ID LPXK_ECODH Reviewed; 328 AA.
AC B1X855;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
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=ECDH10B_0985;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
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=a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+);
CC Xref=Rhea:RHEA:67840, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:176343, ChEBI:CHEBI:176425, ChEBI:CHEBI:456216;
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; CP000948; ACB02115.1; -; Genomic_DNA.
DR RefSeq; WP_000570544.1; NC_010473.1.
DR AlphaFoldDB; B1X855; -.
DR SMR; B1X855; -.
DR KEGG; ecd:ECDH10B_0985; -.
DR HOGENOM; CLU_038816_2_0_6; -.
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 InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00682; lpxK; 1.
DR PANTHER; PTHR42724; TETRAACYLDISACCHARIDE 4'-KINASE; 1.
DR PANTHER; PTHR42724:SF1; TETRAACYLDISACCHARIDE 4'-KINASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02606; LpxK; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Nucleotide-binding; Transferase.
FT CHAIN 1..328
FT /note="Tetraacyldisaccharide 4'-kinase"
FT /id="PRO_1000123708"
FT BINDING 55..62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
SQ SEQUENCE 328 AA; 35588 MW; B4D2476F3833F2DF CRC64;
MIEKIWSGES PLWRLLLPLS WLYGLVSGAI RLCYKLKLKR AWRAPVPVVV VGNLTAGGNG
KTPVVVWLVE QLQQRGIRVG VVSRGYGGKA ESYPLLLSAD TTTAQAGDEP VLIYQRTDAP
VAVSPVRSDA VKAILAQHPD VQIIVTDDGL QHYRLARNVE IVVIDGVRRF GNGWWLPAGP
MRERAGRLKS VDAVIVNGGV PRSGEIPMHL LPGQAVNLRT GTRCDVAQLE HVVAMAGIGH
PPRFFATLKM CGVQPEKCVP LADHQSLNHA DVSALVSAGQ TLVMTEKDAV KCRAFAEENW
WYLPVDAQLS GDEPAKLLTQ LTLLASGN
//
