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 McpC

Gene

mcpC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 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. McpC is required for taxis to cysteine, proline, threonine, glycine, serine, lysine, valine and arginine and for aspartate, glutamine, histidine and glutamate. Primarily mediates response to positive stimulus of PTS carbohydrates. Greatly influences the duration or magnitude of the response to negative PTS carbohydrate stimulus.2 Publications

GO - Molecular functioni

  1. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

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

Keywords - Molecular functioni

Transducer

Keywords - Biological processi

Chemotaxis

Enzyme and pathway databases

BioCyciBSUB:BSU13950-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-accepting chemotaxis protein McpC
Gene namesi
Name:mcpC
Synonyms:prg71
Ordered Locus Names:BSU13950
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU13950. [Micado]

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence Analysis
Transmembranei9 – 2921HelicalSequence AnalysisAdd
BLAST
Topological domaini30 – 276247ExtracellularSequence AnalysisAdd
BLAST
Transmembranei277 – 29721HelicalSequence AnalysisAdd
BLAST
Topological domaini298 – 655358CytoplasmicSequence AnalysisAdd
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 655655Methyl-accepting chemotaxis protein McpCPRO_0000110558Add
BLAST

Post-translational modificationi

Some glutamine residues are deamidated to glutamate by CheD and subsequently methylated.2 Publications

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP54576.

Expressioni

Inductioni

Induced by SigD. Expression increases in the late-exponential growth-phase and is maximal during the early-stationary phase.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU13950.

Structurei

3D structure databases

ProteinModelPortaliP54576.
SMRiP54576. Positions 298-350, 357-654.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini148 – 22578CacheAdd
BLAST
Domaini298 – 35053HAMPPROSITE-ProRule annotationAdd
BLAST
Domaini369 – 619251Methyl-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.
HOGENOMiHOG000261838.
InParanoidiP54576.
KOiK03406.
OMAiWSIGFAV.
OrthoDBiEOG67HJTT.
PhylomeDBiP54576.

Family and domain databases

InterProiIPR004010. Cache_domain.
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.
[Graphical view]
SMARTiSM00304. HAMP. 1 hit.
SM00283. MA. 1 hit.
[Graphical view]
SUPFAMiSSF103190. SSF103190. 1 hit.
PROSITEiPS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
PS50885. HAMP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P54576-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKKLHMKIA VFVSIMLIIT VVLLMLSSYL TLKPMITEDG KNTTQNVTQS
60 70 80 90 100
LEQNIELQLK SYAISLSRLA NGELTHTFVT KPSKEASRLF HDDIKQIKDN
110 120 130 140 150
DDYVAMAYIG TAKKEMFTYP KADFAEDYDP TSRPWYKLAA ETPDQVVWTE
160 170 180 190 200
PYKDVVTGDM IVTASKAILD RQKVIGVASY DLKLSAIQSM VNKQKVPYKG
210 220 230 240 250
FAFLADASGN LLAHPSNQGK NISKDQTLQT IASEKKGIQD VNGKMVVYQT
260 270 280 290 300
IGETGWKVGT QFDTDQLMWI SDKMNRANLW ISLIALIITI ILSYFLAKTI
310 320 330 340 350
TGPIQQLIVK TKAVSAGDLT VRAESKSKDE VGILTRDFNL MVENMKEMVE
360 370 380 390 400
QVRLSSGKVS DTSEQLTAVA AETNETSGQI AKAIEEVAAG ASEQASEVET
410 420 430 440 450
INEKSESLST KIRQIAEEAG GIKERSKSSE DASYKGLDAL GQLLMKSNEA
460 470 480 490 500
NMETKKVETM LLDLENQTKN IEEVVTAISN ISDQTNLLAL NASIEAARAG
510 520 530 540 550
ESGRGFAVVA DEVRKLAEQS ALSTKHISET VKLIQLETKE ASHAMVEASR
560 570 580 590 600
MNDEQNSAIH ETGEVLNTIT AEMQSLVQGI DHIYAEIQRM SEEQLAISEA
610 620 630 640 650
IQSISAISQE SAAAAEEVNA STDEQLVTLD KVKHSTETLK HASQELMNTI

