ID   CPSD_STREE              Reviewed;         227 AA.
AC   Q54520; O52234;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Tyrosine-protein kinase CpsD;
DE            EC=2.7.10.2;
GN   Name=cpsD; Synonyms=cps19fD;
OS   Streptococcus pneumoniae.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serotype 19F;
RX   PubMed=7960118; DOI=10.1128/iai.62.12.5384-5396.1994;
RA   Guidolin A., Morona J.K., Morona R., Hansman D., Paton J.C.;
RT   "Nucleotide sequence analysis of genes essential for capsular
RT   polysaccharide biosynthesis in Streptococcus pneumoniae type 19F.";
RL   Infect. Immun. 62:5384-5396(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-196.
RC   STRAIN=NCTC 11906 / Serotype 19F, PO-329 / Serotype 19F,
RC   SP-496 / Serotype 19F, and SP-GA71 / Serotype 19F;
RX   PubMed=9466257; DOI=10.1046/j.1365-2958.1998.00658.x;
RA   Coffey T.J., Enright M.C., Daniels M., Morona J.K., Morona R.,
RA   Hryniewicz W., Paton J.C., Spratt B.G.;
RT   "Recombinational exchanges at the capsular polysaccharide biosynthetic
RT   locus lead to frequent serotype changes among natural isolates of
RT   Streptococcus pneumoniae.";
RL   Mol. Microbiol. 27:73-83(1998).
RN   [3]
RP   CHARACTERIZATION.
RC   STRAIN=Rx1-19F / Serotype 19F;
RX   PubMed=10760144; DOI=10.1046/j.1365-2958.2000.01808.x;
RA   Morona J.K., Paton J.C., Miller D.C., Morona R.;
RT   "Tyrosine phosphorylation of CpsD negatively regulates capsular
RT   polysaccharide biosynthesis in Streptococcus pneumoniae.";
RL   Mol. Microbiol. 35:1431-1442(2000).
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.
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   -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Autophosphorylated.
CC   -!- SIMILARITY: Belongs to the CpsD/CapB family. {ECO:0000305}.
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DR   EMBL; U09239; AAC44961.1; -; Genomic_DNA.
DR   EMBL; AF030367; AAC38719.1; -; Genomic_DNA.
DR   EMBL; AF030368; AAC38724.1; -; Genomic_DNA.
DR   EMBL; AF030370; AAC38733.1; -; Genomic_DNA.
DR   EMBL; AF030371; AAC38738.1; -; Genomic_DNA.
DR   RefSeq; WP_050128984.1; NZ_PIZF01000014.1.
DR   AlphaFoldDB; Q54520; -.
DR   SMR; Q54520; -.
DR   UniPathway; UPA00934; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   ATP-binding; Capsule biogenesis/degradation; Cytoplasm;
KW   Exopolysaccharide synthesis; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..227
FT                   /note="Tyrosine-protein kinase CpsD"
FT                   /id="PRO_0000217240"
FT   VARIANT         14
FT                   /note="I -> V (in strain: NCTC 11906 and PO-329)"
FT   VARIANT         74
FT                   /note="T -> I (in strain: NCTC 11906 and PO-329)"
SQ   SEQUENCE   227 AA;  24949 MW;  42EF26DE49CF9773 CRC64;
     MPTLEIAQKK LEFIKKAEEY YNALCTNIQL SGDKLKVISV TSVNPGEGKT TTSVNIARSF
     ARAGYKTLLI DGDTRNSVMS GFFKSREKIT GLTEFLSGTA DLSHGLCDTN IENLFVVQSG
     TVSPNPTALL QSKNFNDMIE TLRKYFDYII VDTAPIGIVI DAAIITQKCD ASILVTATGE
     VNKRDVQKAK QQLEQTGKLF LGVVFNKLDI SVDKYGVYGF YGNYGKK