3_ECOLI
AccessioniPrimary (citable) accession number: P05704
Secondary accession number(s): P77448
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1997
Last modified: January 20, 2016
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.