ID   LPXK_GEOSL              Reviewed;         353 AA.
AC   Q74AU2;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=GSU2258;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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; AE017180; AAR35634.1; -; Genomic_DNA.
DR   RefSeq; NP_953307.1; NC_002939.5.
DR   RefSeq; WP_010942898.1; NC_002939.5.
DR   AlphaFoldDB; Q74AU2; -.
DR   SMR; Q74AU2; -.
DR   STRING; 243231.GSU2258; -.
DR   EnsemblBacteria; AAR35634; AAR35634; GSU2258.
DR   KEGG; gsu:GSU2258; -.
DR   PATRIC; fig|243231.5.peg.2289; -.
DR   eggNOG; COG1663; Bacteria.
DR   HOGENOM; CLU_038816_6_0_7; -.
DR   InParanoid; Q74AU2; -.
DR   OMA; MDDGFQN; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000000577; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009029; F:tetraacyldisaccharide 4'-kinase activity; IBA:GO_Central.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IBA:GO_Central.
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..353
FT                   /note="Tetraacyldisaccharide 4'-kinase"
FT                   /id="PRO_0000190927"
FT   BINDING         66..73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
SQ   SEQUENCE   353 AA;  37248 MW;  EB01D8DB0CFFF7DB CRC64;
     MSCTGFWRKL ASGEECGAAA RLLGAVLAIP AALYGLVVRL RALAYARGLS TVRHLDRPVI
     SVGNLTVGGT GKTPMVAYLA RRLMARGKRV AVISRGYGGS LEGETRIVSD GRTIVLSAAE
     AGDEPVHLAT SVPGLMTVIG TDRYTAGLLA LEQLDPDVFI LDDGYQHLRL HRDLNILLMD
     CNRPLGNGRT LPAGLLREPQ TAVRRADLVV YTRCTGGKAP AVHGMIPSCR AGHALTGAAL
     LPDGEVQPLA ALRGLRGVAC AGIAEPEGFF DALRREGLDI VAAIPFADHA SYGEREVSTL
     REAAAGADYL ITTGKDGVKL SAHLARLLPV YATVLEMRPL DPAPLEAALD KVL