AKFTL
Length:655
Mass (Da):72,031
Last modified:June 16, 2009 - v2
Checksum:iCD5485BD8D8D693A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 962KQ → NE in CAA66052 (PubMed:9353924).Curated
Sequence conflicti115 – 1206EMFTYP → RNVYIS in CAA66052 (PubMed:9353924).Curated
Sequence conflicti125 – 13511AEDYDPTSRPW → LRITIQHQDM in CAA66052 (PubMed:9353924).CuratedAdd
BLAST
Sequence conflicti190 – 1901M → L in CAA66052 (PubMed:9353924).Curated
Sequence conflicti376 – 3761T → R in CAA66052 (PubMed:9353924).Curated
Sequence conflicti438 – 4381D → H in CAA66052 (PubMed:9353924).Curated
Sequence conflicti457 – 4571V → E in CAA66052 (PubMed:9353924).Curated
Sequence conflicti492 – 4921A → R in CAA66052 (PubMed:9353924).Curated
Sequence conflicti645 – 6473ELM → DVI in CAA66052 (PubMed:9353924).Curated
Sequence conflicti651 – 6511A → R in CAA66052 (PubMed:9353924).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97385 Genomic DNA. Translation: CAA66052.1.
AL009126 Genomic DNA. Translation: CAB13268.2.
PIRiA69656.
RefSeqiNP_389278.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13268; CAB13268; BSU13950.
GeneIDi936206.
KEGGibsu:BSU13950.
PATRICi18974573. VBIBacSub10457_1478.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97385 Genomic DNA. Translation: CAA66052.1.
AL009126 Genomic DNA. Translation: CAB13268.2.
PIRiA69656.
RefSeqiNP_389278.2. NC_000964.3.

3D structure databases

ProteinModelPortaliP54576.
SMRiP54576. Positions 298-350, 357-654.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU13950.

Proteomic databases

PaxDbiP54576.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13268; CAB13268; BSU13950.
GeneIDi936206.
KEGGibsu:BSU13950.
PATRICi18974573. VBIBacSub10457_1478.

Organism-specific databases

GenoListiBSU13950. [Micado]

Phylogenomic databases

eggNOGiCOG0840.
HOGENOMiHOG000261838.
InParanoidiP54576.
KOiK03406.
OMAiWSIGFAV.
OrthoDBiEOG67HJTT.
PhylomeDBiP54576.

Enzyme and pathway databases

BioCyciBSUB:BSU13950-MONOMER.

Family and domain databases

InterProiIPR004010. Cache_domain.
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.
[Graphical view]
SMARTiSM00304. HAMP. 1 hit.
SM00283. MA. 1 hit.
[Graphical view]
SUPFAMiSSF103190. SSF103190. 1 hit.
PROSITEiPS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
PS50885. HAMP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Functional and genetic characterization of mcpC, which encodes a third methyl-accepting chemotaxis protein in Bacillus subtilis."
    Mueller J., Schiel S., Ordal G.W., Saxild H.H.
    Microbiology 143:3231-3240(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, METHYLATION, EXPRESSION, INDUCTION.
    Strain: 168.
  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(1996) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "Unique regulation of carbohydrate chemotaxis in Bacillus subtilis by the phosphoenolpyruvate-dependent phosphotransferase system and the methyl-accepting chemotaxis protein McpC."
    Garrity L.F., Schiel S.L., Merrill R., Reizer J., Saier M.H. Jr., Ordal G.W.
    J. Bacteriol. 180:4475-4480(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RESPONSE TO PTS SUBSTRATES.
  5. "Bacillus subtilis CheD is a chemoreceptor modification enzyme required for chemotaxis."
    Kristich C.J., Ordal G.W.
    J. Biol. Chem. 277:25356-25362(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEAMIDATION BY CHED.

Entry informationi

Entry nameiMCPC_BACSU
AccessioniPrimary (citable) accession number: P54576
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 16, 2009
Last modified: January 7, 2015
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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 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.