LPXK_HELPH
ID LPXK_HELPH Reviewed; 312 AA.
AC Q1CUH3;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=HPAG1_0332;
OS Helicobacter pylori (strain HPAG1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=357544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPAG1;
RX PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA Gordon J.I.;
RT "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT pylori strain: evolution during disease progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006).
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; CP000241; ABF84399.1; -; Genomic_DNA.
DR RefSeq; WP_000833918.1; NC_008086.1.
DR AlphaFoldDB; Q1CUH3; -.
DR SMR; Q1CUH3; -.
DR PRIDE; Q1CUH3; -.
DR EnsemblBacteria; ABF84399; ABF84399; HPAG1_0332.
DR KEGG; hpa:HPAG1_0332; -.
DR HOGENOM; CLU_038816_1_0_7; -.
DR OMA; YYPFCLP; -.
DR OrthoDB; 1382484at2; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000008835; 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..312
FT /note="Tetraacyldisaccharide 4'-kinase"
FT /id="PRO_0000291210"
FT BINDING 60..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
SQ SEQUENCE 312 AA; 35468 MW; 3402E26605E7FCC2 CRC64;
MKSDKPFLER YFYDPTLLQK GLIFALYPFS LIYQGIATIK RKTAKKHDFK IPLISIGNLI
AGGSGKTPFI LEIAPRYQEV AIVSRGYQRD SKGLVVVSVK GNILVPQQTA GDEAYLLALN
LKQASVIVSE KRELGVLKAL ELGAKIVFLD DGFRFNFNQF NALLKPKIPP YYPFCLPSGL
YRESIKSYKE AHLVITEDKD YQRITSISHP TKRMLLVTAI ANPSRLDAFL PKEVVKKLYF
KDHALFDLKL LEKEFYQNSA TSLLVTSKDL VKLQDCSLPL SVLDLKLEID PKILEKIDRY
ILSYPCNTKE RL
