ID   CPSD_STRA3              Reviewed;         232 AA.
AC   Q04663;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   17-JAN-2003, sequence version 3.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Tyrosine-protein kinase CpsD;
DE            EC=2.7.10.2;
GN   Name=cpsD; OrderedLocusNames=gbs1245;
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=COH1 / Serotype III;
RX   PubMed=8355611; DOI=10.1111/j.1365-2958.1993.tb01631.x;
RA   Rubens C.E., Heggen L.M., Haft R.F., Wessels M.R.;
RT   "Identification of cpsD, a gene essential for type III capsule expression
RT   in group B streptococci.";
RL   Mol. Microbiol. 8:843-855(1993).
RN   [2]
RP   SEQUENCE REVISION.
RA   Yim H.;
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA   Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT   neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(2002).
CC   -!- FUNCTION: Involved in the regulation of capsular polysaccharide
CC       biosynthesis. Autophosphorylation of CpsD attenuates its activity and
CC       reduces the level of encapsulation. May be part of a complex that
CC       directs the coordinated polymerization and export to the cell surface
CC       of the capsular polysaccharide (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC   -!- ACTIVITY REGULATION: Dephosphorylated and activated by CpsB.
CC       {ECO:0000250}.
CC   -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CpsD/CapB family. {ECO:0000305}.
CC   -!- CAUTION: Was originally called CpsC. {ECO:0000305|PubMed:8355611}.
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DR   EMBL; AF163833; AAB00363.1; -; Genomic_DNA.
DR   EMBL; AL766849; CAD46904.1; -; Genomic_DNA.
DR   PIR; S34976; S34976.
DR   PIR; T44642; T44642.
DR   RefSeq; WP_000197412.1; NC_004368.1.
DR   AlphaFoldDB; Q04663; -.
DR   SMR; Q04663; -.
DR   STRING; 211110.gbs1244; -.
DR   EnsemblBacteria; CAD46904; CAD46904; CAD46904.
DR   KEGG; san:cpsD; -.
DR   eggNOG; COG0489; Bacteria.
DR   HOGENOM; CLU_052027_2_0_9; -.
DR   OMA; MQCIQKT; -.
DR   UniPathway; UPA00934; -.
DR   Proteomes; UP000000823; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR025669; AAA_dom.
DR   InterPro; IPR005702; EPS_synthesis.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF13614; AAA_31; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01007; eps_fam; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Capsule biogenesis/degradation; Exopolysaccharide synthesis;
KW   Kinase; Nucleotide-binding; Phosphoprotein; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN           1..232
FT                   /note="Tyrosine-protein kinase CpsD"
FT                   /id="PRO_0000217235"
FT   CONFLICT        41
FT                   /note="T -> A (in Ref. 1; AAB00363)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218..220
FT                   /note="Missing (in Ref. 1; AAB00363)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   232 AA;  25429 MW;  7F81FA15A9C77C33 CRC64;
     MTRLEIVDSK LRQAKKTEEY FNAIRTNIQF SGKENKILAI TSVREGEGKS TTSTSLALSL
     AQAGFKTLLI DADTRNSVMS GTFKATGTIK GLTNYLSGNA DLGDIICETN VPRLMVVPSG
     KVPPNPTALL QNAYFNKMIE AIKNIFDYII IDTPPIGLVV DAAIIANACD GFILVTQAGR
     IKRNYVEKAK EQMEQSGSKF LGIILNKVNE SVATYGDYGD YGNYGKRDRK RK