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Database: UniProt
Entry: I0IIS5_PHYMF
LinkDB: I0IIS5_PHYMF
Original site: I0IIS5_PHYMF 
ID   I0IIS5_PHYMF            Unreviewed;       356 AA.
AC   I0IIS5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
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   ECO:0000313|EMBL:BAM05163.1};
GN   OrderedLocusNames=PSMK_30040 {ECO:0000313|EMBL:BAM05163.1};
OS   Phycisphaera mikurensis (strain NBRC 102666 / KCTC 22515 / FYK2301M01).
OC   Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC   Phycisphaeraceae; Phycisphaera.
OX   NCBI_TaxID=1142394 {ECO:0000313|EMBL:BAM05163.1, ECO:0000313|Proteomes:UP000007881};
RN   [1] {ECO:0000313|EMBL:BAM05163.1, ECO:0000313|Proteomes:UP000007881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102666 / KCTC 22515 / FYK2301M01
RC   {ECO:0000313|Proteomes:UP000007881};
RA   Ankai A., Hosoyama A., Terui Y., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA   Yamada-Narita S., Kawakoshi A., Fukunaga Y., Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Phycisphaera mikurensis NBRC 102666.";
RL   Submitted (FEB-2012) 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, 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}.
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DR   EMBL; AP012338; BAM05163.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0IIS5; -.
DR   STRING; 1142394.PSMK_30040; -.
DR   KEGG; phm:PSMK_30040; -.
DR   PATRIC; fig|1142394.8.peg.3110; -.
DR   eggNOG; COG1663; Bacteria.
DR   HOGENOM; CLU_038816_6_0_0; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000007881; 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:UP000007881};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00409}.
FT   REGION          45..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         63..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00409"
SQ   SEQUENCE   356 AA;  37280 MW;  8E6572A99B4CA47B CRC64;
     MPVEDRYVRL VEGRSAGVLA SAARGLLRAA TPAWRLGLAI DQQRKRRGRR PLGRPTASIG
     NLSVGGTGKT PAVAWAVRRL LDAGHRPAVL TRGHGGDAQR PADEVLELRG MLRDAAPVIA
     DPDRHAAAAA ALAASPGLTC FVLDDGFQRL DVARDLDLVL VDASRTLASA RLLPGGLLRE
     PPAALTRADA VLLTRVDRAG PAATGETAAW VTRWHGRPPL ASFAHRWSGV DAYPPAGAAP
     AIAGRRLYAA AGIGHPRAFA EQLAAAGAEV VGAARLADHH RPTAGGLARL HADARAAGAD
     AVATTEKDRV KWAMLDPGPD ALPVLVPRLR FEPVAGEAAL LALLRERLPR PVDRPA
//
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