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P07017 (MCP2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methyl-accepting chemotaxis protein II

Short name=MCP-II
Alternative name(s):
Aspartate chemoreceptor protein
Gene names
Name:tar
Synonyms:cheM
Ordered Locus Names:b1886, JW1875
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length553 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Cell inner membrane; Multi-pass membrane protein. Note: Found predominantly at cell poles. Ref.7

Sequence similarities

Contains 1 HAMP domain.

Contains 1 methyl-accepting transducer domain.

Ontologies

Keywords
   Biological processChemotaxis
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionTransducer
   PTMMethylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchemotaxis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiontransmembrane signaling receptor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

cheWP0A9643EBI-1125130,EBI-1125947

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 553553Methyl-accepting chemotaxis protein II
PRO_0000110538

Regions

Topological domain1 – 66Cytoplasmic Ref.6 Ref.7
Transmembrane7 – 3327Helical; Potential
Topological domain34 – 190157Periplasmic Ref.6 Ref.7
Transmembrane191 – 21121Helical; Potential
Topological domain212 – 553342Cytoplasmic Ref.6 Ref.7
Domain214 – 26653HAMP
Domain271 – 500230Methyl-accepting transducer
Region64 – 7310The 3 Arg may form a positively charged pocket, which binds the alpha-carboxyl group of the attractant AA

Amino acid modifications

Modified residue2951Glutamate methyl ester (Gln)
Modified residue3021Glutamate methyl ester (Glu)
Modified residue3091Glutamate methyl ester (Gln)
Modified residue4911Glutamate methyl ester (Glu)

Experimental info

Sequence conflict1641A → R in AAA23566. Ref.1

Secondary structure

.................. 553
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07017 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: B8DC7F2229CE7DC8

FASTA55359,944
        10         20         30         40         50         60 
MINRIRVVTL LVMVLGVFAL LQLISGSLFF SSLHHSQKSF VVSNQLREQQ GELTSTWDLM 

        70         80         90        100        110        120 
LQTRINLSRS AVRMMMDSSN QQSNAKVELL DSARKTLAQA ATHYKKFKSM APLPEMVATS 

       130        140        150        160        170        180 
RNIDEKYKNY YTALTELIDY LDYGNTGAYF AQPTQGMQNA MGEAFAQYAL SSEKLYRDIV 

       190        200        210        220        230        240 
TDNADDYRFA QWQLAVIALV VVLILLVAWY GIRRMLLTPL AKIIAHIREI AGGNLANTLT 

       250        260        270        280        290        300 
IDGRSEMGDL AQSVSHMQRS LTDTVTHVRE GSDAIYAGTR EIAAGNTDLS SRTEQQASAL 

       310        320        330        340        350        360 
EETAASMEQL TATVKQNADN ARQASQLAQS ASDTAQHGGK VVDGVVKTMH EIADSSKKIA 

       370        380        390        400        410        420 
DIISVIDGIA FQTNILALNA AVEAARAGEQ GRGFAVVAGE VRNLASRSAQ AAKEIKALIE 

       430        440        450        460        470        480 
DSVSRVDTGS VLVESAGETM NNIVNAVTRV TDIMGEIASA SDEQSRGIDQ VALAVSEMDR 

       490        500        510        520        530        540 
VTQQNASLVQ ESAAAAAALE EQASRLTQAV SAFRLAASPL TNKPQTPSRP ASEQPPAQPR 

       550 
LRIAEQDPNW ETF 

« Hide

References

« Hide 'large scale' references
[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]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01705 Genomic DNA. Translation: AAA23566.1.
U00096 Genomic DNA. Translation: AAC74956.1.
AP009048 Genomic DNA. Translation: BAA15702.1.
PIRQRECM4. F64951.
RefSeqNP_416400.1. NC_000913.3.
YP_490148.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ASRX-ray2.30A38-179[»]
2L9GNMR-A214-232[»]
DisProtDP00294.
ProteinModelPortalP07017.
SMRP07017. Positions 38-179, 219-515.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10956N.
IntActP07017. 7 interactions.
STRING511145.b1886.

Proteomic databases

PaxDbP07017.
PRIDEP07017.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74956; AAC74956; b1886.
BAA15702; BAA15702; BAA15702.
GeneID12931387.
946399.
KEGGecj:Y75_p1862.
eco:b1886.
PATRIC32119099. VBIEscCol129921_1967.

Organism-specific databases

EchoBASEEB0981.
EcoGeneEG10988. tar.

Phylogenomic databases

eggNOGCOG0840.
HOGENOMHOG000148074.
KOK05875.
OMAGDDANWE.
OrthoDBEOG6G4VQG.
PhylomeDBP07017.
ProtClustDBPRK15048.

Enzyme and pathway databases

BioCycEcoCyc:TAR-MONOMER.
ECOL316407:JW1875-MONOMER.

Gene expression databases

GenevestigatorP07017.

Family and domain databases

Gene3D1.20.120.30. 1 hit.
InterProIPR004090. 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]
PfamPF00672. HAMP. 1 hit.
PF00015. MCPsignal. 1 hit.
PF02203. TarH. 1 hit.
[Graphical view]
PRINTSPR00260. CHEMTRNSDUCR.
SMARTSM00304. HAMP. 1 hit.
SM00283. MA. 1 hit.
SM00319. TarH. 1 hit.
[Graphical view]
SUPFAMSSF47170. SSF47170. 1 hit.
PROSITEPS00538. CHEMOTAXIS_TRANSDUC_1. 1 hit.
PS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
PS50885. HAMP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07017.
PROP07017.

Entry information

Entry nameMCP2_ECOLI
AccessionPrimary (citable) accession number: P07017
Secondary accession number(s): P76301
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene