SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P96716

- YWQD_BACSU

UniProt

P96716 - YWQD_BACSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Tyrosine-protein kinase YwqD
Gene
ywqD, BSU36250
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 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. enzyme regulator activity Source: InterPro
  3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. capsule 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 YwqD
PRO_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

Protein-protein interaction databases

STRINGi224308.BSU36250.

Structurei

3D structure databases

ProteinModelPortaliP96716.
SMRiP96716. Positions 6-230.

Family & Domainsi

Sequence similaritiesi

Belongs to the CpsD/CapB family.

Phylogenomic databases

eggNOGiCOG0489.
HOGENOMiHOG000004334.
KOiK00903.
OMAiNSVIRES.
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

MALRKNRGSR MQRNVIAMTE PKSLNSEQYR TIRTNIEFAS VDRQMKSVMI    50
TSACPGEGKS TTAANLAVVF AQQGKKVLLI DADLRKPTVH TAFFLENTVG 100
LTSVLLKKSS MEQAVQASNE KHLDVLTSGP IPPNPAELLS SKWMKELAYE 150
ACAAYDMVIF DTPPILAVAD AQILGNVADG SVLVISSGKT EKEQAAKAKE 200
ALATCKSKLL GAIMNGKKLS KHSEYGYYGT KDNFMQK 237
Length:237
Mass (Da):25,790
Last modified:May 1, 1997 - v1
Checksum:i40BE35B5E3FF97D7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
Z92952 Genomic DNA. Translation: CAB07457.1 .
AL009126 Genomic DNA. Translation: CAB15642.1 .
PIRi G70066.
RefSeqi NP_391506.1. NC_000964.3.

3D structure databases

ProteinModelPortali P96716.
SMRi P96716. Positions 6-230.
ModBasei Search...

Protein-protein interaction databases

STRINGi 224308.BSU36250.

PTM databases

PhosSitei P0310110.

Proteomic databases

PaxDbi P96716.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15642 ; CAB15642 ; BSU36250 .
GeneIDi 936896.
KEGGi bsu:BSU36250.
PATRICi 18979270. VBIBacSub10457_3797.

Organism-specific databases

GenoListi BSU36250.

Phylogenomic databases

eggNOGi COG0489.
HOGENOMi HOG000004334.
KOi K00903.
OMAi NSVIRES.
OrthoDBi EOG69D3H6.
PhylomeDBi P96716.

Enzyme and pathway databases

BioCyci BSUB:BSU36250-MONOMER.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR025669. AAA_dom.
IPR005702. EPS_synthesis.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF13614. AAA_31. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01007. eps_fam. 1 hit.
ProtoNeti Search...

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: July 9, 2014
This is version 95 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