ID   CPSD_STRPN              Reviewed;         227 AA.
AC   Q9AHD2;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Tyrosine-protein kinase CpsD;
DE            EC=2.7.10.2;
GN   Name=cpsD; Synonyms=wze; OrderedLocusNames=SP_0349;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WCH35 / Serotype 4;
RX   PubMed=11179285; DOI=10.1128/iai.69.3.1244-1255.2001;
RA   Jiang S.-M., Wang L., Reeves P.R.;
RT   "Molecular characterization of Streptococcus pneumoniae type 4, 6B, 8, and
RT   18C capsular polysaccharide gene clusters.";
RL   Infect. Immun. 69:1244-1255(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(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 (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; AF316639; AAK20669.1; -; Genomic_DNA.
DR   EMBL; AE005672; AAK74522.1; -; Genomic_DNA.
DR   PIR; A95041; A95041.
DR   RefSeq; WP_001142502.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; Q9AHD2; -.
DR   SMR; Q9AHD2; -.
DR   STRING; 170187.SP_0349; -.
DR   EnsemblBacteria; AAK74522; AAK74522; SP_0349.
DR   KEGG; spn:SP_0349; -.
DR   eggNOG; COG0489; Bacteria.
DR   OMA; MQCIQKT; -.
DR   PhylomeDB; Q9AHD2; -.
DR   BioCyc; SPNE170187:G1FZB-359-MON; -.
DR   UniPathway; UPA00934; -.
DR   Proteomes; UP000000585; 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..227
FT                   /note="Tyrosine-protein kinase CpsD"
FT                   /id="PRO_0000217239"
SQ   SEQUENCE   227 AA;  24887 MW;  79D4882D336943B8 CRC64;
     MPTLEIAQKK LEFIKKAEEY YNALCTNIQL SGDKLKVISV TSVNPGEGKT TTSINIAWSF
     ARAGYKTLLI DGDTRNSVML GVFKSREKIT GLTEFLSGTA DLSHGLCDTN IENLFVVQSG
     SVSPNPTALL QSKNFNDMIE TLRKYFDYII IDTPPIGIVI DAAIITQKCD ASILVTATGE
     ANKRDIQKAK QQLKQTGKLF LGVVLNKLDI SVNKYGVYGS YGNYGKK