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Protein

Methyl-accepting chemotaxis protein II

Gene

tar

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

Functioni

Receptor for the attractant L-aspartate and related amino and dicarboxylic acids. Tar also mediates taxis to the attractant maltose via an interaction with the periplasmic maltose binding protein. Tar mediates taxis away from the repellents cobalt and nickel.
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

  • protein histidine kinase binding Source: EcoCyc
  • signal transducer activity Source: EcoCyc
  • transmembrane signaling receptor activity Source: EcoCyc

GO - Biological processi

  • chemotaxis Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Biological processi

Chemotaxis

Enzyme and pathway databases

BioCyciEcoCyc:TAR-MONOMER.
ECOL316407:JW1875-MONOMER.

Protein family/group databases

MoonProtiP07017.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-accepting chemotaxis protein II
Short name:
MCP-II
Alternative name(s):
Aspartate chemoreceptor protein
Gene namesi
Name:tar
Synonyms:cheM
Ordered Locus Names:b1886, JW1875
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10988. tar.

Subcellular locationi

  • Cell inner membrane 1 Publication; Multi-pass membrane protein 1 Publication

  • Note: Found predominantly at cell poles.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66Cytoplasmic
Transmembranei7 – 3327HelicalSequence AnalysisAdd
BLAST
Topological domaini34 – 190157PeriplasmicAdd
BLAST
Transmembranei191 – 21121HelicalSequence AnalysisAdd
BLAST
Topological domaini212 – 553342CytoplasmicAdd
BLAST

GO - Cellular componenti

  • integral component of 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 – 553553Methyl-accepting chemotaxis protein IIPRO_0000110538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei295 – 2951Glutamate methyl ester (Gln)By similarity
Modified residuei302 – 3021Glutamate methyl ester (Glu)By similarity
Modified residuei309 – 3091Glutamate methyl ester (Gln)By similarity
Modified residuei491 – 4911Glutamate methyl ester (Glu)By similarity
Modified residuei500 – 5001Glutamate methyl ester (Glu)By similarity

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP07017.
PRIDEiP07017.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
cheWP0A9643EBI-1125130,EBI-1125947

Protein-protein interaction databases

DIPiDIP-10956N.
IntActiP07017. 7 interactions.
STRINGi511145.b1886.

Structurei

Secondary structure

1
553
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi39 – 7537Combined sources
Helixi81 – 855Combined sources
Helixi86 – 10924Combined sources
Helixi114 – 1163Combined sources
Helixi117 – 14125Combined sources
Turni142 – 1443Combined sources
Helixi146 – 1516Combined sources
Helixi154 – 17623Combined sources
Turni215 – 2195Combined sources
Helixi220 – 2267Combined sources
Turni227 – 2304Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ASRX-ray2.30A38-179[»]
2L9GNMR-A214-232[»]
DisProtiDP00294.
ProteinModelPortaliP07017.
SMRiP07017. Positions 38-179, 219-515.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07017.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini214 – 26653HAMPPROSITE-ProRule annotationAdd
BLAST
Domaini271 – 500230Methyl-accepting transducerPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 7310The 3 Arg may form a positively charged pocket, which binds the alpha-carboxyl group of the attractant AA

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

eggNOGiCOG0840.
HOGENOMiHOG000148074.
InParanoidiP07017.
KOiK05875.
OMAiGDDANWE.
OrthoDBiEOG6G4VQG.
PhylomeDBiP07017.

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_linker_domain.
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.

P07017-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MINRIRVVTL LVMVLGVFAL LQLISGSLFF SSLHHSQKSF VVSNQLREQQ
60 70 80 90 100
GELTSTWDLM LQTRINLSRS AVRMMMDSSN QQSNAKVELL DSARKTLAQA
110 120 130 140 150
ATHYKKFKSM APLPEMVATS RNIDEKYKNY YTALTELIDY LDYGNTGAYF
160 170 180 190 200
AQPTQGMQNA MGEAFAQYAL SSEKLYRDIV TDNADDYRFA QWQLAVIALV
210 220 230 240 250
VVLILLVAWY GIRRMLLTPL AKIIAHIREI AGGNLANTLT IDGRSEMGDL
260 270 280 290 300
AQSVSHMQRS LTDTVTHVRE GSDAIYAGTR EIAAGNTDLS SRTEQQASAL
310 320 330 340 350
EETAASMEQL TATVKQNADN ARQASQLAQS ASDTAQHGGK VVDGVVKTMH
360 370 380 390 400
EIADSSKKIA DIISVIDGIA FQTNILALNA AVEAARAGEQ GRGFAVVAGE
410 420 430 440 450
VRNLASRSAQ AAKEIKALIE DSVSRVDTGS VLVESAGETM NNIVNAVTRV
460 470 480 490 500
TDIMGEIASA SDEQSRGIDQ VALAVSEMDR VTQQNASLVQ ESAAAAAALE
510 520 530 540 550
EQASRLTQAV SAFRLAASPL TNKPQTPSRP ASEQPPAQPR LRIAEQDPNW

ETF
Length:553
Mass (Da):59,944
Last modified:November 1, 1997 - v2
Checksum:iB8DC7F2229CE7DC8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 1641A → R in AAA23566 (PubMed:6305515).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01705 Genomic DNA. Translation: AAA23566.1.
U00096 Genomic DNA. Translation: AAC74956.1.
AP009048 Genomic DNA. Translation: BAA15702.1.
PIRiF64951. QRECM4.
RefSeqiNP_416400.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC74956; AAC74956; b1886.
BAA15702; BAA15702; BAA15702.
GeneIDi946399.
KEGGiecj:Y75_p1862.
eco:b1886.
PATRICi32119099. VBIEscCol129921_1967.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01705 Genomic DNA. Translation: AAA23566.1.
U00096 Genomic DNA. Translation: AAC74956.1.
AP009048 Genomic DNA. Translation: BAA15702.1.
PIRiF64951. QRECM4.
RefSeqiNP_416400.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ASRX-ray2.30A38-179[»]
2L9GNMR-A214-232[»]
DisProtiDP00294.
ProteinModelPortaliP07017.
SMRiP07017. Positions 38-179, 219-515.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10956N.
IntActiP07017. 7 interactions.
STRINGi511145.b1886.

Protein family/group databases

MoonProtiP07017.

Proteomic databases

PaxDbiP07017.
PRIDEiP07017.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74956; AAC74956; b1886.
BAA15702; BAA15702; BAA15702.
GeneIDi946399.
KEGGiecj:Y75_p1862.
eco:b1886.
PATRICi32119099. VBIEscCol129921_1967.

Organism-specific databases

EchoBASEiEB0981.
EcoGeneiEG10988. tar.

Phylogenomic databases

eggNOGiCOG0840.
HOGENOMiHOG000148074.
InParanoidiP07017.
KOiK05875.
OMAiGDDANWE.
OrthoDBiEOG6G4VQG.
PhylomeDBiP07017.

Enzyme and pathway databases

BioCyciEcoCyc:TAR-MONOMER.
ECOL316407:JW1875-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP07017.
PROiP07017.

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_linker_domain.
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. "Sensory transducers of E. coli are composed of discrete structural and functional domains."
    Krikos A., Mutoh N., Boyd A., Simon M.I.
    Cell 33:615-622(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  6. "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: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  7. "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, TOPOLOGY.
    Strain: K12 / MG1655 / ATCC 47076.
  8. "The three-dimensional structure of the aspartate receptor from Escherichia coli."
    Bowie J.U., Pakula A.A., Simon M.I.
    Acta Crystallogr. D 51:145-154(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 38-179.
  9. "Apo structure of the ligand-binding domain of aspartate receptor from Escherichia coli and its comparison with ligand-bound or pseudoligand-bound structures."
    Chi Y.-I., Yokota H., Kim S.-H.
    FEBS Lett. 414:327-332(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 38-180.

Entry informationi

Entry nameiMCP2_ECOLI
AccessioniPrimary (citable) accession number: P07017
Secondary accession number(s): P76301
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: June 24, 2015
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.