ID   CPSD_STRA5              Reviewed;         229 AA.
AC   Q9AFI1;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   17-JAN-2003, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Tyrosine-protein kinase CpsD;
DE            EC=2.7.10.2;
GN   Name=cpsD; OrderedLocusNames=SAG1172;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CNCTC 1/82 / Serotype V;
RA   McKinnon K., Chaffin D.O., Rubens C.E.;
RT   "Streptococcus agalactiae type V polysaccharide synthesis operon complete
RT   sequence.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(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}.
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DR   EMBL; AF349539; AAK29650.1; -; Genomic_DNA.
DR   EMBL; AE009948; AAN00054.1; -; Genomic_DNA.
DR   RefSeq; NP_688181.1; NC_004116.1.
DR   RefSeq; WP_000197405.1; NC_004116.1.
DR   AlphaFoldDB; Q9AFI1; -.
DR   SMR; Q9AFI1; -.
DR   STRING; 208435.SAG1172; -.
DR   DNASU; 1013979; -.
DR   EnsemblBacteria; AAN00054; AAN00054; SAG1172.
DR   KEGG; sag:SAG1172; -.
DR   PATRIC; fig|208435.3.peg.1178; -.
DR   HOGENOM; CLU_052027_2_0_9; -.
DR   OMA; MQCIQKT; -.
DR   UniPathway; UPA00934; -.
DR   Proteomes; UP000000821; 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; Reference proteome;
KW   Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..229
FT                   /note="Tyrosine-protein kinase CpsD"
FT                   /id="PRO_0000217236"
FT   CONFLICT        219
FT                   /note="G -> GDYG (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   229 AA;  25064 MW;  47806254BE6FC580 CRC64;
     MTRLEIVDSK LRQAKKTEEY FNAIRTNIQF SGKENKILAI TSVREGEGKS TASTSLALSL
     AQAGFKTLLI DADTRNSVMS GTFKATGTIK GLTNYLSGNA DLGDIICETN VPRLMVVPSG
     KVPPNPTALL QNAYFNKMIE AIKNIFDYII IDTPPIGLVV DAAIIANACD GFILVTQAGR
     IKRNYVEKAK EQMEQSGSKF LGIILNKVNE SVATYGDYGN YGKRDRKRK