ID A0A0A2E6V4_9PORP Unreviewed; 367 AA.
AC A0A0A2E6V4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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 ORFNames=HQ37_00840 {ECO:0000313|EMBL:KGN72189.1};
OS Porphyromonas sp. COT-239 OH1446.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1515613 {ECO:0000313|EMBL:KGN72189.1, ECO:0000313|Proteomes:UP000030150};
RN [1] {ECO:0000313|EMBL:KGN72189.1, ECO:0000313|Proteomes:UP000030150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-239 OH1446 {ECO:0000313|Proteomes:UP000030150};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas sp. COT-239_OH1446 Genome sequencing.";
RL Submitted (AUG-2014) 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:KGN72189.1}.
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DR EMBL; JRAO01000003; KGN72189.1; -; Genomic_DNA.
DR RefSeq; WP_036878904.1; NZ_JRAO01000003.1.
DR AlphaFoldDB; A0A0A2E6V4; -.
DR STRING; 1515613.HQ37_00840; -.
DR eggNOG; COG1663; Bacteria.
DR OrthoDB; 9766423at2; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000030150; 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}; Reference proteome {ECO:0000313|Proteomes:UP000030150};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00409}.
FT BINDING 51..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00409"
SQ SEQUENCE 367 AA; 41713 MW; 0C4232DD486CF772 CRC64;
MPYSSNPYRA LLRPLSVLYG WGVALRHFCF DRGILPQVSY PIPVICVGNI IAGGTGKTPH
VEYLIRLLGE RRRVALISRG YKRKSRGMII ASSSSSVADI GDEPKQILTK YPNIRLVVDG
NRRRAMAYFM SLPEDERPEV VIMDDGYQHR YVRPSFSILL IDAARHPKDD HLLPEGLLRE
PLEQIHRADC VIISKCPANM SSIERRIIDR GLRLYPHQQL FFSRMQPKAL CPVLSLGTET
AQGRGSAPML GDRVMALAGI AQGEAFVRQL SQSYSVVQSY CFADHHNYRG EDLARLEQAF
AELSAEQADK PLWCICTEKD AVRLYEHRSL LSSALLEHLY YQPIEVKLLQ RQEVFDRLIL
SKARPLR
//
