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Protein

Methyl-accepting chemotaxis protein McpA

Gene

mcpA

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. McpA is required for taxis towards glucose and alpha-methylglucoside.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:BSU31240-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-accepting chemotaxis protein McpA
Alternative name(s):
H1
Gene namesi
Name:mcpA
Ordered Locus Names:BSU31240
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU31240. [Micado]

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei17 – 3721HelicalSequence AnalysisAdd
BLAST
Topological domaini38 – 281244ExtracellularSequence AnalysisAdd
BLAST
Transmembranei282 – 30221HelicalSequence AnalysisAdd
BLAST
Topological domaini303 – 661359CytoplasmicSequence 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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi593 – 5931Q → A: No CheD modification at Q-593 and Q-594 but modification possible at the unidentified second site; when associated with A-594. 1 Publication
Mutagenesisi594 – 5941Q → A: No CheD modification at Q-593 and Q-594 but modification possible at the unidentified second site; when associated with A-593. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 661661Methyl-accepting chemotaxis protein McpAPRO_0000110556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei370 – 3701Glutamate methyl ester (Glu)1 Publication
Modified residuei593 – 5931Deamidated glutamine1 Publication
Modified residuei594 – 5941Deamidated glutamine1 Publication
Modified residuei594 – 5941Glutamate methyl ester (Gln)2 Publications
Modified residuei629 – 6291Glutamate methyl ester (Glu)1 Publication
Modified residuei636 – 6361Glutamate methyl ester (Glu)1 Publication

Post-translational modificationi

Deamidated by CheD on Gln-593 and Gln-594, producing glutamate residues. The glutamate residues are then methylated. Other additional sites are deamidated and methylated as well.2 Publications

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP39214.

Interactioni

Protein-protein interaction databases

IntActiP39214. 23 interactions.
STRINGi224308.BSU31240.

Structurei

3D structure databases

ProteinModelPortaliP39214.
SMRiP39214. Positions 303-355, 364-659.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini152 – 22877CacheAdd
BLAST
Domaini303 – 35553HAMPPROSITE-ProRule annotationAdd
BLAST
Domaini374 – 610237Methyl-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.
InParanoidiP39214.
KOiK03406.
OMAiRIEDIQH.
OrthoDBiEOG67HJTT.
PhylomeDBiP39214.

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.

P39214-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKILQLIKQ RSITRKLLVS FLSILIIPVV ILAIFAYQSA SSSLDRQMMG
60 70 80 90 100
SALENVQQLN EIINTSIGEK ENSADYFSEW LTKEKYNAKS NASIAEKFSQ
110 120 130 140 150
YISINKDVES IYTSDTKGHF TRYPDLPMPS GYNPVERDWY KKAVANKGKV
160 170 180 190 200
VITDPYKTAS TNTMVVTIAQ QTKDGSGVIA INMTIENLLK TTKKVNIGTQ
210 220 230 240 250
GYAFIMTKDK KVVAHPNEQS GTELKGDWLD KMLSADKGDF QYTMDGDKKK
260 270 280 290 300
MAFDTNKLTG WKIGGTMYLD EIHEAAQPVL HLALIVLAAA IIIGIIVMTL
310 320 330 340 350
IIRSITTPLK QLVGSSKRIS EGDLTETIDI RSKDELGELG KSFNNMASSL
360 370 380 390 400
RSLIHAIQDS VDNVAASSEE LTASAAQTSK ATEHITLAIE QFSNGNEKQN
410 420 430 440 450
ENIETAAEHI YQMNDGLTNM AQASEVITDS SVQSTEIASE GGKLVHQTVG
460 470 480 490 500
QMNVIDKSVK EAEQVVRGLE TKSKDITNIL RVINGIADQT NLLALNAAIE
510 520 530 540 550
AARAGEYGRG FSVVAEEVRK LAVQSADSAK EIEGLIIEIV KEINTSLGMF
560 570 580 590 600
QSVNQEVQTG LDITDKTEMS FKRISEMTNQ IAGELQNMSA TVQQLSASSE
610 620 630 640 650
EVSGASEHIA SISKESSAHI QDIAASAEEQ LASMEEISSS AETLSSMAEE
660
LRDMTKRFKI E
Length:661
Mass (Da):72,314
Last modified:July 7, 2009 - v2
Checksum:iE46A09AB33604141
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951A → R in AAA20556 (PubMed:8188684).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29189 Genomic DNA. Translation: AAA20556.1.
AL009126 Genomic DNA. Translation: CAB15102.2.
PIRiB54078.
RefSeqiNP_391002.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15102; CAB15102; BSU31240.
GeneIDi937154.
KEGGibsu:BSU31240.
PATRICi18978206. VBIBacSub10457_3266.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29189 Genomic DNA. Translation: AAA20556.1.
AL009126 Genomic DNA. Translation: CAB15102.2.
PIRiB54078.
RefSeqiNP_391002.2. NC_000964.3.

3D structure databases

ProteinModelPortaliP39214.
SMRiP39214. Positions 303-355, 364-659.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP39214. 23 interactions.
STRINGi224308.BSU31240.

Proteomic databases

PaxDbiP39214.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15102; CAB15102; BSU31240.
GeneIDi937154.
KEGGibsu:BSU31240.
PATRICi18978206. VBIBacSub10457_3266.

Organism-specific databases

GenoListiBSU31240. [Micado]

Phylogenomic databases

eggNOGiCOG0840.
HOGENOMiHOG000083278.
InParanoidiP39214.
KOiK03406.
OMAiRIEDIQH.
OrthoDBiEOG67HJTT.
PhylomeDBiP39214.

Enzyme and pathway databases

BioCyciBSUB:BSU31240-MONOMER.

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]
ProtoNetiSearch...

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 GLU-370; GLN-594; GLU-629 AND GLU-636, DEAMIDATION AT GLN-594, 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 95.
  4. "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: PROTEIN SEQUENCE OF 589-595, DEAMIDATION AT GLN-593 AND GLN-594 BY CHED, MUTAGENESIS OF GLN-593 AND GLN-594.

Entry informationi

Entry nameiMCPA_BACSU
AccessioniPrimary (citable) accession number: P39214
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 7, 2009
Last modified: January 7, 2015
This is version 107 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, Direct protein sequencing, 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.