ID   LPXK_BACFR              Reviewed;         376 AA.
AC   Q64QN6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=BF3452;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD50195.1; -; Genomic_DNA.
DR   RefSeq; WP_009292736.1; NC_006347.1.
DR   RefSeq; YP_100729.1; NC_006347.1.
DR   AlphaFoldDB; Q64QN6; -.
DR   SMR; Q64QN6; -.
DR   STRING; 295405.BF3452; -.
DR   EnsemblBacteria; BAD50195; BAD50195; BF3452.
DR   KEGG; bfr:BF3452; -.
DR   PATRIC; fig|295405.11.peg.3317; -.
DR   HOGENOM; CLU_038816_6_0_10; -.
DR   OMA; MDDGFQN; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000002197; 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; Transferase.
FT   CHAIN           1..376
FT                   /note="Tetraacyldisaccharide 4'-kinase"
FT                   /id="PRO_0000340820"
FT   BINDING         51..58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
SQ   SEQUENCE   376 AA;  43166 MW;  7805B2FA3E42AC02 CRC64;
     MEENSIKIHK WLYPASWLYG AGVALRNKLF DWGKLQSKSF NVPIICIGNI AVGGTGKTPH
     TEYLIKLLHD EFQVAVLSRG YKRHTKGFVL STAESDARSI GDEPYQIQSK FSDIRVAVDE
     DRCHGIERLL TLKEPPVEVI LLDDAFQHRY VKAGLNILLT DYHRLFCDDT LMPAGRLRES
     AQGKNRAQIV IVTKCPPDIK PIDYNIITKR LNLFPYQQLY FSSFRYGNLR AVFPDCATVQ
     ERKLSSLQTE EQILLITGIA SPDTIIRELE IHTRNIDLLA FSDHHNFSQR DLAQIKERFG
     KLRKGQRLIV TTEKDATRLI CHQELDEGLK PFIYALPIEV EILQNQQDNF NQHIIGYVRE
     NTRNGSLPER KDAHKS