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P39215

- MCPB_BACSU

UniProt

P39215 - MCPB_BACSU

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Protein
Methyl-accepting chemotaxis protein McpB
Gene
mcpB, BSU31260
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

GO - Biological processi

  1. chemotaxis Source: UniProtKB-KW
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei17 – 3721Helical; Reviewed prediction
Add
BLAST
Topological domaini38 – 282245Extracellular Reviewed prediction
Add
BLAST
Transmembranei283 – 30321Helical; Reviewed prediction
Add
BLAST
Topological domaini304 – 662359Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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 McpB
PRO_0000110557Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei371 – 3711Glutamate methyl ester (Gln)2 Publications
Modified residuei595 – 5951Glutamate methyl ester (Gln) Inferred
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.2 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.2 Publications

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini153 – 22977Cache
Add
BLAST
Domaini304 – 35653HAMP
Add
BLAST
Domaini375 – 611237Methyl-accepting transducer
Add
BLAST

Sequence similaritiesi

Contains 1 cache domain.
Contains 1 HAMP domain.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti360 – 3601D → N in AAA20554. 1 Publication
Sequence conflicti402 – 4021E → R in AAA20554. 1 Publication
Sequence conflicti450 – 4501V → G in AAA20554. 1 Publication

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...

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 104 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

Similar proteinsi