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P54576

- MCPC_BACSU

UniProt

P54576 - MCPC_BACSU

Protein

Methyl-accepting chemotaxis protein McpC

Gene

mcpC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    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. All amino acids serve as attractants in B.subtilis, they appear to cause an increase in the turnover methyl groups, leading to methylation of an unidentified acceptor, while repellents have been shown to cause a decrease in methyl group turnover. The methyl groups are added by a methyltransferase and removed by a methylesterase. McpC is required for taxis to cysteine, proline, threonine, glycine, serine, lysine, valine and arginine and for aspartate, glutamine, histidine and glutamate. Primarily mediates response to positive stimulus of PTS carbohydrates. Greatly influences the duration or magnitude of the response to negative PTS carbohydrate stimulus.2 Publications

    GO - Molecular functioni

    1. signal transducer activity Source: UniProtKB-KW

    GO - Biological processi

    1. chemotaxis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Transducer

    Keywords - Biological processi

    Chemotaxis

    Enzyme and pathway databases

    BioCyciBSUB:BSU13950-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methyl-accepting chemotaxis protein McpC
    Gene namesi
    Name:mcpC
    Synonyms:prg71
    Ordered Locus Names:BSU13950
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU13950. [Micado]

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 655655Methyl-accepting chemotaxis protein McpCPRO_0000110558Add
    BLAST

    Post-translational modificationi

    Some glutamine residues are deamidated to glutamate by CheD and subsequently methylated.2 Publications

    Keywords - PTMi

    Methylation

    Proteomic databases

    PaxDbiP54576.

    Expressioni

    Inductioni

    Induced by SigD. Expression increases in the late-exponential growth-phase and is maximal during the early-stationary phase.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU13950.

    Structurei

    3D structure databases

    ProteinModelPortaliP54576.
    SMRiP54576. Positions 298-350, 357-654.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 88CytoplasmicSequence Analysis
    Topological domaini30 – 276247ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini298 – 655358CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei9 – 2921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei277 – 29721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini148 – 22578CacheAdd
    BLAST
    Domaini298 – 35053HAMPPROSITE-ProRule annotationAdd
    BLAST
    Domaini369 – 619251Methyl-accepting transducerPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 cache domain.Curated
    Contains 1 HAMP domain.PROSITE-ProRule annotation
    Contains 1 methyl-accepting transducer domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0840.
    HOGENOMiHOG000261838.
    KOiK03406.
    OrthoDBiEOG67HJTT.
    PhylomeDBiP54576.

