LPXK_CAMC1
ID LPXK_CAMC1 Reviewed; 306 AA.
AC A8Z6M1;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 58.
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=Ccon26_12660; ORFNames=CCC13826_2050;
OS Campylobacter concisus (strain 13826).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13826;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., On S., Nelson K.E.;
RT "Genome sequence of Campylobacter concisus 13826 isolated from human
RT feces.";
RL Submitted (OCT-2007) 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; CP000792; ABW74801.1; -; Genomic_DNA.
DR RefSeq; WP_048809842.1; NC_009802.2.
DR AlphaFoldDB; A8Z6M1; -.
DR SMR; A8Z6M1; -.
DR STRING; 360104.CCC13826_2050; -.
DR EnsemblBacteria; ABW74801; ABW74801; CCC13826_2050.
DR KEGG; cco:CCC13826_2050; -.
DR eggNOG; COG1663; Bacteria.
DR HOGENOM; CLU_038816_1_0_7; -.
DR OMA; YYPFCLP; -.
DR OrthoDB; 1382484at2; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000001121; 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..306
FT /note="Tetraacyldisaccharide 4'-kinase"
FT /id="PRO_0000340826"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
SQ SEQUENCE 306 AA; 34519 MW; 7875030416702ABC CRC64;
MFKKFNILLH SWANDYFFRP NFFQILLAFL LLPLSLIYTL VVVCKKFSAQ KKDFGIKIIS
VGNLTLGGSG KTPLCVAIAK NYGGAFIILR GYKRKSKGMQ VVARNGEILL DVAASGDEAM
IYATSIKNAN VIVSEDRKIA INYAKKHGAK YILLDDGFSK FDIAKFDILV RPNPEPKLRL
CLPSGAYRYP FSFYKFGNFI ACEGQTHFRK SEILNKTEKM VLVTAIANPA RLEAFFSECV
GQVFFPDHYD FSKEELSEIL QSYGATSLLM TQKDYVKVKD FGLRVSLITL EVTLSEEFKK
VLAKQI
