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P07017

- MCP2_ECOLI

UniProt

P07017 - MCP2_ECOLI

Protein

Methyl-accepting chemotaxis protein II

Gene

tar

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    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

    1. protein binding Source: IntAct
    2. protein histidine kinase binding Source: EcoCyc
    3. signal transducer activity Source: EcoCyc
    4. transmembrane signaling receptor activity Source: EcoCyc

    GO - Biological processi

    1. chemotaxis Source: EcoCyc

    Keywords - Molecular functioni

    Transducer

    Keywords - Biological processi

    Chemotaxis

    Enzyme and pathway databases

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

    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: Chromosome, UP000000625: 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.

    GO - Cellular componenti

    1. integral component of plasma membrane Source: EcoCyc

    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)
    Modified residuei302 – 3021Glutamate methyl ester (Glu)
    Modified residuei309 – 3091Glutamate methyl ester (Gln)
    Modified residuei491 – 4911Glutamate methyl ester (Glu)

    Keywords - PTMi

    Methylation

    Proteomic databases

    PaxDbiP07017.
    PRIDEiP07017.

    Expressioni

    Gene expression databases

    GenevestigatoriP07017.

    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 – 7537
    Helixi81 – 855
    Helixi86 – 10924
    Helixi114 – 1163
    Helixi117 – 14125
    Turni142 – 1443
    Helixi146 – 1516
    Helixi154 – 17623
    Turni215 – 2195
    Helixi220 – 2267
    Turni227 – 2304

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66Cytoplasmic
    Topological domaini34 – 190157PeriplasmicAdd
    BLAST
    Topological domaini212 – 553342CytoplasmicAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 3327HelicalSequence AnalysisAdd
    BLAST
    Transmembranei191 – 21121HelicalSequence AnalysisAdd
    BLAST

    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.
    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

    MINRIRVVTL LVMVLGVFAL LQLISGSLFF SSLHHSQKSF VVSNQLREQQ    50
    GELTSTWDLM LQTRINLSRS AVRMMMDSSN QQSNAKVELL DSARKTLAQA 100
    ATHYKKFKSM APLPEMVATS RNIDEKYKNY YTALTELIDY LDYGNTGAYF 150
    AQPTQGMQNA MGEAFAQYAL SSEKLYRDIV TDNADDYRFA QWQLAVIALV 200
    VVLILLVAWY GIRRMLLTPL AKIIAHIREI AGGNLANTLT IDGRSEMGDL 250
    AQSVSHMQRS LTDTVTHVRE GSDAIYAGTR EIAAGNTDLS SRTEQQASAL 300
    EETAASMEQL TATVKQNADN ARQASQLAQS ASDTAQHGGK VVDGVVKTMH 350
    EIADSSKKIA DIISVIDGIA FQTNILALNA AVEAARAGEQ GRGFAVVAGE 400
    VRNLASRSAQ AAKEIKALIE DSVSRVDTGS VLVESAGETM NNIVNAVTRV 450
    TDIMGEIASA SDEQSRGIDQ VALAVSEMDR VTQQNASLVQ ESAAAAAALE 500
    EQASRLTQAV SAFRLAASPL TNKPQTPSRP ASEQPPAQPR LRIAEQDPNW 550
    ETF 553
    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:
    EMBL
    GenBank
    DDBJ
    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.
    YP_490148.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74956; AAC74956; b1886.
    BAA15702; BAA15702; BAA15702.
    GeneIDi12931387.
    946399.
    KEGGiecj:Y75_p1862.
    eco:b1886.
    PATRICi32119099. VBIEscCol129921_1967.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01705 Genomic DNA. Translation: AAA23566.1 .
    U00096 Genomic DNA. Translation: AAC74956.1 .
    AP009048 Genomic DNA. Translation: BAA15702.1 .
    PIRi F64951. QRECM4.
    RefSeqi NP_416400.1. NC_000913.3.
    YP_490148.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ASR X-ray 2.30 A 38-179 [» ]
    2L9G NMR - A 214-232 [» ]
    DisProti DP00294.
    ProteinModelPortali P07017.
    SMRi P07017. Positions 38-179, 219-515.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10956N.
    IntActi P07017. 7 interactions.
    STRINGi 511145.b1886.

    Proteomic databases

    PaxDbi P07017.
    PRIDEi P07017.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74956 ; AAC74956 ; b1886 .
    BAA15702 ; BAA15702 ; BAA15702 .
    GeneIDi 12931387.
    946399.
    KEGGi ecj:Y75_p1862.
    eco:b1886.
    PATRICi 32119099. VBIEscCol129921_1967.

    Organism-specific databases

    EchoBASEi EB0981.
    EcoGenei EG10988. tar.

    Phylogenomic databases

    eggNOGi COG0840.
    HOGENOMi HOG000148074.
    KOi K05875.
    OMAi GDDANWE.
    OrthoDBi EOG6G4VQG.
    PhylomeDBi P07017.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTracei P07017.
    PROi P07017.

    Gene expression databases

    Genevestigatori P07017.

    Family and domain databases

    Gene3Di 1.20.120.30. 1 hit.
    InterProi 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 ]
    Pfami PF00672. HAMP. 1 hit.
    PF00015. MCPsignal. 1 hit.
    PF02203. TarH. 1 hit.
    [Graphical view ]
    PRINTSi PR00260. CHEMTRNSDUCR.
    SMARTi SM00304. HAMP. 1 hit.
    SM00283. MA. 1 hit.
    SM00319. TarH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47170. SSF47170. 1 hit.
    PROSITEi PS00538. CHEMOTAXIS_TRANSDUC_1. 1 hit.
    PS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
    PS50885. HAMP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 147 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