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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 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)DescriptionActionsGraphical viewLength
Topological domaini1 – 6Cytoplasmic6
Transmembranei7 – 33HelicalSequence analysisAdd BLAST27
Topological domaini34 – 190PeriplasmicAdd BLAST157
Transmembranei191 – 211HelicalSequence analysisAdd BLAST21
Topological domaini212 – 553CytoplasmicAdd BLAST342

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001105381 – 553Methyl-accepting chemotaxis protein IIAdd BLAST553

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei295Glutamate methyl ester (Gln)By similarity1
Modified residuei302Glutamate methyl ester (Glu)By similarity1
Modified residuei309Glutamate methyl ester (Gln)By similarity1
Modified residuei491Glutamate methyl ester (Glu)By similarity1
Modified residuei500Glutamate methyl ester (Glu)By similarity1

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP07017.
PRIDEiP07017.

Interactioni

Binary interactionsi

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

GO - Molecular functioni

  • protein histidine kinase binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4260381. 311 interactors.
DIPiDIP-10956N.
IntActiP07017. 7 interactors.
STRINGi511145.b1886.

Structurei

Secondary structure

1553
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi37 – 74Combined sources38
Helixi81 – 85Combined sources5
Helixi86 – 109Combined sources24
Helixi114 – 116Combined sources3
Helixi117 – 142Combined sources26
Helixi146 – 151Combined sources6
Helixi154 – 182Combined sources29
Turni215 – 219Combined sources5
Helixi220 – 226Combined sources7
Turni227 – 230Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ASRX-ray2.30A38-179[»]
2L9GNMR-A214-232[»]
4Z9HX-ray1.45A/B26-193[»]
4Z9IX-ray1.57A/B26-193[»]
4Z9JX-ray1.78A/B26-193[»]
DisProtiDP00294.
ProteinModelPortaliP07017.
SMRiP07017.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07017.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini214 – 266HAMPPROSITE-ProRule annotationAdd BLAST53
Domaini271 – 500Methyl-accepting transducerPROSITE-ProRule annotationAdd BLAST230

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni64 – 73The 3 Arg may form a positively charged pocket, which binds the alpha-carboxyl group of the attractant AA10

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.
InParanoidiP07017.
KOiK05875.
OMAiGDDANWE.
PhylomeDBiP07017.

Family and domain databases

CDDicd06225. HAMP. 1 hit.
cd00181. Tar_Tsr_LBD. 1 hit.
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.

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)DescriptionActionsGraphical viewLength
Sequence conflicti164A → R in AAA23566 (PubMed:6305515).Curated1

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.
WP_001297437.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74956; AAC74956; b1886.
BAA15702; BAA15702; BAA15702.
GeneIDi946399.
KEGGiecj:JW1875.
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.
WP_001297437.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ASRX-ray2.30A38-179[»]
2L9GNMR-A214-232[»]
4Z9HX-ray1.45A/B26-193[»]
4Z9IX-ray1.57A/B26-193[»]
4Z9JX-ray1.78A/B26-193[»]
DisProtiDP00294.
ProteinModelPortaliP07017.
SMRiP07017.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260381. 311 interactors.
DIPiDIP-10956N.
IntActiP07017. 7 interactors.
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:JW1875.
eco:b1886.
PATRICi32119099. VBIEscCol129921_1967.

Organism-specific databases

EchoBASEiEB0981.
EcoGeneiEG10988. tar.

Phylogenomic databases

eggNOGiENOG4105C8Q. Bacteria.
COG0840. LUCA.
HOGENOMiHOG000148074.
InParanoidiP07017.
KOiK05875.
OMAiGDDANWE.
PhylomeDBiP07017.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP07017.
PROiP07017.

Family and domain databases

CDDicd06225. HAMP. 1 hit.
cd00181. Tar_Tsr_LBD. 1 hit.
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...

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: November 2, 2016
This is version 161 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

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.