ID   LPXK_PARD8              Reviewed;         369 AA.
AC   A6LIV7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=BDI_3942;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR45621.1; -; Genomic_DNA.
DR   RefSeq; WP_012056234.1; NC_009615.1.
DR   AlphaFoldDB; A6LIV7; -.
DR   SMR; A6LIV7; -.
DR   STRING; 435591.BDI_3942; -.
DR   EnsemblBacteria; ABR45621; ABR45621; BDI_3942.
DR   KEGG; pdi:BDI_3942; -.
DR   PATRIC; fig|435591.13.peg.3892; -.
DR   eggNOG; COG1663; Bacteria.
DR   HOGENOM; CLU_038816_6_0_10; -.
DR   OMA; MDDGFQN; -.
DR   OrthoDB; 1382484at2; -.
DR   BioCyc; PDIS435591:G1G5A-4053-MON; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000000566; 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   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR42724; PTHR42724; 1.
DR   Pfam; PF02606; LpxK; 1.
DR   SUPFAM; SSF52540; SSF52540; 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; Reference proteome; Transferase.
FT   CHAIN           1..369
FT                   /note="Tetraacyldisaccharide 4'-kinase"
FT                   /id="PRO_0000340843"
FT   BINDING         52..59
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
SQ   SEQUENCE   369 AA;  42738 MW;  2147CE5CF3EFC8CD CRC64;
     MLTDHTIKFN KLLTPFSFLY GIGVRFRNQL FDWKVLRTER YDLPIICVGN LTVGGTGKTP
     HTEYIIRLIK DRYRVAVLSR GYKRKTSGFL LADQRSTSKD IGDEPYQMKR KFPDILVAVD
     ADRRRGIRNL LALPENKRPD VIVLDDAFQH RYVAPTLNIL LTDCHRLYTQ DRLLPAGRLR
     EPMDGARRAD VIIVTKCESC IQPIDFRIIE EDIHLSAYQE LYFSRILYGE LEPVFSGKAP
     RRTLKGLAST TEVLLVSGIA SPAPLEKEIH KYTEHVTSLI FPDHHAFDRH DIQKIQTAFK
     RLTSTSKLII ITEKDAARLR DLPSLPMEWF SHLYCLPITV GFCMDREKQF QELIVKHIDT
     RIKNHPILR