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Entry: A0A0N9ZZN9_9RHOB
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Original site: A0A0N9ZZN9_9RHOB 
ID   A0A0N9ZZN9_9RHOB        Unreviewed;       330 AA.
AC   A0A0N9ZZN9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=IMCC12053_1891 {ECO:0000313|EMBL:ALI55838.1},
GN   SAMN05444421_11084 {ECO:0000313|EMBL:SFK90232.1};
OS   Celeribacter marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=1397108 {ECO:0000313|EMBL:ALI55838.1, ECO:0000313|Proteomes:UP000064920};
RN   [1] {ECO:0000313|EMBL:ALI55838.1, ECO:0000313|Proteomes:UP000064920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC 12053 {ECO:0000313|EMBL:ALI55838.1,
RC   ECO:0000313|Proteomes:UP000064920};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SFK90232.1, ECO:0000313|Proteomes:UP000181863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100036 {ECO:0000313|EMBL:SFK90232.1,
RC   ECO:0000313|Proteomes:UP000181863};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; CP012023; ALI55838.1; -; Genomic_DNA.
DR   EMBL; FOSM01000010; SFK90232.1; -; Genomic_DNA.
DR   RefSeq; WP_062218391.1; NZ_FOSM01000010.1.
DR   AlphaFoldDB; A0A0N9ZZN9; -.
DR   STRING; 1397108.IMCC12053_1891; -.
DR   KEGG; cmar:IMCC12053_1891; -.
DR   PATRIC; fig|1397108.4.peg.1933; -.
DR   OrthoDB; 9766423at2; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000064920; Chromosome.
DR   Proteomes; UP000181863; 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:UP000064920};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00409}.
FT   BINDING         54..61
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00409"
SQ   SEQUENCE   330 AA;  35578 MW;  51AD9BA8F4B603D1 CRC64;
     MREPKFWSNP AQHPGLMTRI LTPLGAIYAS QTARRAAKTG YKSSVPVICV GNINAGGTGK
     TPTVIALAQR LIERGKSVHV VSRGYGGSLH GPVRVNERSH NADQVGDEPL LIAAFTPTWV
     AKDRADGVRL AEKDGADVIL LDDGMQNGSV QKDATFVVVD AHRGFGNGRV IPAGPLREPI
     ERGLMRADAV VSIGDAAAQD RFSGLWADTV TVPRVRANLA PLQTGFDWAD QPVLAFAGIG
     HPEKFFATLR GLGAHLRRAE ALNDHQPLSM QLMTRLEIEA LALGAQMVTT EKDAVRLPRA
     FRQKVVTLPV RLMSEDWSVI DAKLAQLGLD
//
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