ID   CPSD_STRAG              Reviewed;         229 AA.
AC   P0C0T9; Q93TJ2; Q9ALX5; Q9S0S7;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Tyrosine-protein kinase CpsD;
DE            EC=2.7.10.2;
GN   Name=cpsD; Synonyms=cpsIaD;
OS   Streptococcus agalactiae.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NT6 / Serotype VI;
RA   McKinnon K., Chaffin D.O., Rubens C.E.;
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49446 / 3139 / CNCTC 1/82 / Serotype IV;
RA   McKinnon K., Chaffin D.O., Rubens C.E.;
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
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; AF337958; AAK11661.1; -; Genomic_DNA.
DR   EMBL; AF355776; AAK43605.1; -; Genomic_DNA.
DR   RefSeq; WP_000197406.1; NZ_MBLL01000044.1.
DR   RefSeq; WP_000197418.1; NZ_WNJB01000002.1.
DR   AlphaFoldDB; P0C0T9; -.
DR   SMR; P0C0T9; -.
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   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..229
FT                   /note="Tyrosine-protein kinase CpsD"
FT                   /id="PRO_0000217237"
FT   VARIANT         54
FT                   /note="T -> I (in strain: CNTC 1/82)"
FT   VARIANT         167
FT                   /note="S -> N (in strain: CNTC 1/82)"
FT   VARIANT         173
FT                   /note="V -> I (in strain: CNTC 1/82)"
FT   VARIANT         219
FT                   /note="G -> GDYG (in strain: CNTC 1/82)"
SQ   SEQUENCE   229 AA;  25053 MW;  AD8133B41ECAC237 CRC64;
     MTRLEIVDSK LRQAKKTEEY FNAIRTNIQF SGKENKILAI TSVREGEGKS TTSTSLALSL
     AQAGFKTLLI DADTRNSVMS GTFKATGTIK GLTNYLSGNA DLGDIICETN VPRLMVVPSG
     KVPPNPTALL QNAYFNKMIE AIKNIFDYII IDTPPIGLVV DAAIIASACD GFVLVTQAGR
     IKRNYVEKAK EQMEQSGSKF LGIILNKVNE SVATYGDYGN YGKRDRKRK