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Database: UniProt
Entry: B9BTA7_9BURK
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Original site: B9BTA7_9BURK 
ID   B9BTA7_9BURK            Unreviewed;       342 AA.
AC   B9BTA7;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Tetraacyldisaccharide 4'-kinase {ECO:0000256|ARBA:ARBA00016436, ECO:0000256|HAMAP-Rule:MF_00409};
DE            EC=2.7.1.130 {ECO:0000256|ARBA:ARBA00012071, ECO:0000256|HAMAP-Rule:MF_00409};
DE   AltName: Full=Lipid A 4'-kinase {ECO:0000256|ARBA:ARBA00029757, ECO:0000256|HAMAP-Rule:MF_00409};
GN   Name=lpxK {ECO:0000256|HAMAP-Rule:MF_00409,
GN   ECO:0000313|EMBL:EEE05675.1};
GN   ORFNames=BURMUCGD2_0912 {ECO:0000313|EMBL:EEE05675.1};
OS   Burkholderia multivorans CGD2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=513052 {ECO:0000313|EMBL:EEE05675.1, ECO:0000313|Proteomes:UP000004535};
RN   [1] {ECO:0000313|EMBL:EEE05675.1, ECO:0000313|Proteomes:UP000004535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGD2 {ECO:0000313|EMBL:EEE05675.1,
RC   ECO:0000313|Proteomes:UP000004535};
RX   PubMed=23105085; DOI=10.1128/JB.01306-12;
RA   Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., Radune D.,
RA   Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., Greenberg D.E.,
RA   Holland S.M., Goldberg J.B.;
RT   "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic
RT   Granulomatous Disease Burkholderia multivorans Isolates.";
RL   J. Bacteriol. 194:6356-6357(2012).
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:0000256|ARBA:ARBA00002274, ECO:0000256|HAMAP-Rule:MF_00409}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+);
CC         Xref=Rhea:RHEA:67840, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:176343, ChEBI:CHEBI:176425, ChEBI:CHEBI:456216;
CC         EC=2.7.1.130; Evidence={ECO:0000256|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:0000256|ARBA:ARBA00004870,
CC       ECO:0000256|HAMAP-Rule:MF_00409}.
CC   -!- SIMILARITY: Belongs to the LpxK family. {ECO:0000256|HAMAP-
CC       Rule:MF_00409}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEE05675.1}.
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DR   EMBL; ACFC01000008; EEE05675.1; -; Genomic_DNA.
DR   RefSeq; WP_006406418.1; NZ_ACFC01000008.1.
DR   AlphaFoldDB; B9BTA7; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000004535; Unassembled WGS sequence.
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   NCBIfam; TIGR00682; lpxK; 1.
DR   PANTHER; PTHR42724; TETRAACYLDISACCHARIDE 4'-KINASE; 1.
DR   PANTHER; PTHR42724:SF1; TETRAACYLDISACCHARIDE 4'-KINASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02606; LpxK; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00409};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00409};
KW   Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP-
KW   Rule:MF_00409};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_00409};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_00409};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00409};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00409}.
FT   BINDING         68..75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00409"
SQ   SEQUENCE   342 AA;  36371 MW;  6C4798E5C3C3109D CRC64;
     MSAADGLLAR LETRVTREWQ RRGAFAWALT PFACAFGLCA ALRRTAYARG WKQAVDVGVP
     VVVVGNVTVG GTGKTPTVIA LVDALRAAGF TPGVVSRGYG ANVKTPTAVT PASRAGTAGD
     EPLLIARRTG APVWVCPDRV AAAQALRAAH PDVDVIVSDD GLQHYRLART VELVVFDHRL
     GGNGFLLPAG PLREPLSRHR DATLVNDPYS GALPPWPDTY SLALTPGAAW HLDQPTLRRP
     LSQFADERVL AAAGIGAPER FFATLRAAGL APATRALPDH YAFADNPFVD DAVDAILITE
     KDAVKLGASW RDARLWVVPV EAALDPRLIA LVVEKLRGRS PA
//
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