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P39214

- MCPA_BACSU

UniProt

P39214 - MCPA_BACSU

Protein

Methyl-accepting chemotaxis protein McpA

Gene

mcpA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (07 Jul 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. McpA is required for taxis towards glucose and alpha-methylglucoside.1 Publication

    GO - Molecular functioni

    1. transmembrane signaling receptor activity Source: InterPro

    GO - Biological processi

    1. chemotaxis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Transducer

    Keywords - Biological processi

    Chemotaxis

    Enzyme and pathway databases

    BioCyciBSUB:BSU31240-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methyl-accepting chemotaxis protein McpA
    Alternative name(s):
    H1
    Gene namesi
    Name:mcpA
    Ordered Locus Names:BSU31240
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU31240. [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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi593 – 5931Q → A: No CheD modification at Q-593 and Q-594 but modification possible at the unidentified second site; when associated with A-594. 1 Publication
    Mutagenesisi594 – 5941Q → A: No CheD modification at Q-593 and Q-594 but modification possible at the unidentified second site; when associated with A-593. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 661661Methyl-accepting chemotaxis protein McpAPRO_0000110556Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei370 – 3701Glutamate methyl ester (Glu)1 Publication
    Modified residuei593 – 5931Deamidated glutamine1 Publication
    Modified residuei593 – 5931Glutamate methyl ester (Gln)1 Publication
    Modified residuei594 – 5941Deamidated glutamine1 Publication
    Modified residuei594 – 5941Glutamate methyl ester (Gln)2 Publications
    Modified residuei629 – 6291Glutamate methyl ester (Glu)1 Publication
    Modified residuei636 – 6361Glutamate methyl ester (Glu)1 Publication

    Post-translational modificationi

    Deamidated by CheD on Gln-593 and Gln-594, producing glutamate residues. The glutamate residues are then methylated. Other additional sites are deamidated and methylated as well.2 Publications

    Keywords - PTMi

    Methylation

    Proteomic databases

    PaxDbiP39214.

    Interactioni

    Protein-protein interaction databases

    IntActiP39214. 23 interactions.
    STRINGi224308.BSU31240.

    Structurei

    3D structure databases

    ProteinModelPortaliP39214.
    SMRiP39214. Positions 303-355, 364-659.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini38 – 281244ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini303 – 661359CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei17 – 3721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei282 – 30221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini152 – 22877CacheAdd
    BLAST
    Domaini303 – 35553HAMPPROSITE-ProRule annotationAdd
    BLAST
    Domaini374 – 610237Methyl-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.
    HOGENOMiHOG000083278.
    KOiK03406.
    OrthoDBiEOG67HJTT.
    PhylomeDBiP39214.

    Family and domain databases

    InterProiIPR004010. Cache_domain.
    IPR003122. Chemotax_Me-accpt_rcpt_lig-bd.
    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.
    PF02203. TarH. 1 hit.
    [Graphical view]
    SMARTiSM00304. HAMP. 1 hit.
    SM00283. MA. 1 hit.
    SM00319. TarH. 1 hit.
    [Graphical view]
    SUPFAMiSSF103190. SSF103190. 1 hit.
    PROSITEiPS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
    PS50885. HAMP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P39214-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKILQLIKQ RSITRKLLVS FLSILIIPVV ILAIFAYQSA SSSLDRQMMG    50
    SALENVQQLN EIINTSIGEK ENSADYFSEW LTKEKYNAKS NASIAEKFSQ 100
    YISINKDVES IYTSDTKGHF TRYPDLPMPS GYNPVERDWY KKAVANKGKV 150
    VITDPYKTAS TNTMVVTIAQ QTKDGSGVIA INMTIENLLK TTKKVNIGTQ 200
    GYAFIMTKDK KVVAHPNEQS GTELKGDWLD KMLSADKGDF QYTMDGDKKK 250
    MAFDTNKLTG WKIGGTMYLD EIHEAAQPVL HLALIVLAAA IIIGIIVMTL 300
    IIRSITTPLK QLVGSSKRIS EGDLTETIDI RSKDELGELG KSFNNMASSL 350
    RSLIHAIQDS VDNVAASSEE LTASAAQTSK ATEHITLAIE QFSNGNEKQN 400
    ENIETAAEHI YQMNDGLTNM AQASEVITDS SVQSTEIASE GGKLVHQTVG 450
    QMNVIDKSVK EAEQVVRGLE TKSKDITNIL RVINGIADQT NLLALNAAIE 500
    AARAGEYGRG FSVVAEEVRK LAVQSADSAK EIEGLIIEIV KEINTSLGMF 550
    QSVNQEVQTG LDITDKTEMS FKRISEMTNQ IAGELQNMSA TVQQLSASSE 600
    EVSGASEHIA SISKESSAHI QDIAASAEEQ LASMEEISSS AETLSSMAEE 650
    LRDMTKRFKI E 661
    Length:661
    Mass (Da):72,314
    Last modified:July 7, 2009 - v2
    Checksum:iE46A09AB33604141
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti95 – 951A → R in AAA20556. (PubMed:8188684)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29189 Genomic DNA. Translation: AAA20556.1.
    AL009126 Genomic DNA. Translation: CAB15102.2.
    PIRiB54078.
    RefSeqiNP_391002.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15102; CAB15102; BSU31240.
    GeneIDi937154.
    KEGGibsu:BSU31240.
    PATRICi18978206. VBIBacSub10457_3266.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29189 Genomic DNA. Translation: AAA20556.1 .
    AL009126 Genomic DNA. Translation: CAB15102.2 .
    PIRi B54078.
    RefSeqi NP_391002.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali P39214.
    SMRi P39214. Positions 303-355, 364-659.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P39214. 23 interactions.
    STRINGi 224308.BSU31240.

    Proteomic databases

    PaxDbi P39214.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15102 ; CAB15102 ; BSU31240 .
    GeneIDi 937154.
    KEGGi bsu:BSU31240.
    PATRICi 18978206. VBIBacSub10457_3266.

    Organism-specific databases

    GenoListi BSU31240. [Micado ]

    Phylogenomic databases

    eggNOGi COG0840.
    HOGENOMi HOG000083278.
    KOi K03406.
    OrthoDBi EOG67HJTT.
    PhylomeDBi P39214.

    Enzyme and pathway databases

    BioCyci BSUB:BSU31240-MONOMER.

    Family and domain databases

    InterProi IPR004010. Cache_domain.
    IPR003122. Chemotax_Me-accpt_rcpt_lig-bd.
    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.
    PF02203. TarH. 1 hit.
    [Graphical view ]
    SMARTi SM00304. HAMP. 1 hit.
    SM00283. MA. 1 hit.
    SM00319. TarH. 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. "Cloning and characterization of genes encoding methyl-accepting chemotaxis proteins in Bacillus subtilis."
      Hanlon D.W., Ordal G.W.
      J. Biol. Chem. 269:14038-14046(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], METHYLATION AT GLU-370; GLN-594; GLU-629 AND GLU-636, FUNCTION.
      Strain: 168 / OI1085.
    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 TO 95.
    4. "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: PROTEIN SEQUENCE OF 589-595, DEAMIDATION AT GLN-593 AND GLN-594 BY CHED, MUTAGENESIS OF GLN-593 AND GLN-594.

    Entry informationi

    Entry nameiMCPA_BACSU
    AccessioniPrimary (citable) accession number: P39214
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 105 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, Direct protein sequencing, 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