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Database: UniProt
Entry: U5S9D6_9LACT
LinkDB: U5S9D6_9LACT
Original site: U5S9D6_9LACT 
ID   U5S9D6_9LACT            Unreviewed;       240 AA.
AC   U5S9D6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Tyrosine-protein kinase CpsD {ECO:0000256|ARBA:ARBA00019200};
DE            EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN   ORFNames=Q783_06630 {ECO:0000313|EMBL:AGY81904.1};
OS   Carnobacterium inhibens subsp. gilichinskyi.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=1266845 {ECO:0000313|EMBL:AGY81904.1, ECO:0000313|Proteomes:UP000017469};
RN   [1] {ECO:0000313|EMBL:AGY81904.1, ECO:0000313|Proteomes:UP000017469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WN1359 {ECO:0000313|EMBL:AGY81904.1,
RC   ECO:0000313|Proteomes:UP000017469};
RX   PubMed=24285647;
RA   Leonard M.T., Panayotova N., Farmerie W.G., Triplett E.W., Nicholson W.L.;
RT   "Complete Genome Sequence of Carnobacterium gilichinskyi Strain WN1359T
RT   (DSM 27470T).";
RL   Genome Announc. 1:e00985-13(2013).
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; CP006812; AGY81904.1; -; Genomic_DNA.
DR   RefSeq; WP_023178264.1; NC_022606.1.
DR   AlphaFoldDB; U5S9D6; -.
DR   STRING; 1266845.Q783_06630; -.
DR   KEGG; caw:Q783_06630; -.
DR   PATRIC; fig|1266845.5.peg.1221; -.
DR   eggNOG; COG0489; Bacteria.
DR   HOGENOM; CLU_052027_2_1_9; -.
DR   UniPathway; UPA00934; -.
DR   Proteomes; UP000017469; 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:AGY81904.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   DOMAIN          47..188
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
SQ   SEQUENCE   240 AA;  26785 MW;  846190601B551B96 CRC64;
     MFKKRISEKK YEEKNLITLI DPTSIISEEF RTLRTNIQFS MIDKELKTLM VTSSKQGEGK
     STIAANLAVV FASQGKKVLL VDADMRNPSL HKLFKVRNQQ GLTSILTTKN RQLRSLLHET
     SQENLNLLTS GILPPNPSEL LASQRMAQFI EAVKQEYDLI VFDMPPVNVV TDAQVMGNKA
     DGTVFVIRKE VADLSEILKA KELLNLVQAN VLGAVFNSKE RVKGLNGGYH AKEKELDTVG
//
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