ID A0A0R2RLV9_9PROT Unreviewed; 295 AA.
AC A0A0R2RLV9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=ABS03_04015 {ECO:0000313|EMBL:KRO63716.1};
OS Pelagibacteraceae bacterium BACL5 MAG-120820-bin39.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=1655605 {ECO:0000313|EMBL:KRO63716.1, ECO:0000313|Proteomes:UP000051468};
RN [1] {ECO:0000313|EMBL:KRO63716.1, ECO:0000313|Proteomes:UP000051468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL5 MAG-120820-bin39 {ECO:0000313|EMBL:KRO63716.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-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}.
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:KRO63716.1}.
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DR EMBL; LIBV01000139; KRO63716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2RLV9; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000051468; 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 HAMAP; MF_00409; LpxK; 1.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRO63716.1};
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 Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT NON_TER 295
FT /evidence="ECO:0000313|EMBL:KRO63716.1"
SQ SEQUENCE 295 AA; 34906 MW; C50C1E560D73CFAC CRC64;
MQLKKPEFWD YKKPNLISWL LFPISKLVEV YSSFFLNKKK NNFKIKTICI GNIYIGGTGK
TSLAITINEI LKKNKFRTCF IKKFYSNQDD EQKILQQNGR VFLEKKRFDS LKIAENEKYQ
YAIFDDGLQD HSIDYDFKLV CFNTINWIGN GMVIPAGPLR ENIKNLKQYN YVFLNGNLEN
LDFIKKEIFS LNPKIQIMIG EYIPTNLNEF NFNENYLAFS GIGNHETFIA MLKSNKFKIV
KHIEYPDHYK YSKNDIKELL KISKKLNCKI ITTEKDFLRL EEENINEIKF VKTKL
//