ID   LPXK_CAMJ8              Reviewed;         308 AA.
AC   A8FLM4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-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}; OrderedLocusNames=C8J_0762;
OS   Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
OS   11828).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=407148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81116 / NCTC 11828;
RX   PubMed=17873037; DOI=10.1128/jb.01404-07;
RA   Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M.,
RA   van Vliet A.H.M.;
RT   "The complete genome sequence of Campylobacter jejuni strain 81116
RT   (NCTC11828).";
RL   J. Bacteriol. 189:8402-8403(2007).
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}.
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DR   EMBL; CP000814; ABV52361.1; -; Genomic_DNA.
DR   RefSeq; WP_002865989.1; NC_009839.1.
DR   AlphaFoldDB; A8FLM4; -.
DR   SMR; A8FLM4; -.
DR   KEGG; cju:C8J_0762; -.
DR   HOGENOM; CLU_038816_1_0_7; -.
DR   OMA; YYPFCLP; -.
DR   UniPathway; UPA00359; UER00482.
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; 2.
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_1000072275"
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;  36235 MW;  A1237FEAC96229D0 CRC64;
     MSEEKNYELW LDNYFFKPNF WQKCLAFILL PLSVFYAFFA ILNTFFRKKI VFKKPVISVG
     NLSFGGNGKT PLCKAIAREF DGVFIVLRGY KRKSKGLFVV KNQNEILCTL TQSGDEAMEY
     AFEENIKGVI VSEDRVKGIE KAFELGAKIV VLDDAFSKFH IKKFDILLES KIKPYFNFTL
     PSGAYRLPKF YEKRADFIAL EGRDFVRYSF VKENPKAVLV TAIAKPFRLY EHFIKARACY
     FFKDHYEFKK EELENLLKKH NCDTLMLTFK DFVKVKDFGF KCQIIELNIE LKDSLREKIK
     TYIKEFEQ