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Database: UniProt
Entry: G5NAZ0_SALET
LinkDB: G5NAZ0_SALET
Original site: G5NAZ0_SALET 
ID   G5NAZ0_SALET            Unreviewed;        81 AA.
AC   G5NAZ0;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Tetraacyldisaccharide 4'-kinase {ECO:0000256|ARBA:ARBA00016436};
DE            EC=2.7.1.130 {ECO:0000256|ARBA:ARBA00012071};
DE   AltName: Full=Lipid A 4'-kinase {ECO:0000256|ARBA:ARBA00029757};
DE   Flags: Fragment;
GN   ORFNames=LTSEINV_1653 {ECO:0000313|EMBL:EHC59867.1};
OS   Salmonella enterica subsp. enterica serovar Inverness str. R8-3668.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913075 {ECO:0000313|EMBL:EHC59867.1, ECO:0000313|Proteomes:UP000003532};
RN   [1] {ECO:0000313|EMBL:EHC59867.1, ECO:0000313|Proteomes:UP000003532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R8-3668 {ECO:0000313|EMBL:EHC59867.1,
RC   ECO:0000313|Proteomes:UP000003532};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(2011).
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}.
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   -!- 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:EHC59867.1}.
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DR   EMBL; AFCO01000570; EHC59867.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5NAZ0; -.
DR   PATRIC; fig|913075.3.peg.1258; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000003532; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009029; F:tetraacyldisaccharide 4'-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR003758; LpxK.
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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EHC59867.1};
KW   Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EHC59867.1"
SQ   SEQUENCE   81 AA;  8776 MW;  8BDB2457C03ACEF5 CRC64;
     KAILAAHNVQ IIITDDGLQH YRLARDIEIV VIDGVRRFGN GWWLPAGPMR ERASRLKTVD
     AAIVNGGVAR AGEGRAKSPC S
//
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