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O06979 (YVCQ_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Sensor histidine kinase YvcQ
EC=2.7.13.3
Gene names
Name:yvcQ
Ordered Locus Names:BSU34710
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Member of the two-component regulatory system YvcQ/YvcP. Probably activates YvcP by phosphorylation. Ref.3

Catalytic activity

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

Subcellular location

Cell membrane; Multi-pass membrane protein Potential.

Sequence similarities

Contains 1 histidine kinase domain.

Ontologies

Keywords
   Biological processTwo-component regulatory system
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processsignal transduction by phosphorylation

Inferred from electronic annotation. Source: GOC

   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphorelay sensor kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Sensor histidine kinase YvcQ
PRO_0000360785

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3221Helical; Potential
Topological domain33 – 4210Extracellular Potential
Transmembrane43 – 6321Helical; Potential
Topological domain64 – 356293Cytoplasmic Potential
Domain133 – 349217Histidine kinase

Amino acid modifications

Modified residue1361Phosphohistidine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
O06979 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 6A707CC99BBD00D8

FASTA35640,180
        10         20         30         40         50         60 
MLKTYLIDRL AIILFSLLGI GSAMLIAYLS IVESGAEPSK ENMMYIWILP GTLLAAGFAA 

        70         80         90        100        110        120 
DYVRQFSFLT YVKKLAEQAS SSNDIGQSLK ARKPRTGEQA LWTKMINALG QQYESRLSQY 

       130        140        150        160        170        180 
INQQKQHYTF TNQWVHHMKT PVSVISLMIQ EGKNGTSSSF PTFLEELEDE NERFRHGLDM 

       190        200        210        220        230        240 
MLQTARLEEF AFDVKPQTFD LAEMVRSLIN QEKRQFIKRR LFPTLHVPPN AVQISSDQKW 

       250        260        270        280        290        300 
LSFVVEQILF NALKYSKQGV GDPITIRIET QGHETRLSVA DEGIGIPPQD LPRIFDAFFT 

       310        320        330        340        350 
GENGRTMKEA TGMGLYLAKQ VCSRLGHKLY AESKEGAGTV MTIVFSSDTL VNVTAL

« Hide

References

« Hide 'large scale' references
[1]Denizot F.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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. expand/collapse author list , 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]"Comprehensive DNA microarray analysis of Bacillus subtilis two-component regulatory systems."
Kobayashi K., Ogura M., Yamaguchi H., Yoshida K., Ogasawara N., Tanaka T., Fujita Y.
J. Bacteriol. 183:7365-7370(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z94043 Genomic DNA. Translation: CAB08063.1.
AL009126 Genomic DNA. Translation: CAB15476.1.
PIRE70032.
RefSeqNP_391351.1. NC_000964.3.

3D structure databases

ProteinModelPortalO06979.
SMRO06979. Positions 116-349.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU34710.

Proteomic databases

PaxDbO06979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15476; CAB15476; BSU34710.
GeneID938024.
KEGGbsu:BSU34710.
PATRIC18978946. VBIBacSub10457_3635.

Organism-specific databases

GenoListBSU34710.

Phylogenomic databases

eggNOGCOG0642.
HOGENOMHOG000032012.
KOK02484.
OMAENERFRH.
ProtClustDBCLSK247695.

Enzyme and pathway databases

BioCycBSUB:BSU34710-MONOMER.

Family and domain databases

Gene3D3.30.565.10. 1 hit.
InterProIPR003594. HATPase_ATP-bd.
IPR004358. Sig_transdc_His_kin-like_C.
IPR003661. Sig_transdc_His_kin_sub1_dim/P.
IPR005467. Sig_transdc_His_kinase_core.
[Graphical view]
PfamPF02518. HATPase_c. 1 hit.
[Graphical view]
PRINTSPR00344. BCTRLSENSOR.
SMARTSM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
[Graphical view]
SUPFAMSSF55874. ATP_bd_ATPase. 1 hit.
PROSITEPS50109. HIS_KIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameYVCQ_BACSU
AccessionPrimary (citable) accession number: O06979
Secondary accession number(s): Q795G1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: July 1, 1997
Last modified: May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents