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Database: UniProt
Entry: Q1G8E4_LACDA
LinkDB: Q1G8E4_LACDA
Original site: Q1G8E4_LACDA 
ID   Q1G8E4_LACDA            Unreviewed;       257 AA.
AC   Q1G8E4;
DT   27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   27-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Tyrosine-protein kinase CpsD {ECO:0000256|ARBA:ARBA00019200};
DE            EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN   Name=epsIC {ECO:0000313|EMBL:CAI98747.1};
GN   OrderedLocusNames=Ldb2009 {ECO:0000313|EMBL:CAI98747.1};
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS   / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS   00102 / Lb 14).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=390333 {ECO:0000313|EMBL:CAI98747.1, ECO:0000313|Proteomes:UP000001259};
RN   [1] {ECO:0000313|EMBL:CAI98747.1, ECO:0000313|Proteomes:UP000001259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 /
RC   NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14
RC   {ECO:0000313|Proteomes:UP000001259};
RX   PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA   van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA   Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA   Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA   Weissenbach J., Ehrlich S.D., Maguin E.;
RT   "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT   and ongoing reductive evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(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; CR954253; CAI98747.1; -; Genomic_DNA.
DR   RefSeq; WP_011544276.1; NZ_JQAV01000029.1.
DR   AlphaFoldDB; Q1G8E4; -.
DR   STRING; 390333.Ldb2009; -.
DR   KEGG; ldb:Ldb2009; -.
DR   PATRIC; fig|390333.7.peg.1760; -.
DR   eggNOG; COG0489; Bacteria.
DR   HOGENOM; CLU_052027_2_4_9; -.
DR   BioCyc; LDEL390333:LDB_RS08745-MONOMER; -.
DR   UniPathway; UPA00934; -.
DR   Proteomes; UP000001259; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001259};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   DOMAIN          51..198
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
SQ   SEQUENCE   257 AA;  28150 MW;  0820304B5DFA88FC CRC64;
     MAFGRKKHLN NDTMKNGVKL ITLANPQSVI SEQFRNIRTN INFMNVDREV KTIVFTSAMA
     SAGKSTVSAN VAITMAQAGK KTILVDADLR RPTMHSTFNV SNSNGLTTLL TSRSMEMDAN
     SVIRESGVEN LSILTAGPIP PNPSELLSSK HMLDLIEDLK QEYDMVVLDL APILDAGETQ
     QLTSFLNGTI LVVRQAYSQK SAVKRAVELL KLTKSPILGY VMNDVDADGD DGYGYGYGYG
     YGYGEEKEKK GLFGRKK
//
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