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Database: UniProt
Entry: A0A0Q5YYF3_9BURK
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ID   A0A0Q5YYF3_9BURK        Unreviewed;       332 AA.
AC   A0A0Q5YYF3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
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   ORFNames=ASG30_08865 {ECO:0000313|EMBL:KQT10903.1};
OS   Ramlibacter sp. Leaf400.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT10903.1, ECO:0000313|Proteomes:UP000051173};
RN   [1] {ECO:0000313|EMBL:KQT10903.1, ECO:0000313|Proteomes:UP000051173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf400 {ECO:0000313|EMBL:KQT10903.1,
RC   ECO:0000313|Proteomes:UP000051173};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT10903.1, ECO:0000313|Proteomes:UP000051173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf400 {ECO:0000313|EMBL:KQT10903.1,
RC   ECO:0000313|Proteomes:UP000051173};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQT10903.1}.
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DR   EMBL; LMQL01000010; KQT10903.1; -; Genomic_DNA.
DR   RefSeq; WP_055897020.1; NZ_LMQL01000010.1.
DR   AlphaFoldDB; A0A0Q5YYF3; -.
DR   STRING; 1736365.ASG30_08865; -.
DR   OrthoDB; 9766423at2; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000051173; 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}; Reference proteome {ECO:0000313|Proteomes:UP000051173};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00409}.
FT   BINDING         58..65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00409"
SQ   SEQUENCE   332 AA;  36392 MW;  D0F4324E1E4286C8 CRC64;
     MREALQRAWL RRGPLARLLW PLCLPMRAAV RLRQWLYRRG SLASHKAPVP VVVIGNVVAG
     GAGKTPVVMA VAEHLVRTGL KVAVVSRGHG RTSTGCLEVT PGSDPAQSGD EPLLIATRCR
     VPVFVAERRF EAVQSALQAY PETDVVVSDD GLQHYAMARD VEVCVFDDRG LGNGWLLPAG
     PLREPWPRPA DLVLRTAGAE GLPGFVVRRR LSTTAWRADG KRVDLASFAH QDCDALAGIA
     RPQAFFDMLT AAGLRLDRTW ALDDHHDFAA DGPWLQGEPP LLCTEKDAVK LWRRNPRAWA
     VPLEVEIDDG FWTQLDSLLQ PKLSSAHGPQ TA
//
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