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Database: UniProt
Entry: F3GE67_PSESJ
LinkDB: F3GE67_PSESJ
Original site: F3GE67_PSESJ 
ID   F3GE67_PSESJ            Unreviewed;       268 AA.
AC   F3GE67;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Lipopolysaccharide core heptose(I) kinase {ECO:0000256|PIRNR:PIRNR037318};
DE            EC=2.7.1.- {ECO:0000256|PIRNR:PIRNR037318};
GN   ORFNames=PSYPI_24829 {ECO:0000313|EMBL:EGH45367.1};
OS   Pseudomonas syringae pv. pisi str. 1704B.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH45367.1, ECO:0000313|Proteomes:UP000004986};
RN   [1] {ECO:0000313|EMBL:EGH45367.1, ECO:0000313|Proteomes:UP000004986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1704B {ECO:0000313|EMBL:EGH45367.1,
RC   ECO:0000313|Proteomes:UP000004986};
RX   PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA   Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA   Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT   "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT   genomics of 19 Pseudomonas syringae isolates.";
RL   PLoS Pathog. 7:E1002132-e1002132(2011).
CC   -!- FUNCTION: Kinase involved in the biosynthesis of the core
CC       oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the
CC       phosphorylation of heptose I (HepI), the first heptose added to the
CC       Kdo2-lipid A module. {ECO:0000256|PIRNR:PIRNR037318}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC       {ECO:0000256|PIRNR:PIRNR037318}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. KdkA/rfaP
CC       family. {ECO:0000256|PIRNR:PIRNR037318}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGH45367.1}.
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DR   EMBL; AEAI01001265; EGH45367.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3GE67; -.
DR   PATRIC; fig|629263.4.peg.4024; -.
DR   HOGENOM; CLU_081267_0_0_6; -.
DR   BioCyc; PSYR629263:G11X0-4495-MONOMER; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000004986; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017172; Lsacc_core_hep_kinase_RfaP.
DR   Pfam; PF06293; Kdo; 1.
DR   PIRSF; PIRSF037318; RfaP; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR037318};
KW   Kinase {ECO:0000256|PIRNR:PIRNR037318, ECO:0000313|EMBL:EGH45367.1};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|PIRNR:PIRNR037318};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037318};
KW   Transferase {ECO:0000256|PIRNR:PIRNR037318}.
SQ   SEQUENCE   268 AA;  30643 MW;  507A70AD0F169014 CRC64;
     MKLFLAEPFK SLWAGRDAFV EIEGLSGEVY RELEGRRTLR TEVDGRGYFV KIHRGIGWGE
     IAKNLATAKL PVLGAGKEWD AIERLHEVGV PTMTAVAYGE RGSNPAAQHS FIVTEELAPT
     TSLEDVSLNW RNESPEPRLK RAFIAEVARL VGMMHRAGVN HRDCYICHFL LHTDKPVTAD
     DFKLSVIDLH RAQTRRAITP RWRNKDLAAL YFSALDIGLT RRDKLRFLQG YFQKPLREIL
     LKEATLLTWL DKKADKLYQR KVRYGDAL
//
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