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LPXK_BRUAB
ID   LPXK_BRUAB              Reviewed;         341 AA.
AC   Q579M9;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=BruAb2_0212;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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; AE017224; AAX75655.1; -; Genomic_DNA.
DR   RefSeq; WP_002966366.1; NC_006933.1.
DR   AlphaFoldDB; Q579M9; -.
DR   SMR; Q579M9; -.
DR   EnsemblBacteria; AAX75655; AAX75655; BruAb2_0212.
DR   GeneID; 45053292; -.
DR   GeneID; 55591930; -.
DR   KEGG; bmb:BruAb2_0212; -.
DR   HOGENOM; CLU_038816_0_0_5; -.
DR   OMA; MDDGFQN; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000000540; Chromosome II.
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..341
FT                   /note="Tetraacyldisaccharide 4'-kinase"
FT                   /id="PRO_0000229945"
FT   BINDING         54..61
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
SQ   SEQUENCE   341 AA;  36782 MW;  93014F0F6B7C3DCE CRC64;
     MASEAPPFWW DEPDWRALAL APAAWIYGRV SGRRLIRAVP PRVSLPVLCV GNFTVGGAGK
     TPTAIAFARG AIARGMKPGI VSRGYGGNYS GLHLVDPGHD GARHVGDEPL LLARHAAVAL
     SPDRVKAAEY LKSLGCDFII MDDGFQSARL HADFSLLVVD ASRGIGNGRV IPAGPLRAPL
     TDQMRKTDAL LCIGKGNGAD FVIRQAARAG RPIYHAQLRP SSSATVAGRR WLAFAGIGNP
     DKFYESVRQA GGEVVETHSF ADHYSFEPDD IRGLVDMARR QGLGLITTAK DHVRLATMPG
     VPPEFLSKLA VLDVDLEFDR TDALDHILDT VVERFKSRLH G
 
 
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