ID Q83YR5_STRGN Unreviewed; 233 AA.
AC Q83YR5; A0A0F3HTD5;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 71.
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:AAN64566.1};
GN ORFNames=A6J85_04370 {ECO:0000313|EMBL:ARC46694.1}, TZ86_01436
GN {ECO:0000313|EMBL:KJQ59565.1};
OS Streptococcus gordonii.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1302 {ECO:0000313|EMBL:AAN64566.1};
RN [1] {ECO:0000313|EMBL:AAN64566.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=38 {ECO:0000313|EMBL:AAN64566.1};
RA Xu D.-Q., Cisar J.O.;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAN64566.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=38 {ECO:0000313|EMBL:AAN64566.1};
RX PubMed=12949094; DOI=10.1128/JB.185.18.5419-5430.2003;
RA Xu D.Q., Thompson J., Cisar J.O.;
RT "Genetic loci for coaggregation receptor polysaccharide biosynthesis in
RT Streptococcus gordonii 38.";
RL J. Bacteriol. 185:5419-5430(2003).
RN [3] {ECO:0000313|EMBL:KJQ59565.1, ECO:0000313|Proteomes:UP000033658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G9B {ECO:0000313|EMBL:KJQ59565.1,
RC ECO:0000313|Proteomes:UP000033658};
RA Haase E.M.;
RT "Evolution of amylase-binding proteins of oral streptococcal species.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000191220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_257 {ECO:0000313|Proteomes:UP000191220};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S., Nadendla S.,
RA Geyer C., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:ARC46694.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FDAARGOS_257 {ECO:0000313|EMBL:ARC46694.1};
RA Campos J., Goldberg B., Tallon L., Sadzewicz L., Sengamalay N., Ott S.,
RA Godinez A., Nagaraj S., Vyas G., Aluvathingal J., Nadendla S., Geyer C.,
RA Nandy P., Hobson J., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (DEC-2017) 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. {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; AY147914; AAN64566.1; -; Genomic_DNA.
DR EMBL; CP020450; ARC46694.1; -; Genomic_DNA.
DR EMBL; JYGL01000001; KJQ59565.1; -; Genomic_DNA.
DR RefSeq; WP_008809952.1; NZ_RJVX01000025.1.
DR PATRIC; fig|1302.15.peg.1435; -.
DR UniPathway; UPA00934; -.
DR Proteomes; UP000033658; Unassembled WGS sequence.
DR Proteomes; UP000191220; 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 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:ARC46694.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KJQ59565.1};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 36..164
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 233 AA; 25244 MW; 81A7002A237B5F9B CRC64;
MATLEIIKNK LAEMHQAEEY FNALSTNIQL SGSDIKVVAV SSVQPNEGKS TISINLSLAF
ARAGYRTLLI DADIRNSVMT GVFKSQRKVE GLTEVLSGNA DISRALADTD YPNLDVFLSG
QVSPNPTGLL QGKNFEVIMG VLREHYDYIV VDTPPIGMVI DAAIIAQRCD GSFLVSASGA
VSRKAVQKAK EQLEQTGTPF LGVVLNKFDV KSEKYGSYGN YGNYGNYGNY GKK
//
