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Database: UniProt
Entry: C3JBH6_POREA
LinkDB: C3JBH6_POREA
Original site: C3JBH6_POREA 
ID   C3JBH6_POREA            Unreviewed;       358 AA.
AC   C3JBH6;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
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:EEN82326.1};
GN   ORFNames=POREN0001_1710 {ECO:0000313|EMBL:EEN82326.1};
OS   Porphyromonas endodontalis (strain ATCC 35406 / BCRC 14492 / JCM 8526 /
OS   NCTC 13058 / HG 370).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=553175 {ECO:0000313|EMBL:EEN82326.1, ECO:0000313|Proteomes:UP000004295};
RN   [1] {ECO:0000313|EMBL:EEN82326.1, ECO:0000313|Proteomes:UP000004295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35406 / BCRC 14492 / JCM 8526 / NCTC 13058 / HG 370
RC   {ECO:0000313|Proteomes:UP000004295};
RA   Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (APR-2009) 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}.
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:EEN82326.1}.
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DR   EMBL; ACNN01000026; EEN82326.1; -; Genomic_DNA.
DR   RefSeq; WP_004334078.1; NZ_ACNN01000026.1.
DR   AlphaFoldDB; C3JBH6; -.
DR   STRING; 553175.POREN0001_1710; -.
DR   GeneID; 84818267; -.
DR   eggNOG; COG1663; Bacteria.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000004295; Unassembled WGS sequence.
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:UP000004295};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00409}.
FT   BINDING         49..56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00409"
SQ   SEQUENCE   358 AA;  40966 MW;  E91B70EDB9F9E2DA CRC64;
     MKPVGTSPWL APAAALYGAG VRLRNWLYDR NILSGKSFPI PIICVGNLAV GGTGKTPLVE
     YLIETLQSEY RIAVVSRGYK RATKGLLHAT PESTAREIGD EPRQILRKYP HITMVVEGNR
     NRAIEYIMTL PEEERPQVIL LDDGFQHRAT KASLSLLLTD CQHPFMSDKL LPAGRLREPI
     KGRLRADAVV VTRCPQDMSP MDQRIMERNL SLYSNQTIYF STIQYGQLSP LFPEEAIPQL
     IQDPHTARVI AIAGIGQPEL FFRELSRRFS RVETHTYADH HVFSPREIAQ METWLRSSCD
     FIIMTEKDAM RLEGGDYKLS PLLRQRIYYL PIQTLFLGRS AERLQELLHT TLRKYYPR
//
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