Methyl-accepting chemotaxis protein II - Escherichia coli (strain K12)

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P07017 (MCP2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 138. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	553 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Chemotaxis
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Transducer
PTM	Methylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chemotaxis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	transmembrane signaling receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
cheW	P0A964	3	EBI-1125130,EBI-1125947

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 553

553

Methyl-accepting chemotaxis protein II

PRO_0000110538

Regions

Topological domain

1 – 6

Cytoplasmic Ref.6 Ref.7

Transmembrane

7 – 33

Helical; Potential

Topological domain

34 – 190

157

Periplasmic Ref.6 Ref.7

Transmembrane

191 – 211

Helical; Potential

Topological domain

212 – 553

342

Cytoplasmic Ref.6 Ref.7

Domain

214 – 266

HAMP

Domain

271 – 500

230

Methyl-accepting transducer

Region

64 – 73

The 3 Arg may form a positively charged pocket, which binds the alpha-carboxyl group of the attractant AA

Amino acid modifications

Modified residue

295

Glutamate methyl ester (Gln)

Modified residue

302

Glutamate methyl ester (Glu)

Modified residue

309

Glutamate methyl ester (Gln)

Modified residue

491

Glutamate methyl ester (Glu)

Experimental info

Sequence conflict

164

A → R in AAA23566. Ref.1

Secondary structure

553

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P07017 [UniParc].

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

FASTA

553

59,944

        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' referencesShow '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. 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 277:1453-1474(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.

PIR

QRECM4. F64951.

RefSeq

NP_416400.1. NC_000913.2.
YP_490148.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ASR	X-ray	2.30	A	38-179	[»]
2L9G	NMR	-	A	214-232	[»]

DisProt

DP00294.

ProteinModelPortal

P07017.

SMR

P07017. Positions 38-179, 219-515.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10956N.

IntAct

P07017. 7 interactions.

STRING

511145.b1886.

Proteomic databases

PaxDb

P07017.

PRIDE

P07017.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74956; AAC74956; b1886.
BAA15702; BAA15702; BAA15702.

GeneID

12931387.
946399.

KEGG

ecj:Y75_p1862.
eco:b1886.

PATRIC

32119099. VBIEscCol129921_1967.

Organism-specific databases

EchoBASE

EB0981.

EcoGene

EG10988. tar.

Phylogenomic databases

eggNOG

COG0840.

HOGENOM

HOG000148074.

K05875.

OMA

GDDANWE.

ProtClustDB

PRK15048.

Enzyme and pathway databases

BioCyc

EcoCyc:TAR-MONOMER.
ECOL316407:JW1875-MONOMER.

Gene expression databases

Genevestigator

P07017.

Family and domain databases

Gene3D

1.20.120.30. 1 hit.

InterPro

IPR004090. 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]

Pfam

PF00672. HAMP. 1 hit.
PF00015. MCPsignal. 1 hit.
PF02203. TarH. 1 hit.
[Graphical view]

PRINTS

PR00260. CHEMTRNSDUCR.

SMART

SM00304. HAMP. 1 hit.
SM00283. MA. 1 hit.
SM00319. TarH. 1 hit.
[Graphical view]

SUPFAM

SSF47170. Chemotax_Me-accpt_rcpt_lig-bd. 1 hit.

PROSITE

PS00538. CHEMOTAXIS_TRANSDUC_1. 1 hit.
PS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
PS50885. HAMP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P07017.

Entry information

Entry name

MCP2_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 138 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents