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Q3K0T0 (CPSD_STRA1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 57. 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 CpsD

EC=2.7.10.2
Gene names
Name:cpsD
Synonyms:cpsIaD
Ordered Locus Names:SAK_1259
OrganismStreptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC SS700) [Complete proteome] [HAMAP]
Taxonomic identifier205921 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylation of CpsD attenuates its activity and reduces the level of encapsulation. May be part of a complex that directs the coordinated polymerization and export to the cell surface of the capsular polysaccharide. Ref.3

Catalytic activity

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

Enzyme regulation

Dephosphorylated and activated by CpsB By similarity.

Pathway

Capsule biogenesis; capsule polysaccharide biosynthesis.

Post-translational modification

Autophosphorylated By similarity.

Sequence similarities

Belongs to the CpsD/CapB family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 232232Tyrosine-protein kinase CpsD
PRO_0000217238

Experimental info

Sequence conflict218 – 2203Missing in BAA82278. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3K0T0 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: DE4CFA15A9C77C26

FASTA23225,402
        10         20         30         40         50         60 
MTRLEIVDSK LRQAKKTEEY FNAIRTNIQF SGKENKILAI TSVREGEGKS TTSTSLALSL 

        70         80         90        100        110        120 
AQAGFKTLLI DADTRNSVMS GTFKATGTIK GLTNYLSGNA DLGDIICETN VPRLMVVPSG 

       130        140        150        160        170        180 
KVPPNPTALL QNAYFNKMIE AIKNIFDYII IDTPPIGLVV DAAIIANACD GFILVTQAGR 

       190        200        210        220        230 
IKRNYVEKAK EQMEQSGSKF LGIILNKVSE SVATYGDYGD YGNYGKRDRK RK 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization of type-specific capsular polysaccharide biosynthesis genes of Streptococcus agalactiae type Ia."
Yamamoto S., Miyake K., Koike Y., Watanabe M., Machida Y., Ohta M., Iijima S.
J. Bacteriol. 181:5176-5184(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: OI1 / Serotype Ia.
[2]"Genome analysis of multiple pathogenic isolates of Streptococcus agalactiae: implications for the microbial 'pan-genome'."
Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D., Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T., Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D., Hauser C.R., Sundaram J.P. expand/collapse author list , Nelson W.C., Madupu R., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H., Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D., Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O., Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L., Wessels M.R., Rappuoli R., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27591 / A909 / CDC SS700.
[3]"Functional analysis in type Ia group B Streptococcus of a cluster of genes involved in extracellular polysaccharide production by diverse species of Streptococci."
Cieslewicz M.J., Kasper D.L., Wang Y., Wessels M.R.
J. Biol. Chem. 276:139-146(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: 515 / Serotype Ia.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB028896 Genomic DNA. Translation: BAA82278.1.
CP000114 Genomic DNA. Translation: ABA45962.1.
RefSeqYP_329873.1. NC_007432.1.

3D structure databases

ProteinModelPortalQ3K0T0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205921.SAK_1259.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA45962; ABA45962; SAK_1259.
GeneID3686251.
KEGGsak:SAK_1259.
PATRIC19633793. VBIStrAga82541_1203.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0489.
HOGENOMHOG000004334.
OMAGKYYGKY.
OrthoDBEOG69D3H6.
ProtClustDBCLSK883944.

Enzyme and pathway databases

BioCycSAGA205921:GHD7-1260-MONOMER.
UniPathwayUPA00934.

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 nameCPSD_STRA1
AccessionPrimary (citable) accession number: Q3K0T0
Secondary accession number(s): Q93TJ2, Q9ALX5, Q9S0S7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: November 8, 2005
Last modified: April 16, 2014
This is version 57 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

PATHWAY comments

Index of metabolic and biosynthesis pathways