ID   LPXK_CUPMC              Reviewed;         372 AA.
AC   Q1LR05;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Rmet_0535;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF07421.1; -; Genomic_DNA.
DR   RefSeq; WP_011515396.1; NC_007973.1.
DR   AlphaFoldDB; Q1LR05; -.
DR   SMR; Q1LR05; -.
DR   STRING; 266264.Rmet_0535; -.
DR   EnsemblBacteria; ABF07421; ABF07421; Rmet_0535.
DR   KEGG; rme:Rmet_0535; -.
DR   eggNOG; COG1663; Bacteria.
DR   HOGENOM; CLU_038816_2_0_4; -.
DR   OMA; MDDGFQN; -.
DR   OrthoDB; 1382484at2; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000002429; 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..372
FT                   /note="Tetraacyldisaccharide 4'-kinase"
FT                   /id="PRO_0000291230"
FT   REGION          351..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
SQ   SEQUENCE   372 AA;  40905 MW;  AC311D0376C7446C CRC64;
     MAAPQHTLAD FVTDQWQRRS WFTWLMWPLS LLFGLIARIR RYGYQQGWFK STRLPMPVIV
     VGNVTVGGTG KTPAVIALAH ALAEAGLRPG VVSRGYGVKL NHPRRVKPTS KAADVGDEPL
     LIARAADVPV WVFPDRALCT QAMLVSHPGV NVLLLDDGLQ HYKLQRDFEI VMFDTRMGGN
     GMMLPAGPLR EPLTRPRDAT LINDPNFRAT PDKPDVYGMR LELDEAWQLN DPTMSCDVSK
     FADKRVLAAA GIGHPERFFA SLRQAGLSPA TLPLPDHYDF VQDPFADNPA ALEADVILIT
     EKDAVKCERF DDPRIWVVPT TPVIDAGLID KIRRVVQARN PAIATPVTVG QSTATGMADG
     LDKEHQDGQP AA