ID   LPXK_NITEC              Reviewed;         396 AA.
AC   Q0AEA0;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Tetraacyldisaccharide 4'-kinase;
DE            EC=2.7.1.130;
DE   AltName: Full=Lipid A 4'-kinase;
GN   Name=lpxK; OrderedLocusNames=Neut_2110;
OS   Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=335283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 101675 / C91 / Nm57;
RX   PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA   Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA   Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.;
RT   "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas
RT   eutropha C91: implications for niche adaptation.";
RL   Environ. Microbiol. 9:2993-3007(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). {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: In the N-terminal section; belongs to the LpxK family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the UPF0434 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved motif Gly-Gly-x-Gly-Lys-Thr that is the
CC       consensus ATP-binding site for this enzyme. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000450; ABI60332.1; -; Genomic_DNA.
DR   RefSeq; WP_011635129.1; NC_008344.1.
DR   AlphaFoldDB; Q0AEA0; -.
DR   SMR; Q0AEA0; -.
DR   STRING; 335283.Neut_2110; -.
DR   EnsemblBacteria; ABI60332; ABI60332; Neut_2110.
DR   KEGG; net:Neut_2110; -.
DR   eggNOG; COG1663; Bacteria.
DR   eggNOG; COG2835; Bacteria.
DR   HOGENOM; CLU_038816_2_0_4; -.
DR   OMA; MDDGFQN; -.
DR   OrthoDB; 1382484at2; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000001966; 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   HAMAP; MF_01187; UPF0434; 1.
DR   InterPro; IPR003758; LpxK.
DR   InterPro; IPR005651; Trm112-like.
DR   PANTHER; PTHR42724; PTHR42724; 1.
DR   Pfam; PF02606; LpxK; 1.
DR   Pfam; PF03966; Trm112p; 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..396
FT                   /note="Tetraacyldisaccharide 4'-kinase"
FT                   /id="PRO_0000291219"
FT   REGION          1..336
FT                   /note="Tetraacyldisaccharide 4'-kinase"
FT   REGION          337..396
FT                   /note="UPF0434"
SQ   SEQUENCE   396 AA;  45510 MW;  BA7ED74C37D35FD5 CRC64;
     MNWSELYWQR ITPLHLLLWP VSLLFVLFQS IRRHLYRRAI LTSVHLPVPV IVVDSITATS
     PVKTPLIIQI VNMLRASGLR PGIIGHGYTD NYHSPMSVTI DSPLQLAGKK SLLLAYYLRE
     TCPVWIGHDR IEVAKALLET HKECNVLICN DGLQDLRLQR DFEVVIVDTS VINSGNGLIM
     PAGPLRDSFA RLKHSNVVVQ AGHHRQIPDI GEEIRTFYIT PLKEHFFNLS RPELTASAAE
     LANKRIHAVT CDPDIQNFLD NLKFLRLTVT PYIFSEDHHF VAEDFPFDEA EIILIPEEDA
     VKCFNLHDER IWVLQQEYRV DLGLRTIILK KLREKFMDPK LLDILACPLC KGPLIYKKDR
     LELICKADRL AYPIRDGIPV MLEDEARRLP DEEEIK