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Protein

Tyrosine-protein kinase YwqD

Gene

ywqD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei81 – 811Required for activity
Sitei83 – 831Required for activity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. extracellular polysaccharide biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Capsule biogenesis/degradation, Exopolysaccharide synthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU36250-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase YwqD (EC:2.7.10.2)
Gene namesi
Name:ywqD
Ordered Locus Names:BSU36250
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU36250.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi81 – 811D → A: Abolishes ATPase activity. 1 Publication
Mutagenesisi83 – 831D → A: Abolishes ATPase activity. 1 Publication
Mutagenesisi225 – 2251Y → F: Prevents phosphorylation and increases ATPase activity; when associated with F-227 and F-228. 1 Publication
Mutagenesisi227 – 2271Y → F: Prevents phosphorylation and increases ATPase activity; when associated with F-225 and F-228. 1 Publication
Mutagenesisi228 – 2281Y → F: Prevents phosphorylation and increases ATPase activity; when associated with F-225 and F-227. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 237237Tyrosine-protein kinase YwqDPRO_0000217242Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei228 – 2281Phosphotyrosine; by autocatalysis1 Publication

Post-translational modificationi

Autophosphorylated in vitro, which inhibits ATPase activity. Dephosphorylated by YwqE in vitro.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP96716.

PTM databases

PhosSiteiP0310110.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
hprKO344832EBI-9302929,EBI-5242785
minDQ014644EBI-9302929,EBI-6502875
prkCO345072EBI-9302929,EBI-6667154
yabTP375623EBI-9302929,EBI-9303331
ywqCP967156EBI-9302929,EBI-9302918

Protein-protein interaction databases

IntActiP96716. 14 interactions.
STRINGi224308.BSU36250.

Structurei

3D structure databases

ProteinModelPortaliP96716.
SMRiP96716. Positions 6-230.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CpsD/CapB family.Curated

Phylogenomic databases

eggNOGiCOG0489.
HOGENOMiHOG000004334.
InParanoidiP96716.
KOiK00903.
OMAiIAHQADA.
OrthoDBiEOG69D3H6.
PhylomeDBiP96716.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR025669. AAA_dom.
IPR005702. EPS_synthesis.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF13614. AAA_31. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01007. eps_fam. 1 hit.

Sequencei

Sequence statusi: Complete.

P96716-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALRKNRGSR MQRNVIAMTE PKSLNSEQYR TIRTNIEFAS VDRQMKSVMI
60 70 80 90 100
TSACPGEGKS TTAANLAVVF AQQGKKVLLI DADLRKPTVH TAFFLENTVG
110 120 130 140 150
LTSVLLKKSS MEQAVQASNE KHLDVLTSGP IPPNPAELLS SKWMKELAYE
160 170 180 190 200
ACAAYDMVIF DTPPILAVAD AQILGNVADG SVLVISSGKT EKEQAAKAKE
210 220 230
ALATCKSKLL GAIMNGKKLS KHSEYGYYGT KDNFMQK
Length:237
Mass (Da):25,790
Last modified:May 1, 1997 - v1
Checksum:i40BE35B5E3FF97D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z92952 Genomic DNA. Translation: CAB07457.1.
AL009126 Genomic DNA. Translation: CAB15642.1.
PIRiG70066.
RefSeqiNP_391506.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15642; CAB15642; BSU36250.
GeneIDi936896.
KEGGibsu:BSU36250.
PATRICi18979270. VBIBacSub10457_3797.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z92952 Genomic DNA. Translation: CAB07457.1.
AL009126 Genomic DNA. Translation: CAB15642.1.
PIRiG70066.
RefSeqiNP_391506.1. NC_000964.3.

3D structure databases

ProteinModelPortaliP96716.
SMRiP96716. Positions 6-230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP96716. 14 interactions.
STRINGi224308.BSU36250.

PTM databases

PhosSiteiP0310110.

Proteomic databases

PaxDbiP96716.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15642; CAB15642; BSU36250.
GeneIDi936896.
KEGGibsu:BSU36250.
PATRICi18979270. VBIBacSub10457_3797.

Organism-specific databases

GenoListiBSU36250.

Phylogenomic databases

eggNOGiCOG0489.
HOGENOMiHOG000004334.
InParanoidiP96716.
KOiK00903.
OMAiIAHQADA.
OrthoDBiEOG69D3H6.
PhylomeDBiP96716.

Enzyme and pathway databases

BioCyciBSUB:BSU36250-MONOMER.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR025669. AAA_dom.
IPR005702. EPS_synthesis.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF13614. AAA_31. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01007. eps_fam. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiYWQD_BACSU
AccessioniPrimary (citable) accession number: P96716
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: May 1, 1997
Last modified: January 7, 2015
This is version 98 of the entry and version 1 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.