ID V9UUY4_9PSED Unreviewed; 268 AA.
AC V9UUY4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Lipopolysaccharide core heptose(I) kinase {ECO:0000256|PIRNR:PIRNR037318};
DE EC=2.7.1.- {ECO:0000256|PIRNR:PIRNR037318};
GN ORFNames=X970_00020 {ECO:0000313|EMBL:AHC85853.1};
OS Pseudomonas monteilii SB3101.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1435058 {ECO:0000313|EMBL:AHC85853.1, ECO:0000313|Proteomes:UP000018660};
RN [1] {ECO:0000313|EMBL:AHC85853.1, ECO:0000313|Proteomes:UP000018660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3101 {ECO:0000313|EMBL:AHC85853.1,
RC ECO:0000313|Proteomes:UP000018660};
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D., Nilsen P.H.,
RA Nielsen J.L.;
RT "Complete Genomes of Pseudomonas monteilii SB3078 and SB3101, two Benzene,
RT Toluene and Ethylbenzene Degrading Bacteria used for Bioaugmentation.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP006979; AHC85853.1; -; Genomic_DNA.
DR RefSeq; WP_013970539.1; NC_023076.1.
DR AlphaFoldDB; V9UUY4; -.
DR GeneID; 58533211; -.
DR KEGG; pmot:X970_00020; -.
DR PATRIC; fig|1435058.3.peg.4; -.
DR HOGENOM; CLU_081267_0_0_6; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000018660; Chromosome.
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:AHC85853.1};
KW Lipopolysaccharide biosynthesis {ECO:0000256|PIRNR:PIRNR037318};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037318};
KW Transferase {ECO:0000256|PIRNR:PIRNR037318}.
SQ SEQUENCE 268 AA; 30759 MW; F71BF3C61C0145D2 CRC64;
MKLILAEPFK RLWAGRDAFD AVEALQGEVY RELEGRRTLR TEVAGEGFFV KIHRGIGWGE
IFKNLLTAKL PVLGAGQEWQ AIQRLHQVGV PTMTAVAYGE RGSNPAAQHS FIITEELAPT
ISLEDFSIDW VRQPPEPRLK RALIAEVAKM TGGMHRAGVN HRDCYICHFL LHTDRPVTAE
DFKLSVIDLH RAQTRAKISR RWRDKDLAAL YFSALDIGLT QRDKLRFLRG YFQRPLRQVL
KDEAALLAWL ERKAQKLYDR KQRYGDAL
//