LPXK_HELAH
ID LPXK_HELAH Reviewed; 312 AA.
AC Q17X64;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Hac_0992;
OS Helicobacter acinonychis (strain Sheeba).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=382638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheeba;
RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA Gressmann H., Achtman M., Schuster S.C.;
RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT host jump from early humans to large felines.";
RL PLoS Genet. 2:1097-1110(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; AM260522; CAJ99762.1; -; Genomic_DNA.
DR RefSeq; WP_011577872.1; NC_008229.1.
DR AlphaFoldDB; Q17X64; -.
DR SMR; Q17X64; -.
DR STRING; 382638.Hac_0992; -.
DR EnsemblBacteria; CAJ99762; CAJ99762; Hac_0992.
DR KEGG; hac:Hac_0992; -.
DR eggNOG; COG1663; Bacteria.
DR HOGENOM; CLU_038816_1_0_7; -.
DR OMA; YYPFCLP; -.
DR OrthoDB; 1382484at2; -.
DR BioCyc; HACI382638:HAC_RS04265-MON; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000000775; 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.
DR TIGRFAMs; TIGR00682; 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_0000291209"
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; 35654 MW; 6F59F229035EA80D CRC64;
MKSDKPFLER YFYTPTLLQK GLIFALYPFS LIYQCIATFK RKTAKKHDFK IPIISVGNLI
AGGSGKTPFI LEIAPRYQEV AIISRGYQRN SKGLVVVSVK GKILVSQNTA GDEAYLLALN
LKQASVIVSE KRELGILKAL ELGSKIVFLD DGFRFNFNQF NLLLKPKVPP YYPFCLPSGL
YRESIKSYKE AHLVITEDKD YKRITSTTHP TKRMLLVTAI ANPSRLNAFL PKEVVKKIYF
KDHAPFNLKL LEKEFHKNNA TSLLVTSKDL VKLQDCKLPL SVLDLRLEID PKVLEKIDNY
IFSYPYNTKE HL
