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Database: UniProt
Entry: C6X2F9_FLAB3
LinkDB: C6X2F9_FLAB3
Original site: C6X2F9_FLAB3 
ID   C6X2F9_FLAB3            Unreviewed;       344 AA.
AC   C6X2F9;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
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   OrderedLocusNames=FIC_02186 {ECO:0000313|EMBL:ACU08622.1};
OS   Flavobacteriaceae bacterium (strain 3519-10).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=531844 {ECO:0000313|EMBL:ACU08622.1, ECO:0000313|Proteomes:UP000001512};
RN   [1] {ECO:0000313|EMBL:ACU08622.1, ECO:0000313|Proteomes:UP000001512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3519-10 {ECO:0000313|EMBL:ACU08622.1,
RC   ECO:0000313|Proteomes:UP000001512};
RX   PubMed=18622572; DOI=10.1007/s00792-008-0178-2;
RA   Raymond J.A., Christner B.C., Schuster S.C.;
RT   "A bacterial ice-binding protein from the Vostok ice core.";
RL   Extremophiles 12:713-717(2008).
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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00409}.
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DR   EMBL; CP001673; ACU08622.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6X2F9; -.
DR   STRING; 531844.FIC_02186; -.
DR   KEGG; fba:FIC_02186; -.
DR   eggNOG; COG1663; Bacteria.
DR   HOGENOM; CLU_038816_6_0_10; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000001512; 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   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:UP000001512};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00409}.
SQ   SEQUENCE   344 AA;  40225 MW;  C751822C762EA405 CRC64;
     MPTMKRWYLY PFSVGYHFVT AIRNVMYDWG IFKSKSFKTP IINVGNLSVG GSGKSPMVMY
     LAEYLSKQYR TGVLSRGYGR ITKGYGITNY DSNYKTVGDE AMQLFERFKN RFVIGVSEER
     VPGAQKMIDD MDLNVLVLDD AYQHRKIKPG FNILMTDYND PYFKDFLLPA GDLRESRSGA
     ARAQIIMVSK CPADLTDEKK QYYISRIKPQ HDQKVFFSSI GYDENVYSAD KFLPDNNLSY
     YDILLITGIA NPKPLINHLA NFSHRVKHLK FKDHHNFSDQ DIKNILAEYK KLGEYKIILT
     TEKDYVRLKT FDYLRDLMYY WPINVIIDRK DDFNQIIQNY VSRN
//
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