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Database: UniProt
Entry: A0A0A0M8A6_9GAMM
LinkDB: A0A0A0M8A6_9GAMM
Original site: A0A0A0M8A6_9GAMM 
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
//
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