ID A0A0A0M8A6_9GAMM Unreviewed; 198 AA.
AC A0A0A0M8A6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, 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=N791_03940 {ECO:0000313|EMBL:KGO98252.1};
OS Lysobacter defluvii IMMIB APB-9 = DSM 18482.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1385515 {ECO:0000313|EMBL:KGO98252.1, ECO:0000313|Proteomes:UP000030003};
RN [1] {ECO:0000313|EMBL:KGO98252.1, ECO:0000313|Proteomes:UP000030003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMMIB APB-9 {ECO:0000313|EMBL:KGO98252.1,
RC ECO:0000313|Proteomes:UP000030003};
RA Wang Q., Wang G.;
RT "Genomic analysis of Lysobacter defluvii.";
RL Submitted (AUG-2013) 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:KGO98252.1}.
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DR EMBL; AVBH01000107; KGO98252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0M8A6; -.
DR STRING; 1385515.GCA_000423325_01153; -.
DR eggNOG; COG1663; Bacteria.
DR OrthoDB; 9766423at2; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000030003; 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:KGO98252.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000030003};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGO98252.1"
SQ SEQUENCE 198 AA; 21913 MW; 2BD9AD2775E9BA39 CRC64;
AEAGCDIVLC DDGLQHYRLE RDIEIEVVDA RRRYGNGRLL PAGPLRELPA RAARCDFRVV
NVAGAKNGEG PGTGFGEWPM RLVFDRAVPV RGGRPRSLES FVGHRVHAVA GIGNPERFFG
MLRDMGIAVV PHAFADHHRY RESDFEFGSA LPVLMTEKDA VKCAGFATDA FYAVPVRAEL
PEAFWVKLLD RLDALRTP
//