Q9AFI1 (CPSD_STRA5) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase CpsD
EC=2.7.10.2

Gene names

Name:	cpsD
Ordered Locus Names:	SAG1172

Organism

Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R) [Complete proteome] [HAMAP]

Taxonomic identifier

208435 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus agalactiae › Streptococcus agalactiae serogroup V

Protein attributes

Sequence length	229 AA.
Sequence status	Complete.
Protein existence	Inferred 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 By similarity.
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.

Ontologies

Keywords
Biological process	Capsule biogenesis/degradation Exopolysaccharide synthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	capsule polysaccharide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway regulation of catalytic activity Inferred from electronic annotation. Source: GOC
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW enzyme regulator activity Inferred from electronic annotation. Source: InterPro non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 229	229	Tyrosine-protein kinase CpsD		PRO_0000217236
Experimental info
	Sequence conflict	219	1	G → GDYG Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9AFI1 [UniParc]. Last modified January 17, 2003. Version 2. Checksum: 47806254BE6FC580	FASTA	229	25,064
	10 20 30 40 50 60 MTRLEIVDSK LRQAKKTEEY FNAIRTNIQF SGKENKILAI TSVREGEGKS TASTSLALSL 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 IKRNYVEKAK EQMEQSGSKF LGIILNKVNE SVATYGDYGN YGKRDRKRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Streptococcus agalactiae type V polysaccharide synthesis operon complete sequence." McKinnon K., Chaffin D.O., Rubens C.E. Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CNCTC 1/82 / Serotype V.
[2]	"Complete genome sequence and comparative genomic analysis of an emerging human pathogen, serotype V Streptococcus agalactiae." Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N., Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D., Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F. , Madupu R., Lewis M.R., Radune D., Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A., Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T., Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D., Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-611 / 2603 V/R.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF349539 Genomic DNA. Translation: AAK29650.1. AE009948 Genomic DNA. Translation: AAN00054.1.
RefSeq	NP_688181.1. NC_004116.1.
3D structure databases
ProteinModelPortal	Q9AFI1.
ModBase	Search...
Protein-protein interaction databases
STRING	208435.SAG1172.
Protocols and materials databases
DNASU	1013979.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN00054; AAN00054; SAG1172.
GeneID	1013979.
KEGG	sag:SAG1172.
PATRIC	19629180. VBIStrAga72745_1178.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0489.
HOGENOM	HOG000004334.
OMA	PDEIEMI.
ProtClustDB	CLSK883944.
Enzyme and pathway databases
BioCyc	SAGA208435:GHVY-1173-MONOMER.
UniPathway	UPA00934.
Family and domain databases
InterPro	IPR025669. AAA_dom. IPR005702. EPS_synthesis. [Graphical view]
Pfam	PF13614. AAA_31. 1 hit. [Graphical view]
TIGRFAMs	TIGR01007. eps_fam. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CPSD_STRA5

Accession

Primary (citable) accession number: Q9AFI1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 17, 2003
Last sequence update:	January 17, 2003
Last modified:	May 1, 2013
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program