Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methyl-accepting chemotaxis protein McpB

Gene

mcpB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: 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

GO - Biological processi

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
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 16CytoplasmicSequence analysisAdd BLAST16
Transmembranei17 – 37HelicalSequence analysisAdd BLAST21
Topological domaini38 – 282ExtracellularSequence analysisAdd BLAST245
Transmembranei283 – 303HelicalSequence analysisAdd BLAST21
Topological domaini304 – 662CytoplasmicSequence analysisAdd BLAST359

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi371Q → 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 Publication1
Mutagenesisi595Q → D: Wild-type production of methanol. 1 Publication1
Mutagenesisi630E → 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 Publication1
Mutagenesisi637E → 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 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001105571 – 662Methyl-accepting chemotaxis protein McpBAdd BLAST662

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei371Glutamate methyl ester (Gln)2 Publications1
Modified residuei595Glutamate methyl ester (Gln)1 Publication1
Modified residuei630Glutamate methyl ester (Glu)2 Publications1
Modified residuei637Glutamate methyl ester (Glu)2 Publications1

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 interactors.
STRINGi224308.Bsubs1_010100016991.

Structurei

3D structure databases

ProteinModelPortaliP39215.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini153 – 229CacheAdd BLAST77
Domaini304 – 356HAMPPROSITE-ProRule annotationAdd BLAST53
Domaini375 – 611Methyl-accepting transducerPROSITE-ProRule annotationAdd BLAST237

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

eggNOGiENOG4105C8Q. Bacteria.
COG0840. LUCA.
HOGENOMiHOG000083278.
InParanoidiP39215.
KOiK03406.
OMAiYTTNELT.
PhylomeDBiP39215.

Family and domain databases

CDDicd06225. HAMP. 1 hit.
InterProiIPR003122. Chemotax_Me-accpt_rcpt_lig-bd.
IPR033479. dCache_1.
IPR003660. HAMP_dom.
IPR004089. MCPsignal_dom.
IPR029151. Sensor-like.
[Graphical view]
PfamiPF02743. dCache_1. 1 hit.
PF00672. HAMP. 1 hit.
PF00015. MCPsignal. 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)DescriptionActionsGraphical viewLength
Sequence conflicti360D → N in AAA20554 (PubMed:8188684).Curated1
Sequence conflicti402E → R in AAA20554 (PubMed:8188684).Curated1
Sequence conflicti450V → G in AAA20554 (PubMed:8188684).Curated1

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.
WP_003243461.1. NZ_JNCM01000033.1.

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.
PIRiA54078.
RefSeqiNP_391004.2. NC_000964.3.
WP_003243461.1. NZ_JNCM01000033.1.

3D structure databases

ProteinModelPortaliP39215.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP39215. 2 interactors.
STRINGi224308.Bsubs1_010100016991.

Proteomic databases

PaxDbiP39215.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105C8Q. Bacteria.
COG0840. LUCA.
HOGENOMiHOG000083278.
InParanoidiP39215.
KOiK03406.
OMAiYTTNELT.
PhylomeDBiP39215.

Enzyme and pathway databases

BioCyciBSUB:BSU31260-MONOMER.

Family and domain databases

CDDicd06225. HAMP. 1 hit.
InterProiIPR003122. Chemotax_Me-accpt_rcpt_lig-bd.
IPR033479. dCache_1.
IPR003660. HAMP_dom.
IPR004089. MCPsignal_dom.
IPR029151. Sensor-like.
[Graphical view]
PfamiPF02743. dCache_1. 1 hit.
PF00672. HAMP. 1 hit.
PF00015. MCPsignal. 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]
ProtoNetiSearch...

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 5, 2016
This is version 119 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.