ID   LPXK_NITEU              Reviewed;         396 AA.
AC   Q82SY2;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Tetraacyldisaccharide 4'-kinase;
DE            EC=2.7.1.130;
DE   AltName: Full=Lipid A 4'-kinase;
GN   Name=lpxK; OrderedLocusNames=NE2164;
OS   Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS   14298).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=228410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX   PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA   Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA   Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA   Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT   "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT   chemolithoautotroph Nitrosomonas europaea.";
RL   J. Bacteriol. 185:2759-2773(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). {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}.
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DR   EMBL; AL954747; CAD86075.1; -; Genomic_DNA.
DR   RefSeq; WP_011112662.1; NC_004757.1.
DR   AlphaFoldDB; Q82SY2; -.
DR   SMR; Q82SY2; -.
DR   STRING; 228410.NE2164; -.
DR   EnsemblBacteria; CAD86075; CAD86075; NE2164.
DR   KEGG; neu:NE2164; -.
DR   eggNOG; COG1663; Bacteria.
DR   eggNOG; COG2835; Bacteria.
DR   HOGENOM; CLU_038816_2_0_4; -.
DR   OMA; MDDGFQN; -.
DR   OrthoDB; 1382484at2; -.
DR   PhylomeDB; Q82SY2; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000001416; 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; Reference proteome; Transferase.
FT   CHAIN           1..396
FT                   /note="Tetraacyldisaccharide 4'-kinase"
FT                   /id="PRO_0000291218"
FT   REGION          1..336
FT                   /note="Tetraacyldisaccharide 4'-kinase"
FT   REGION          337..396
FT                   /note="UPF0434"
SQ   SEQUENCE   396 AA;  45501 MW;  B5F5C9E708159C1C CRC64;
     MNWYELYWQR ITPLHLFLWP VSQLLILFQS VRRFLYRRAI LTSIHLPVPI IIIDSITTDS
     PVKTSLIIQI ANILKAAGLR PGIISRGYPD NHRPPTRVTI SSHPHLTGEK SLLLTYHLRE
     TCPVWIGYDR IETAKALLNA HKECNVLICD DGLQDLRLQR DFEAVIVDTS VINSGNGLIM
     PAGPLRDSFA RLKHTDAVIL AGHQRRIPDI TDEIRTIHTR PQKEHFFNLS WPELTADAAG
     LAGKRIHAIV CDPDTQNFLD NLEFLKLTVT PRVFPENHHF IATDFQSDEA EIILIPEEDA
     VKCLSLHDDR IWVLQQEYRV DPGLREIILK KLREKFMDPK LLDILVCPLC KGSLIYKKDR
     LELICKADRL AYPIRDGIPV MLEDEARKLP DEEEIK