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P39214

- MCPA_BACSU

UniProt

P39214 - MCPA_BACSU

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Protein
Methyl-accepting chemotaxis protein McpA
Gene
mcpA, BSU31240
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. McpA is required for taxis towards glucose and alpha-methylglucoside.1 Publication

GO - Molecular functioni

  1. transmembrane signaling receptor activity Source: InterPro
Complete GO annotation...

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 – 1616Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei17 – 3721Helical; Reviewed prediction
Add
BLAST
Topological domaini38 – 281244Extracellular Reviewed prediction
Add
BLAST
Transmembranei282 – 30221Helical; Reviewed prediction
Add
BLAST
Topological domaini303 – 661359Cytoplasmic Reviewed prediction
Add
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 McpA
PRO_0000110556Add
BLAST

Amino acid modifications

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

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.1 Publication

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini152 – 22877Cache
Add
BLAST
Domaini303 – 35553HAMP
Add
BLAST
Domaini374 – 610237Methyl-accepting transducer
Add
BLAST

Sequence similaritiesi

Contains 1 cache domain.
Contains 1 HAMP domain.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0840.
HOGENOMiHOG000083278.
KOiK03406.
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

MKKILQLIKQ RSITRKLLVS FLSILIIPVV ILAIFAYQSA SSSLDRQMMG    50
SALENVQQLN EIINTSIGEK ENSADYFSEW LTKEKYNAKS NASIAEKFSQ 100
YISINKDVES IYTSDTKGHF TRYPDLPMPS GYNPVERDWY KKAVANKGKV 150
VITDPYKTAS TNTMVVTIAQ QTKDGSGVIA INMTIENLLK TTKKVNIGTQ 200
GYAFIMTKDK KVVAHPNEQS GTELKGDWLD KMLSADKGDF QYTMDGDKKK 250
MAFDTNKLTG WKIGGTMYLD EIHEAAQPVL HLALIVLAAA IIIGIIVMTL 300
IIRSITTPLK QLVGSSKRIS EGDLTETIDI RSKDELGELG KSFNNMASSL 350
RSLIHAIQDS VDNVAASSEE LTASAAQTSK ATEHITLAIE QFSNGNEKQN 400
ENIETAAEHI YQMNDGLTNM AQASEVITDS SVQSTEIASE GGKLVHQTVG 450
QMNVIDKSVK EAEQVVRGLE TKSKDITNIL RVINGIADQT NLLALNAAIE 500
AARAGEYGRG FSVVAEEVRK LAVQSADSAK EIEGLIIEIV KEINTSLGMF 550
QSVNQEVQTG LDITDKTEMS FKRISEMTNQ IAGELQNMSA TVQQLSASSE 600
EVSGASEHIA SISKESSAHI QDIAASAEEQ LASMEEISSS AETLSSMAEE 650
LRDMTKRFKI E 661
Length:661
Mass (Da):72,314
Last modified:July 7, 2009 - v2
Checksum:iE46A09AB33604141
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951A → R in AAA20556. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
L29189 Genomic DNA. Translation: AAA20556.1 .
AL009126 Genomic DNA. Translation: CAB15102.2 .
PIRi B54078.
RefSeqi NP_391002.2. NC_000964.3.

3D structure databases

ProteinModelPortali P39214.
SMRi P39214. Positions 303-355, 364-659.
ModBasei Search...

Protein-protein interaction databases

IntActi P39214. 23 interactions.
STRINGi 224308.BSU31240.

Proteomic databases

PaxDbi P39214.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15102 ; CAB15102 ; BSU31240 .
GeneIDi 937154.
KEGGi bsu:BSU31240.
PATRICi 18978206. VBIBacSub10457_3266.

Organism-specific databases

GenoListi BSU31240. [Micado ]

Phylogenomic databases

eggNOGi COG0840.
HOGENOMi HOG000083278.
KOi K03406.
OrthoDBi EOG67HJTT.
PhylomeDBi P39214.

Enzyme and pathway databases

BioCyci BSUB:BSU31240-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 GLU-370; GLN-594; GLU-629 AND GLU-636, 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: July 9, 2014
This is version 104 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

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