ID   LPXK_CAMJJ              Reviewed;         308 AA.
AC   A1VZF9;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Tetraacyldisaccharide 4'-kinase {ECO:0000255|HAMAP-Rule:MF_00409};
DE            EC=2.7.1.130 {ECO:0000255|HAMAP-Rule:MF_00409};
DE   AltName: Full=Lipid A 4'-kinase {ECO:0000255|HAMAP-Rule:MF_00409};
GN   Name=lpxK {ECO:0000255|HAMAP-Rule:MF_00409};
GN   OrderedLocusNames=CJJ81176_0832;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfers the gamma-phosphate of ATP to the 4'-position of a
CC       tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form
CC       tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
CC       {ECO:0000255|HAMAP-Rule:MF_00409}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + {2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-
CC         glucosaminyl}-(1->6)-{2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-
CC         D-glucosaminyl phosphate} = ADP + {2-N,3-O-bis[(3R)-3-
CC         hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl}-(1->6)-{2-N,3-
CC         O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate}.;
CC         EC=2.7.1.130; Evidence={ECO:0000255|HAMAP-Rule:MF_00409};
CC   -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC       from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC       acetyl-alpha-D-glucosamine: step 6/6. {ECO:0000255|HAMAP-
CC       Rule:MF_00409}.
CC   -!- SIMILARITY: Belongs to the LpxK family. {ECO:0000255|HAMAP-
CC       Rule:MF_00409}.
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; CP000538; EAQ72377.1; -; Genomic_DNA.
DR   RefSeq; WP_011812737.1; NC_008787.1.
DR   AlphaFoldDB; A1VZF9; -.
DR   SMR; A1VZF9; -.
DR   STRING; 354242.CJJ81176_0832; -.
DR   EnsemblBacteria; EAQ72377; EAQ72377; CJJ81176_0832.
DR   KEGG; cjj:CJJ81176_0832; -.
DR   eggNOG; COG1663; Bacteria.
DR   HOGENOM; CLU_038816_1_0_7; -.
DR   OMA; YYPFCLP; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000000646; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009029; F:tetraacyldisaccharide 4'-kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   HAMAP; MF_00409; LpxK; 1.
DR   InterPro; IPR003758; LpxK.
DR   PANTHER; PTHR42724; PTHR42724; 2.
DR   Pfam; PF02606; LpxK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Nucleotide-binding; Transferase.
FT   CHAIN           1..308
FT                   /note="Tetraacyldisaccharide 4'-kinase"
FT                   /id="PRO_0000291202"
FT   BINDING         63..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
SQ   SEQUENCE   308 AA;  36186 MW;  11A0F0B734D0531F CRC64;
     MSEEKNYELW LDNYFFKPNF WQKCLTFVLF PLSVLYAFFA ILNTFFRKKI VFKKPVISVG
     NLSFGGNGKT PLCKAIAREF DGVFIVLRGY KRKSKGLFVV KNQNEILCTL AQSGDEAMEY
     AFEENIKGVI VSEDRVKGIE KAFELGAKIV VLDDAFSKFH IKKFDILLES KIKPYFNFTL
     PSGAYRLPKI YEKRADFIAL EGRDFVRYSF VKENPKAVLV TAIAKPFRLY EHFIKARACY
     FFKDHYEFKK EELENLLKKH NCDTLMLTFK DFVKVKDFGF KCQIIELNIE LKDSLREKIK
     TYIKEFEQ