    Family and domain databases

    InterProiIPR004010. Cache_domain.
    IPR003660. HAMP_linker_domain.
    IPR004089. MCPsignal_dom.
    IPR029151. Sensor-like.
    [Graphical view]
    PfamiPF02743. Cache_1. 1 hit.
    PF00672. HAMP. 1 hit.
    PF00015. MCPsignal. 1 hit.
    [Graphical view]
    SMARTiSM00304. HAMP. 1 hit.
    SM00283. MA. 1 hit.
    [Graphical view]
    SUPFAMiSSF103190. SSF103190. 1 hit.
    PROSITEiPS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
    PS50885. HAMP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P54576-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFKKLHMKIA VFVSIMLIIT VVLLMLSSYL TLKPMITEDG KNTTQNVTQS    50
    LEQNIELQLK SYAISLSRLA NGELTHTFVT KPSKEASRLF HDDIKQIKDN 100
    DDYVAMAYIG TAKKEMFTYP KADFAEDYDP TSRPWYKLAA ETPDQVVWTE 150
    PYKDVVTGDM IVTASKAILD RQKVIGVASY DLKLSAIQSM VNKQKVPYKG 200
    FAFLADASGN LLAHPSNQGK NISKDQTLQT IASEKKGIQD VNGKMVVYQT 250
    IGETGWKVGT QFDTDQLMWI SDKMNRANLW ISLIALIITI ILSYFLAKTI 300
    TGPIQQLIVK TKAVSAGDLT VRAESKSKDE VGILTRDFNL MVENMKEMVE 350
    QVRLSSGKVS DTSEQLTAVA AETNETSGQI AKAIEEVAAG ASEQASEVET 400
    INEKSESLST KIRQIAEEAG GIKERSKSSE DASYKGLDAL GQLLMKSNEA 450
    NMETKKVETM LLDLENQTKN IEEVVTAISN ISDQTNLLAL NASIEAARAG 500
    ESGRGFAVVA DEVRKLAEQS ALSTKHISET VKLIQLETKE ASHAMVEASR 550
    MNDEQNSAIH ETGEVLNTIT AEMQSLVQGI DHIYAEIQRM SEEQLAISEA 600
    IQSISAISQE SAAAAEEVNA STDEQLVTLD KVKHSTETLK HASQELMNTI 650
    AKFTL 655
    Length:655
    Mass (Da):72,031
    Last modified:June 16, 2009 - v2
    Checksum:iCD5485BD8D8D693A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti95 – 962KQ → NE in CAA66052. (PubMed:9353924)Curated
    Sequence conflicti115 – 1206EMFTYP → RNVYIS in CAA66052. (PubMed:9353924)Curated
    Sequence conflicti125 – 13511AEDYDPTSRPW → LRITIQHQDM in CAA66052. (PubMed:9353924)CuratedAdd
    BLAST
    Sequence conflicti190 – 1901M → L in CAA66052. (PubMed:9353924)Curated
    Sequence conflicti376 – 3761T → R in CAA66052. (PubMed:9353924)Curated
    Sequence conflicti438 – 4381D → H in CAA66052. (PubMed:9353924)Curated
    Sequence conflicti457 – 4571V → E in CAA66052. (PubMed:9353924)Curated
    Sequence conflicti492 – 4921A → R in CAA66052. (PubMed:9353924)Curated
    Sequence conflicti645 – 6473ELM → DVI in CAA66052. (PubMed:9353924)Curated
    Sequence conflicti651 – 6511A → R in CAA66052. (PubMed:9353924)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97385 Genomic DNA. Translation: CAA66052.1.
    AL009126 Genomic DNA. Translation: CAB13268.2.
    PIRiA69656.
    RefSeqiNP_389278.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13268; CAB13268; BSU13950.
    GeneIDi936206.
    KEGGibsu:BSU13950.
    PATRICi18974573. VBIBacSub10457_1478.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97385 Genomic DNA. Translation: CAA66052.1 .
    AL009126 Genomic DNA. Translation: CAB13268.2 .
    PIRi A69656.
    RefSeqi NP_389278.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali P54576.
    SMRi P54576. Positions 298-350, 357-654.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU13950.

    Proteomic databases

    PaxDbi P54576.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13268 ; CAB13268 ; BSU13950 .
    GeneIDi 936206.
    KEGGi bsu:BSU13950.
    PATRICi 18974573. VBIBacSub10457_1478.

    Organism-specific databases

    GenoListi BSU13950. [Micado ]

    Phylogenomic databases

    eggNOGi COG0840.
    HOGENOMi HOG000261838.
    KOi K03406.
    OrthoDBi EOG67HJTT.
    PhylomeDBi P54576.

    Enzyme and pathway databases

    BioCyci BSUB:BSU13950-MONOMER.

    Family and domain databases

    InterProi IPR004010. Cache_domain.
    IPR003660. HAMP_linker_domain.
    IPR004089. MCPsignal_dom.
    IPR029151. Sensor-like.
    [Graphical view ]
    Pfami PF02743. Cache_1. 1 hit.
    PF00672. HAMP. 1 hit.
    PF00015. MCPsignal. 1 hit.
    [Graphical view ]
    SMARTi SM00304. HAMP. 1 hit.
    SM00283. MA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103190. SSF103190. 1 hit.
    PROSITEi PS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
    PS50885. HAMP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Functional and genetic characterization of mcpC, which encodes a third methyl-accepting chemotaxis protein in Bacillus subtilis."
      Mueller J., Schiel S., Ordal G.W., Saxild H.H.
      Microbiology 143:3231-3240(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, METHYLATION, EXPRESSION, INDUCTION.
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. "Unique regulation of carbohydrate chemotaxis in Bacillus subtilis by the phosphoenolpyruvate-dependent phosphotransferase system and the methyl-accepting chemotaxis protein McpC."
      Garrity L.F., Schiel S.L., Merrill R., Reizer J., Saier M.H. Jr., Ordal G.W.
      J. Bacteriol. 180:4475-4480(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RESPONSE TO PTS SUBSTRATES.
    5. "Bacillus subtilis CheD is a chemoreceptor modification enzyme required for chemotaxis."
      Kristich C.J., Ordal G.W.
      J. Biol. Chem. 277:25356-25362(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEAMIDATION BY CHED.

    Entry informationi

    Entry nameiMCPC_BACSU
    AccessioniPrimary (citable) accession number: P54576
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 98 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

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3