Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P39215

- MCPB_BACSU

UniProt

P39215 - MCPB_BACSU

Protein

Methyl-accepting chemotaxis protein McpB

Gene

mcpB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (07 Jul 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. McpB is required for taxis towards asparagine, aspartate, glutamine, and histidine.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:BSU31260-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methyl-accepting chemotaxis protein McpB
    Alternative name(s):
    H3
    Gene namesi
    Name:mcpB
    Ordered Locus Names:BSU31260
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU31260. [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
    Mutagenesisi371 – 3711Q → D: Marked diminution of methanol upon both addition and removal of asparagine. No release of methanol upon asparagine addition but methanol release upon asparagine removal is not affected; when associated with D-630. Release of methanol upon both asparagine addition and removal; when associated with D-637. No methylation; when associated with D-630 and D-637. 1 Publication
    Mutagenesisi595 – 5951Q → D: Wild-type production of methanol. 1 Publication
    Mutagenesisi630 – 6301E → D: Marked diminution of methanol upon both addition and removal of asparagine; methanol release delayed by about 1 minute compared to wild-type; adapts normally to addition of asparagine but fails to adapt to asparagine removal. No release of methanol upon asparagine addition but methanol release upon asparagine removal is not affected; when associated with D-371. Releases methanol upon asparagine addition but not upon asparagine removal; when associated with D-637. No methylation; when associated with D-371 and D-637. 1 Publication
    Mutagenesisi637 – 6371E → D: Marked diminution of methanol upon both addition and removal of asparagine; fails to adapt to addition of asparagine. Release of methanol upon both asparagine addition and removal; when associated with D-371. Releases methanol upon asparagine addition but not upon asparagine removal; when associated with D-630. No methylation; when associated with D-371 and D-630. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 662662Methyl-accepting chemotaxis protein McpBPRO_0000110557Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei371 – 3711Glutamate methyl ester (Gln)3 Publications
    Modified residuei595 – 5951Glutamate methyl ester (Gln)2 Publications
    Modified residuei630 – 6301Glutamate methyl ester (Glu)2 Publications
    Modified residuei637 – 6371Glutamate methyl ester (Glu)2 Publications

    Post-translational modificationi

    Some glutamine residues are deamidated to glutamate by CheD and subsequently methylated.3 Publications
    The demethylation is selective. Gln-371 is demethylated only upon asparagine addition whereas Glu-637 is demethylated only upon asparagine removal. Glu-630 appears indiscriminate and is demethylated upon both addition and removal of asparagine.

    Keywords - PTMi

    Methylation

    Proteomic databases

    PaxDbiP39215.

    Interactioni

    Protein-protein interaction databases

    IntActiP39215. 2 interactions.
    STRINGi224308.BSU31260.

    Structurei

    3D structure databases

    ProteinModelPortaliP39215.
    SMRiP39215. Positions 304-356, 360-660.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini38 – 282245ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini304 – 662359CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei17 – 3721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei283 – 30321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini153 – 22977CacheAdd
    BLAST
    Domaini304 – 35653HAMPPROSITE-ProRule annotationAdd
    BLAST
    Domaini375 – 611237Methyl-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.
    OrthoDBiEOG67X1NZ.
    PhylomeDBiP39215.

    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.

    P39215-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTFINWLKK PSISKKLIVS FIAILIIPIL ILEFSSYRSA SGKLDQEIMG    50
    NAKNSVDTFN TTVTNDLGEK AKAVTFFSES LKRSAFKGKS NQEEIKAKFS 100
    QYVSINQGVA RIYGGADNGT YVQAPKEKLP EGYDPRQRPW YQDAMKAGGE 150
    IVVTDPYVAA SDGSMVITIA QELKDGSGVV AMDITIDKLL EQMKQIKVGK 200
    EGYAFIATKN KTYVAHKNHK AGEKLSGDWV AKMYANDSGE LQYTLNNEDK 250
    KMTYTTNELT GWKIAGTMYM DEIKDASKSV LTTGMIVLIA SIVAGGILIL 300
    FIVRSITKPL KRLVQSSKTI SRGDLTETIE IHSKDELGEL GESFNEMGQS 350
    LRSLISAIQD SVNNVAASSE QLTASAGQTS KATEHITMAI EQFSNGNEEQ 400
    SEKVESSSHQ LNLMNEGLQQ VSQTSSDITK ASIQSTEIAG TGEKFVQQTV 450
    GQMNSINQSV QQAEAVVKGL EGKSKDITSI LRVINGIADQ TNLLALNAAI 500
    EAARAGESGR GFSVVAEEVR KLAVQSADSA KEIEKLIQEI VAEIDTSLHM 550
    FKEVNQEVQS GLVVTDNTKE SFQSIFSMTN EIAGKLQTMN STVEQLSDRS 600
    QHVSAAVSGI ADVSKESSAS IQDIAASAEE QLASMEEISS SATTLAQMAE 650
    ELRDLTKQFK IE 662
    Length:662
    Mass (Da):71,901
    Last modified:July 7, 2009 - v2
    Checksum:i2E4ED0EFC31F2983
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti360 – 3601D → N in AAA20554. (PubMed:8188684)Curated
    Sequence conflicti402 – 4021E → R in AAA20554. (PubMed:8188684)Curated
    Sequence conflicti450 – 4501V → G in AAA20554. (PubMed:8188684)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29189 Genomic DNA. Translation: AAA20554.1.
    AL009126 Genomic DNA. Translation: CAB15104.2.
    PIRiA54078.
    RefSeqiNP_391004.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15104; CAB15104; BSU31260.
    GeneIDi937155.
    KEGGibsu:BSU31260.
    PATRICi18978210. VBIBacSub10457_3268.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29189 Genomic DNA. Translation: AAA20554.1 .
    AL009126 Genomic DNA. Translation: CAB15104.2 .
    PIRi A54078.
    RefSeqi NP_391004.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali P39215.
    SMRi P39215. Positions 304-356, 360-660.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P39215. 2 interactions.
    STRINGi 224308.BSU31260.

    Proteomic databases

    PaxDbi P39215.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15104 ; CAB15104 ; BSU31260 .
    GeneIDi 937155.
    KEGGi bsu:BSU31260.
    PATRICi 18978210. VBIBacSub10457_3268.

    Organism-specific databases

    GenoListi BSU31260. [Micado ]

    Phylogenomic databases

    eggNOGi COG0840.
    HOGENOMi HOG000083278.
    KOi K03406.
    OrthoDBi EOG67X1NZ.
    PhylomeDBi P39215.

    Enzyme and pathway databases

    BioCyci BSUB:BSU31260-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 GLN-371; GLN-595; GLU-630 AND GLU-637, 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 360; 402 AND 450.
    4. "Selective methylation changes on the Bacillus subtilis chemotaxis receptor McpB promote adaptation."
      Zimmer M.A., Tiu J., Collins M.A., Ordal G.W.
      J. Biol. Chem. 275:24264-24272(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT GLN-371; GLU-630 AND GLU-637, MUTAGENESIS OF GLN-371; GLN-595; GLU-630 AND GLU-637.
    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 nameiMCPB_BACSU
    AccessioniPrimary (citable) accession number: P39215
    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

    Miscellaneous

    Only chemotaxis towards asparagine is completely deficient in the absence of McpB.

    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