GenomeNet

Database: UniProt
Entry: A0A0M4NVQ7_9GAMM
LinkDB: A0A0M4NVQ7_9GAMM
Original site: A0A0M4NVQ7_9GAMM 
ID   A0A0M4NVQ7_9GAMM        Unreviewed;       315 AA.
AC   A0A0M4NVQ7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Tetraacyldisaccharide 4'-kinase {ECO:0000256|ARBA:ARBA00016436, ECO:0000256|HAMAP-Rule:MF_00409};
DE            EC=2.7.1.130 {ECO:0000256|ARBA:ARBA00012071, ECO:0000256|HAMAP-Rule:MF_00409};
DE   AltName: Full=Lipid A 4'-kinase {ECO:0000256|ARBA:ARBA00029757, ECO:0000256|HAMAP-Rule:MF_00409};
GN   Name=lpxK {ECO:0000256|HAMAP-Rule:MF_00409};
GN   ORFNames=SP60_01720 {ECO:0000313|EMBL:ALE52068.1};
OS   Candidatus Thioglobus autotrophicus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus.
OX   NCBI_TaxID=1705394 {ECO:0000313|EMBL:ALE52068.1, ECO:0000313|Proteomes:UP000058020};
RN   [1] {ECO:0000313|EMBL:ALE52068.1, ECO:0000313|Proteomes:UP000058020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF1 {ECO:0000313|EMBL:ALE52068.1,
RC   ECO:0000313|Proteomes:UP000058020};
RX   PubMed=26494660;
RA   Shah V., Morris R.M.;
RT   "Genome Sequence of 'Candidatus Thioglobus autotrophica' Strain EF1, a
RT   Chemoautotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL   Genome Announc. 3:e01156-15(2015).
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, ECO:0000256|HAMAP-Rule:MF_00409}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+);
CC         Xref=Rhea:RHEA:67840, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:176343, ChEBI:CHEBI:176425, ChEBI:CHEBI:456216;
CC         EC=2.7.1.130; Evidence={ECO:0000256|HAMAP-Rule:MF_00409};
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       ECO:0000256|HAMAP-Rule:MF_00409}.
CC   -!- SIMILARITY: Belongs to the LpxK family. {ECO:0000256|HAMAP-
CC       Rule:MF_00409}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP010552; ALE52068.1; -; Genomic_DNA.
DR   RefSeq; WP_053951000.1; NZ_CP010552.1.
DR   AlphaFoldDB; A0A0M4NVQ7; -.
DR   STRING; 1705394.SP60_01720; -.
DR   KEGG; tho:SP60_01720; -.
DR   PATRIC; fig|1705394.5.peg.346; -.
DR   OrthoDB; 9766423at2; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000058020; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009029; F:tetraacyldisaccharide 4'-kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01983; SIMIBI; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00409; LpxK; 1.
DR   InterPro; IPR003758; LpxK.
DR   InterPro; IPR027417; P-loop_NTPase.
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.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00409};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00409};
KW   Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP-
KW   Rule:MF_00409};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_00409};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_00409};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00409}; Reference proteome {ECO:0000313|Proteomes:UP000058020};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00409}.
FT   BINDING         52..59
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00409"
SQ   SEQUENCE   315 AA;  35608 MW;  21A6B4555FD2297A CRC64;
     MDLNTRGVVN YLLWPVSGVF YALSKLRRAL YRWGILQTHH FQVPVIVVGN ITVGGSGKTP
     VVIKLVQYFK QQGRRVGVVS RGYGGTHTQG SLLVNAHTNV ALSGDEPLLI VISTGVPVMV
     NKDRSQAVKD LIDQHQVDLV ISDDGLQHYA MDRTVEIAVI DGNRRFGNQF FLPAGPLRES
     QNRLKQVDFI INNGGVFPGE VSVQLKPVKF VHMRSEEEFP LDFFKNQTCH GMAGIGHPER
     FFNTLAQLNI DVQKQAFEDH YPYQAQDLAF EDNYPIIMTA KDWVKCREFA NDKMYYLKVD
     LDIGKDFLNK LAEKL
//
DBGET integrated database retrieval system