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Database: UniProt
Entry: S8DBL5_9LAMI
LinkDB: S8DBL5_9LAMI
Original site: S8DBL5_9LAMI 
ID   S8DBL5_9LAMI            Unreviewed;       311 AA.
AC   S8DBL5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   13-SEP-2023, entry version 24.
DE   RecName: Full=tetraacyldisaccharide 4'-kinase {ECO:0000256|ARBA:ARBA00012071};
DE            EC=2.7.1.130 {ECO:0000256|ARBA:ARBA00012071};
DE   Flags: Fragment;
GN   ORFNames=M569_14666 {ECO:0000313|EMBL:EPS60138.1};
OS   Genlisea aurea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX   NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS60138.1, ECO:0000313|Proteomes:UP000015453};
RN   [1] {ECO:0000313|EMBL:EPS60138.1, ECO:0000313|Proteomes:UP000015453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23855885;
RA   Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA   Logacheva M.D.;
RT   "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT   number of genes and short non-coding sequences.";
RL   BMC Genomics 14:476-476(2013).
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:EPS60138.1}.
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DR   EMBL; AUSU01007791; EPS60138.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8DBL5; -.
DR   OrthoDB; 469548at2759; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000015453; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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};
KW   Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015453};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        24..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EPS60138.1"
FT   NON_TER         311
FT                   /evidence="ECO:0000313|EMBL:EPS60138.1"
SQ   SEQUENCE   311 AA;  34477 MW;  45C9A662C026EC82 CRC64;
     EGIRRAIKQI ASTPSSQSLS NLSYLQLSMI PLLSVISSIY SLAFRIRRQL YRFGLISTHR
     FPVPVISVGN ITWGGTGKTP MVEFLARSFA DFGICSLILT RGYGGGDEAR MLQRKLCGVS
     ARVGVGANRV ATASKFLEHY GYVNFPATTE EILSREEETH PDRIGLLILD DGMQHFSVVR
     DLEIVMVNSL MPWGNRKLLP AGPLREPPRA LSRADIIVFH HADLVEAKDI IALESEIREA
     DESAELFLTK MAALHFFASR DVSCKIPLTA VNNVVVLCLS AIGDADSFLL TIKKMGALYV
     DRIDFSDHHR F
//
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