ID M1VNT5_STRSU Unreviewed; 224 AA.
AC M1VNT5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Tyrosine-protein kinase CpsD {ECO:0000256|ARBA:ARBA00019200};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=cps6C {ECO:0000313|EMBL:BAM94547.1};
GN Synonyms=wze {ECO:0000313|EMBL:CYW13420.1};
GN ORFNames=ERS132453_01570 {ECO:0000313|EMBL:CYW13420.1};
OS Streptococcus suis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1307 {ECO:0000313|EMBL:BAM94547.1};
RN [1] {ECO:0000313|EMBL:BAM94547.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=2524 {ECO:0000313|EMBL:BAM94547.1};
RX PubMed=23416996; DOI=10.1128/AEM.03742-12;
RA Okura M., Takamatsu D., Maruyama F., Nozawa T., Nakagawa I., Osaki M.,
RA Sekizaki T., Gottschalk M., Kumagai Y., Hamada S.;
RT "Genetic analysis of capsular polysaccharide synthesis gene clusters from
RT all serotypes of Streptococcus suis: potential mechanisms for generation of
RT capsular variation.";
RL Appl. Environ. Microbiol. 79:2796-2806(2013).
RN [2] {ECO:0000313|EMBL:CYW13420.1, ECO:0000313|Proteomes:UP000074436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSS91 {ECO:0000313|EMBL:CYW13420.1,
RC ECO:0000313|Proteomes:UP000074436};
RG Pathogen Informatics;
RL Submitted (FEB-2016) 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; AB737818; BAM94547.1; -; Genomic_DNA.
DR EMBL; FIIO01000021; CYW13420.1; -; Genomic_DNA.
DR RefSeq; WP_024386402.1; NZ_FIIO01000021.1.
DR AlphaFoldDB; M1VNT5; -.
DR UniPathway; UPA00934; -.
DR Proteomes; UP000074436; Unassembled WGS sequence.
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:BAM94547.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CYW13420.1};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 36..182
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 224 AA; 24376 MW; CA00829A24FA3612 CRC64;
MTTLEIARTK KELINKTEEY FNAIRTNIQL SGSDIKVVGI TSVQSNEGKS TTAASLAIAY
ARSGYKTVLV DADIRNSVMS GFFKPVTKIT GLTDYLAGTA DLSQGLCDTD IPNLTVIESG
KVSPNPTALL QSKNFENLLA TLRRYYDYVI VDCPPLGLVI DAAIIAQKCD AMVLVVEAGS
VKRSSLKKVK EQLDQTGTPF LGVILNKYDV VTEKYGEYGN YGRK
//