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P96716 (YWQD_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase YwqD

EC=2.7.10.2
Gene names
Name:ywqD
Ordered Locus Names:BSU36250
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB. Ref.3 Ref.4

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Post-translational modification

Autophosphorylated in vitro, which inhibits ATPase activity. Dephosphorylated by YwqE in vitro. Ref.3

Sequence similarities

Belongs to the CpsD/CapB family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 237237Tyrosine-protein kinase YwqD
PRO_0000217242

Sites

Site811Required for activity
Site831Required for activity

Amino acid modifications

Modified residue2281Phosphotyrosine; by autocatalysis Ref.3

Experimental info

Mutagenesis811D → A: Abolishes ATPase activity. Ref.3
Mutagenesis831D → A: Abolishes ATPase activity. Ref.3
Mutagenesis2251Y → F: Prevents phosphorylation and increases ATPase activity; when associated with F-227 and F-228. Ref.3
Mutagenesis2271Y → F: Prevents phosphorylation and increases ATPase activity; when associated with F-225 and F-228. Ref.3
Mutagenesis2281Y → F: Prevents phosphorylation and increases ATPase activity; when associated with F-225 and F-227. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P96716 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 40BE35B5E3FF97D7

FASTA23725,790
        10         20         30         40         50         60 
MALRKNRGSR MQRNVIAMTE PKSLNSEQYR TIRTNIEFAS VDRQMKSVMI TSACPGEGKS 

        70         80         90        100        110        120 
TTAANLAVVF AQQGKKVLLI DADLRKPTVH TAFFLENTVG LTSVLLKKSS MEQAVQASNE 

       130        140        150        160        170        180 
KHLDVLTSGP IPPNPAELLS SKWMKELAYE ACAAYDMVIF DTPPILAVAD AQILGNVADG 

       190        200        210        220        230 
SVLVISSGKT EKEQAAKAKE ALATCKSKLL GAIMNGKKLS KHSEYGYYGT KDNFMQK 

« Hide

References

« Hide 'large scale' references
[1]"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)."
Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
Microbiology 143:3313-3328(1997) [PubMed] [Europe PMC] [Abstract]
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]"Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases."
Mijakovic I., Poncet S., Boel G., Maze A., Gillet S., Jamet E., Decottignies P., Grangeasse C., Doublet P., Le Marechal P., Deutscher J.
EMBO J. 22:4709-4718(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-81; ASP-83; TYR-225; TYR-227 AND TYR-228, PHOSPHORYLATION AT TYR-228.
[4]"Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine."
Mijakovic I., Petranovic D., Macek B., Cepo T., Mann M., Davies J., Jensen P.R., Vujaklija D.
Nucleic Acids Res. 34:1588-1596(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z92952 Genomic DNA. Translation: CAB07457.1.
AL009126 Genomic DNA. Translation: CAB15642.1.
PIRG70066.
RefSeqNP_391506.1. NC_000964.3.

3D structure databases

ProteinModelPortalP96716.
SMRP96716. Positions 6-230.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU36250.

PTM databases

PhosSiteP0310110.

Proteomic databases

PaxDbP96716.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15642; CAB15642; BSU36250.
GeneID936896.
KEGGbsu:BSU36250.
PATRIC18979270. VBIBacSub10457_3797.

Organism-specific databases

GenoListBSU36250.

Phylogenomic databases

eggNOGCOG0489.
HOGENOMHOG000004334.
KOK00903.
OMAIAHQADA.
OrthoDBEOG69D3H6.
ProtClustDBCLSK888014.

Enzyme and pathway databases

BioCycBSUB:BSU36250-MONOMER.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR025669. AAA_dom.
IPR005702. EPS_synthesis.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF13614. AAA_31. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01007. eps_fam. 1 hit.
ProtoNetSearch...

Entry information

Entry nameYWQD_BACSU
AccessionPrimary (citable) accession number: P96716
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Bacillus subtilis

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