ID   LPXK_FRANO              Reviewed;         322 AA.
AC   Q47909;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Tetraacyldisaccharide 4'-kinase;
DE            EC=2.7.1.130;
DE   AltName: Full=Lipid A 4'-kinase;
GN   Name=lpxK; Synonyms=valB;
OS   Francisella novicida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=U112;
RX   PubMed=7881549; DOI=10.1099/13500872-140-12-3309;
RA   Mdluli K.E., Anthony L.S., Baron G.S., McDonald M.K., Myltseva S.V.,
RA   Nano F.E.;
RT   "Serum-sensitive mutation of Francisella novicida: association with an ABC
RT   transporter gene.";
RL   Microbiology 140:3309-3318(1994).
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). {ECO:0000250}.
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;
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.
CC   -!- SIMILARITY: Belongs to the LpxK family. {ECO:0000305}.
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DR   EMBL; L17003; AAD15238.1; -; Genomic_DNA.
DR   RefSeq; WP_003041158.1; NZ_JACVMD010000017.1.
DR   AlphaFoldDB; Q47909; -.
DR   SMR; Q47909; -.
DR   STRING; 676032.FN3523_1669; -.
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   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; Transferase.
FT   CHAIN           1..322
FT                   /note="Tetraacyldisaccharide 4'-kinase"
FT                   /id="PRO_0000190926"
FT   BINDING         54..61
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   322 AA;  36145 MW;  4BFC964B1710CE05 CRC64;
     MLDKIWYRSK PNLLSRVLQP ISLVFIDIAN KRKIKQQLKQ YKSKIPIIVV GNISVGGTGK
     TPVVRMLAQQ YLAQGKKPAI ISRGYGAKAD NYPFEVTSGT LATQCGDEPA MLFDALQAQV
     PIVIAPERVQ AVKYIEKNFP DTDIIISDDG LQHYKLARDK EIVVVDAIRM FGNKLCLPAG
     PLREPIERLK EVDQIIVIGN CSDKDKELLK NYKNVTYAKV VATEFVNILT AKKVAKTEFN
     HQNVIAIAGI GNPTKFFKTL EESAINITAK KVFKDHHKFT QSDFEGIDSD ITVVMTYKDA
     IKCKNFAKAN WWYLDIALDI NV