ID E1KQL5_9BACT Unreviewed; 395 AA.
AC E1KQL5;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Tetraacyldisaccharide 4'-kinase {ECO:0000256|ARBA:ARBA00016436, ECO:0000256|HAMAP-Rule:MF_00409};
DE EC=2.7.1.130 {ECO:0000256|ARBA:ARBA00012071, ECO:0000256|HAMAP-Rule:MF_00409};
DE AltName: Full=Lipid A 4'-kinase {ECO:0000256|ARBA:ARBA00029757, ECO:0000256|HAMAP-Rule:MF_00409};
GN Name=lpxK {ECO:0000256|HAMAP-Rule:MF_00409,
GN ECO:0000313|EMBL:EFL46225.1};
GN ORFNames=HMPREF9296_0982 {ECO:0000313|EMBL:EFL46225.1};
OS Prevotella disiens FB035-09AN.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=866771 {ECO:0000313|EMBL:EFL46225.1, ECO:0000313|Proteomes:UP000003610};
RN [1] {ECO:0000313|EMBL:EFL46225.1, ECO:0000313|Proteomes:UP000003610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB035-09AN {ECO:0000313|EMBL:EFL46225.1,
RC ECO:0000313|Proteomes:UP000003610};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) 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:0000256|ARBA:ARBA00002274, ECO:0000256|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:0000256|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:0000256|ARBA:ARBA00004870,
CC ECO:0000256|HAMAP-Rule:MF_00409}.
CC -!- SIMILARITY: Belongs to the LpxK family. {ECO:0000256|HAMAP-
CC Rule:MF_00409}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFL46225.1}.
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; AEDO01000034; EFL46225.1; -; Genomic_DNA.
DR RefSeq; WP_004356437.1; NZ_AEDO01000034.1.
DR AlphaFoldDB; E1KQL5; -.
DR STRING; 866771.HMPREF9296_0982; -.
DR eggNOG; COG1663; Bacteria.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000003610; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00409};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00409};
KW Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP-
KW Rule:MF_00409};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00409};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00409};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00409};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00409}.
FT REGION 368..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00409"
SQ SEQUENCE 395 AA; 45373 MW; EAF78B71909879F8 CRC64;
MEGDFIKLHK CLLPLSWLYG LGVGLRNELF ELGVLKSRSF DVPVISVGNI TVGGSGKTPH
VEYLIRLLKD IAQVAVLSRG YKRKSKGYVL AEEDTPMEMI GDEPFQMKHK FPNIHVAVDK
KRCEGIDHLV DDEETKNTDV VLLDDAFQHR YVKPGINILL VDYHRLIIYD KLLPVGRLRE
PLSGKNRADI VIVTKCPKEL NPIDYRVLSK AMNLYPFQDL YFTTFEYCNL IPVFEEAKEK
EIALSDIHKT NVLLLSGIAL PKQLEVDLKP YTEGTKVETL EFPDHHSFKK KDVELINSMF
EAMETPKIII TTEKDKARLL NLENLNDEVK QNIYALPIKV KFMLNKEEKF NEKIISYVRK
NSRNSILVKG KDDNKSKDSN HSGNRARTIS FRDNR
//
