GenomeNet

Database: UniProt
Entry: T2SV48_HELPX
LinkDB: T2SV48_HELPX
Original site: T2SV48_HELPX 
ID   T2SV48_HELPX            Unreviewed;       312 AA.
AC   T2SV48;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=L930_08335 {ECO:0000313|EMBL:EQD96507.1};
OS   Helicobacter pylori PZ5004.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1337390 {ECO:0000313|EMBL:EQD96507.1, ECO:0000313|Proteomes:UP000015894};
RN   [1] {ECO:0000313|EMBL:EQD96507.1, ECO:0000313|Proteomes:UP000015894}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PZ5004 {ECO:0000313|EMBL:EQD96507.1,
RC   ECO:0000313|Proteomes:UP000015894};
RX   PubMed=24051318;
RA   Sheh A., Piazuelo M.B., Wilson K.T., Correa P., Fox J.G.;
RT   "Draft Genome Sequences of Helicobacter pylori Strains Isolated from
RT   Regions of Low and High Gastric Cancer Risk in Colombia.";
RL   Genome Announc. 1:e00736-13(2013).
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:EQD96507.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ASZF01000241; EQD96507.1; -; Genomic_DNA.
DR   AlphaFoldDB; T2SV48; -.
DR   PATRIC; fig|1337390.3.peg.1455; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000015894; 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   PANTHER; PTHR42724; TETRAACYLDISACCHARIDE 4'-KINASE; 1.
DR   PANTHER; PTHR42724:SF1; TETRAACYLDISACCHARIDE 4'-KINASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02606; LpxK; 2.
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};
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        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         60..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00409"
SQ   SEQUENCE   312 AA;  35438 MW;  04FE620190B8B283 CRC64;
     MKSDKPFLER YFYDPTLLQK GLIFALYPFS LIYQGIATLK RKTAKKHDFK IPIISIGNLI
     AGGSGKTPFI LEIAPRYQEV AVVSRGYQRD SKGLVVVSVK GNILVPQKTA GDEAYLLALN
     LKQASVIVSE KRELGVLKAL ELGAKIVFLD DGFRFNFNQF NALLKPKVPP YYPFCLPSGL
     YRESVNSYKE AHLVVTEDKD YKRITSIAHP TKRMLLVTAI ANPSRLDAFL PKEVVKKLYF
     RDHAPFDLEL LEKEFYQNNA TSLLVTSKDL VKLQDCKLPL SVLDLKLEIC PKVLEEIDRY
     ILSYPCNTKE RL
//
DBGET integrated database retrieval system