ID   CPSD_STRA1              Reviewed;         232 AA.
AC   Q3K0T0; Q93TJ2; Q9ALX5; Q9S0S7;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Tyrosine-protein kinase CpsD;
DE            EC=2.7.10.2;
GN   Name=cpsD; Synonyms=cpsIaD; OrderedLocusNames=SAK_1259;
OS   Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS   SS700).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=205921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=OI1 / Serotype Ia;
RX   PubMed=10464185; DOI=10.1128/jb.181.17.5176-5184.1999;
RA   Yamamoto S., Miyake K., Koike Y., Watanabe M., Machida Y., Ohta M.,
RA   Iijima S.;
RT   "Molecular characterization of type-specific capsular polysaccharide
RT   biosynthesis genes of Streptococcus agalactiae type Ia.";
RL   J. Bacteriol. 181:5176-5184(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27591 / A909 / CDC SS700;
RX   PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA   Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T.,
RA   Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D.,
RA   Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., Brinkac L.M.,
RA   Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H.,
RA   Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D.,
RA   Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O.,
RA   Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L.,
RA   Wessels M.R., Rappuoli R., Fraser C.M.;
RT   "Genome analysis of multiple pathogenic isolates of Streptococcus
RT   agalactiae: implications for the microbial 'pan-genome'.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005).
RN   [3]
RP   FUNCTION.
RC   STRAIN=515 / Serotype Ia;
RX   PubMed=11027683; DOI=10.1074/jbc.m005702200;
RA   Cieslewicz M.J., Kasper D.L., Wang Y., Wessels M.R.;
RT   "Functional analysis in type Ia group B Streptococcus of a cluster of genes
RT   involved in extracellular polysaccharide production by diverse species of
RT   Streptococci.";
RL   J. Biol. Chem. 276:139-146(2001).
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. {ECO:0000269|PubMed:11027683}.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB028896; BAA82278.1; -; Genomic_DNA.
DR   EMBL; CP000114; ABA45962.1; -; Genomic_DNA.
DR   RefSeq; WP_000197416.1; NC_007432.1.
DR   AlphaFoldDB; Q3K0T0; -.
DR   SMR; Q3K0T0; -.
DR   KEGG; sak:SAK_1259; -.
DR   HOGENOM; CLU_052027_2_0_9; -.
DR   UniPathway; UPA00934; -.
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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05387; BY-kinase; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR025669; AAA_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005702; Wzc-like_C.
DR   NCBIfam; TIGR01007; eps_fam; 1.
DR   PANTHER; PTHR32309; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR32309:SF13; TYROSINE-PROTEIN KINASE ETK-RELATED; 1.
DR   Pfam; PF13614; AAA_31; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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_0000217238"
FT   CONFLICT        218..220
FT                   /note="Missing (in Ref. 1; BAA82278)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   232 AA;  25402 MW;  DE4CFA15A9C77C26 CRC64;
     MTRLEIVDSK LRQAKKTEEY FNAIRTNIQF SGKENKILAI TSVREGEGKS TTSTSLALSL
     AQAGFKTLLI DADTRNSVMS GTFKATGTIK GLTNYLSGNA DLGDIICETN VPRLMVVPSG
     KVPPNPTALL QNAYFNKMIE AIKNIFDYII IDTPPIGLVV DAAIIANACD GFILVTQAGR
     IKRNYVEKAK EQMEQSGSKF LGIILNKVSE SVATYGDYGD YGNYGKRDRK RK
//