LPXK_BURTA
ID LPXK_BURTA Reviewed; 342 AA.
AC Q2T0K1;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 74.
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=BTH_I0742;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABC38937.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000086; ABC38937.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_025369540.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2T0K1; -.
DR SMR; Q2T0K1; -.
DR PRIDE; Q2T0K1; -.
DR EnsemblBacteria; ABC38937; ABC38937; BTH_I0742.
DR GeneID; 66546277; -.
DR KEGG; bte:BTH_I0742; -.
DR HOGENOM; CLU_038816_2_0_4; -.
DR OrthoDB; 1382484at2; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000001930; Chromosome I.
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; 2.
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..342
FT /note="Tetraacyldisaccharide 4'-kinase"
FT /id="PRO_0000291200"
FT BINDING 68..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
SQ SEQUENCE 342 AA; 36555 MW; B246FBC953517A98 CRC64;
MSARPGLLAR AEARLTREWQ RRGALAWALT PFACAFGAIA ALRRAAYARG WKARVDCGVP
VVVVGNVTVG GTGKTPTVIA LVDALRAAGF TPGVVSRGYG AKIVAPTAVT PASAPQQAGD
EPLLIARRTL APVWVCPDRV AAVRALKAAH PEVDVVVSDD GLQHYRLARA VEIVVFDHRL
GGNGFLLPAG PLREPLSRRR DATLVNDPYS RALPPWPDTF ALSLAPGDAW HLARPSRRKP
LAQFAGERVL AAAGIGAPER FFATLRAAGV TPATRALPDH YAFATNPFVD DHFDAILITE
KDAVKLGTSW RDARIWVVPV EAALDPRLIA LVVEKLRGRT SA