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P39215 (MCPB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methyl-accepting chemotaxis protein McpB
Alternative name(s):
H3
Gene names
Name:mcpB
Ordered Locus Names:BSU31260
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length662 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subcellular location

Cell membrane; Multi-pass membrane protein.

Post-translational modification

Some glutamine residues are deamidated to glutamate by CheD and subsequently methylated. Ref.1 Ref.4

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. Ref.1 Ref.4

Miscellaneous

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

Sequence similarities

Contains 1 cache domain.

Contains 1 HAMP domain.

Contains 1 methyl-accepting transducer domain.

Ontologies

Keywords
   Biological processChemotaxis
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionTransducer
   PTMMethylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchemotaxis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiontransmembrane signaling receptor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 662662Methyl-accepting chemotaxis protein McpB
PRO_0000110557

Regions

Topological domain1 – 1616Cytoplasmic Potential
Transmembrane17 – 3721Helical; Potential
Topological domain38 – 282245Extracellular Potential
Transmembrane283 – 30321Helical; Potential
Topological domain304 – 662359Cytoplasmic Potential
Domain153 – 22977Cache
Domain304 – 35653HAMP
Domain375 – 611237Methyl-accepting transducer

Amino acid modifications

Modified residue3711Glutamate methyl ester (Gln) Ref.1 Ref.4
Modified residue5951Glutamate methyl ester (Gln) Probable
Modified residue6301Glutamate methyl ester (Glu) Ref.1 Ref.4
Modified residue6371Glutamate methyl ester (Glu) Ref.1 Ref.4

Experimental info

Mutagenesis3711Q → 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. Ref.4
Mutagenesis5951Q → D: Wild-type production of methanol. Ref.4
Mutagenesis6301E → 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. Ref.4
Mutagenesis6371E → 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. Ref.4
Sequence conflict3601D → N in AAA20554. Ref.1
Sequence conflict4021E → R in AAA20554. Ref.1
Sequence conflict4501V → G in AAA20554. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P39215 [UniParc].

Last modified July 7, 2009. Version 2.
Checksum: 2E4ED0EFC31F2983

FASTA66271,901
        10         20         30         40         50         60 
MKTFINWLKK PSISKKLIVS FIAILIIPIL ILEFSSYRSA SGKLDQEIMG NAKNSVDTFN 

        70         80         90        100        110        120 
TTVTNDLGEK AKAVTFFSES LKRSAFKGKS NQEEIKAKFS QYVSINQGVA RIYGGADNGT 

       130        140        150        160        170        180 
YVQAPKEKLP EGYDPRQRPW YQDAMKAGGE IVVTDPYVAA SDGSMVITIA QELKDGSGVV 

       190        200        210        220        230        240 
AMDITIDKLL EQMKQIKVGK EGYAFIATKN KTYVAHKNHK AGEKLSGDWV AKMYANDSGE 

       250        260        270        280        290        300 
LQYTLNNEDK KMTYTTNELT GWKIAGTMYM DEIKDASKSV LTTGMIVLIA SIVAGGILIL 

       310        320        330        340        350        360 
FIVRSITKPL KRLVQSSKTI SRGDLTETIE IHSKDELGEL GESFNEMGQS LRSLISAIQD 

       370        380        390        400        410        420 
SVNNVAASSE QLTASAGQTS KATEHITMAI EQFSNGNEEQ SEKVESSSHQ LNLMNEGLQQ 

       430        440        450        460        470        480 
VSQTSSDITK ASIQSTEIAG TGEKFVQQTV GQMNSINQSV QQAEAVVKGL EGKSKDITSI 

       490        500        510        520        530        540 
LRVINGIADQ TNLLALNAAI EAARAGESGR GFSVVAEEVR KLAVQSADSA KEIEKLIQEI 

       550        560        570        580        590        600 
VAEIDTSLHM FKEVNQEVQS GLVVTDNTKE SFQSIFSMTN EIAGKLQTMN STVEQLSDRS 

       610        620        630        640        650        660 
QHVSAAVSGI ADVSKESSAS IQDIAASAEE QLASMEEISS SATTLAQMAE ELRDLTKQFK 


IE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L29189 Genomic DNA. Translation: AAA20554.1.
AL009126 Genomic DNA. Translation: CAB15104.2.
PIRA54078.
RefSeqNP_391004.2. NC_000964.3.

3D structure databases

ProteinModelPortalP39215.
SMRP39215. Positions 304-356, 360-660.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP39215. 2 interactions.
STRING224308.BSU31260.

Proteomic databases

PaxDbP39215.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15104; CAB15104; BSU31260.
GeneID937155.
KEGGbsu:BSU31260.
PATRIC18978210. VBIBacSub10457_3268.

Organism-specific databases

GenoListBSU31260. [Micado]

Phylogenomic databases

eggNOGCOG0840.
HOGENOMHOG000083278.
KOK03406.
OrthoDBEOG67X1NZ.
ProtClustDBCLSK2301479.

Enzyme and pathway databases

BioCycBSUB:BSU31260-MONOMER.

Family and domain databases

InterProIPR004010. Cache_domain.
IPR003122. Chemotax_Me-accpt_rcpt_lig-bd.
IPR003660. HAMP_linker_domain.
IPR004089. MCPsignal_dom.
[Graphical view]
PfamPF02743. Cache_1. 1 hit.
PF00672. HAMP. 1 hit.
PF00015. MCPsignal. 1 hit.
PF02203. TarH. 1 hit.
[Graphical view]
SMARTSM00304. HAMP. 1 hit.
SM00283. MA. 1 hit.
SM00319. TarH. 1 hit.
[Graphical view]
PROSITEPS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
PS50885. HAMP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMCPB_BACSU
AccessionPrimary (citable) accession number: P39215
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 7, 2009
Last modified: April 16, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList