ID   Q4JZ18_STREE            Unreviewed;       227 AA.
AC   Q4JZ18;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Tyrosine-protein kinase CpsD {ECO:0000256|ARBA:ARBA00019200};
DE            EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN   Name=wze {ECO:0000313|EMBL:CAI34447.1};
GN   ORFNames=SPC07B_0007 {ECO:0000313|EMBL:CAI32882.1}, SPC40_0006
GN   {ECO:0000313|EMBL:CAI34447.1};
OS   Streptococcus pneumoniae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1313 {ECO:0000313|EMBL:CAI34447.1};
RN   [1] {ECO:0000313|EMBL:CAI34447.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Colemore {ECO:0000313|EMBL:CAI34447.1}, and Johnson
RC   {ECO:0000313|EMBL:CAI32882.1};
RX   PubMed=16532061; DOI=10.1371/journal.pgen.0020031;
RA   Bentley S.D., Aanensen D.M., Mavroidi A., Saunders D., Rabbinowitsch E.,
RA   Collins M., Donohoe K., Harris D., Murphy L., Quail M.A., Samuel G.,
RA   Skovsted I.C., Kaltoft M.S., Barrell B., Reeves P.R., Parkhill J.,
RA   Spratt B.G.;
RT   "Genetic analysis of the capsular biosynthetic locus from all 90
RT   pneumococcal serotypes.";
RL   PLoS Genet. 2:262-268(2006).
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:0000256|ARBA:ARBA00024964}.
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         Evidence={ECO:0000256|ARBA:ARBA00001149};
CC   -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005132}.
CC   -!- SIMILARITY: Belongs to the CpsD/CapB family.
CC       {ECO:0000256|ARBA:ARBA00007316}.
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DR   EMBL; CR931641; CAI32882.1; -; Genomic_DNA.
DR   EMBL; CR931712; CAI34447.1; -; Genomic_DNA.
DR   RefSeq; WP_050079289.1; NZ_UHHG01000005.1.
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 {ECO:0000256|ARBA:ARBA00022840};
KW   Capsule biogenesis/degradation {ECO:0000256|ARBA:ARBA00022903};
KW   Exopolysaccharide synthesis {ECO:0000256|ARBA:ARBA00023169};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAI34447.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAI34447.1};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   DOMAIN          36..166
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
SQ   SEQUENCE   227 AA;  24786 MW;  BCB8CF887F642D0A CRC64;
     MPTLEIAQKK LEFIKKAEEH YNALCTNIQL SGDKLKVISV TSVNPGEGKT TTSVNIARSF
     ARAGYKTLLI DGDTRNSVMS GFFKSREKIT GLTEFLSGTA DLSHGLCDTN IENLFVVQSG
     SVSPNPTALL QSKNFNDMIE TLRKYFDYII VDTAPIGIVI DAAIITQKCD ASILVTATGE
     VNKRDAQKAK QQLEQTGKLF LGVVLNKLDI SVDKYGVYGS YGNYGKK
//