ID W6M9E4_9GAMM Unreviewed; 385 AA.
AC W6M9E4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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:CDI04202.1};
GN ORFNames=BN873_890108 {ECO:0000313|EMBL:CDI04202.1};
OS Candidatus Competibacter denitrificans Run_A_D11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria;
OC Candidatus Competibacteraceae; Competibacter.
OX NCBI_TaxID=1400863 {ECO:0000313|EMBL:CDI04202.1, ECO:0000313|Proteomes:UP000035760};
RN [1] {ECO:0000313|EMBL:CDI04202.1, ECO:0000313|Proteomes:UP000035760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI04202.1,
RC ECO:0000313|Proteomes:UP000035760};
RA McIlroy S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDI04202.1, ECO:0000313|Proteomes:UP000035760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI04202.1,
RC ECO:0000313|Proteomes:UP000035760};
RA McIlroy S.J., Albertsen M., Andresen E.K., Saunders A.M., Kristiansen R.,
RA Stokholm-Bjerregaard M., Nielsen K.L., Nielsen P.H.;
RT "Candidatus Competibacter-lineage genomes retrieved from metagenomes reveal
RT functional metabolic diversity.";
RL Submitted (FEB-2014) 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:CDI04202.1}.
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DR EMBL; CBTJ020000101; CDI04202.1; -; Genomic_DNA.
DR AlphaFoldDB; W6M9E4; -.
DR STRING; 1400863.BN873_890108; -.
DR OrthoDB; 9766423at2; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000035760; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00409}; Reference proteome {ECO:0000313|Proteomes:UP000035760};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00409}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 334..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00409"
SQ SEQUENCE 385 AA; 42622 MW; 37B15DD58B1FC264 CRC64;
MQHWLDRYGY SLNGVAVLLW PISVLFGAVV RLRRWLYQHG LRRSESLRVP VIVVGNISVG
GTGKTPLVAR LVELLREAGY TPGIVSRGYG GHSTEWPRQV VADSDPMLVG DEPVLLARRC
RCAVVVGPDR VAAARLLVET YGCNLVVSDD GLQHYHLRRD IEIAVVDGFR RLGNAACLPA
GPLREPPSRL REVDFVVGNG AARGREYLMS LRGETAVNLE DPLITSTLAS FRQCTVHAVA
GIGDPWRFFD HLRHARLRLI EHPFPDHHPF KPEDLQFRED LPVLMTEKDA IKCRGITPAS
CWYVPVSAQL DPEFEDQLLK RVAMVAMAKG IRRRPETLPR RPRLAPLSEP LSGDEPDGQE
TAGDSGVPRQ QSTAGVRQGA SGIDL
//
