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P39215

- MCPB_BACSU

UniProt

P39215 - MCPB_BACSU

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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

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
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 – 1616CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei17 – 3721HelicalSequence AnalysisAdd
BLAST
Topological domaini38 – 282245ExtracellularSequence AnalysisAdd
BLAST
Transmembranei283 – 30321HelicalSequence AnalysisAdd
BLAST
Topological domaini304 – 662359CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
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 McpBPRO_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)1 Publication
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...

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.
InParanoidiP39215.
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

        10         20         30         40         50
MKTFINWLKK PSISKKLIVS FIAILIIPIL ILEFSSYRSA SGKLDQEIMG
60 70 80 90 100
NAKNSVDTFN TTVTNDLGEK AKAVTFFSES LKRSAFKGKS NQEEIKAKFS
110 120 130 140 150
QYVSINQGVA RIYGGADNGT YVQAPKEKLP EGYDPRQRPW YQDAMKAGGE
160 170 180 190 200
IVVTDPYVAA SDGSMVITIA QELKDGSGVV AMDITIDKLL EQMKQIKVGK
210 220 230 240 250
EGYAFIATKN KTYVAHKNHK AGEKLSGDWV AKMYANDSGE LQYTLNNEDK
260 270 280 290 300
KMTYTTNELT GWKIAGTMYM DEIKDASKSV LTTGMIVLIA SIVAGGILIL
310 320 330 340 350
FIVRSITKPL KRLVQSSKTI SRGDLTETIE IHSKDELGEL GESFNEMGQS
360 370 380 390 400
LRSLISAIQD SVNNVAASSE QLTASAGQTS KATEHITMAI EQFSNGNEEQ
410 420 430 440 450
SEKVESSSHQ LNLMNEGLQQ VSQTSSDITK ASIQSTEIAG TGEKFVQQTV
460 470 480 490 500
GQMNSINQSV QQAEAVVKGL EGKSKDITSI LRVINGIADQ TNLLALNAAI
510 520 530 540 550
EAARAGESGR GFSVVAEEVR KLAVQSADSA KEIEKLIQEI VAEIDTSLHM
560 570 580 590 600
FKEVNQEVQS GLVVTDNTKE SFQSIFSMTN EIAGKLQTMN STVEQLSDRS
610 620 630 640 650
QHVSAAVSGI ADVSKESSAS IQDIAASAEE QLASMEEISS SATTLAQMAE
660
ELRDLTKQFK IE
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi P39215.
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, DEAMIDATION AT GLN-371 AND GLN-595, 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, DEAMIDATION AT GLN-371, 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 29, 2014
This is version 106 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