ID I2QHL2_9BRAD Unreviewed; 338 AA.
AC I2QHL2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=Bra1253DRAFT_03999 {ECO:0000313|EMBL:EIG59268.1};
OS Bradyrhizobium sp. WSM1253.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=319003 {ECO:0000313|EMBL:EIG59268.1, ECO:0000313|Proteomes:UP000005125};
RN [1] {ECO:0000313|EMBL:EIG59268.1, ECO:0000313|Proteomes:UP000005125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM1253 {ECO:0000313|EMBL:EIG59268.1,
RC ECO:0000313|Proteomes:UP000005125};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA Howieson J., Reeve W., Woyke T.;
RT "Improved High-Quality Draft sequence of Bradyrhizobium sp. WSM1253.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM1253 {ECO:0000313|Proteomes:UP000005125};
RX PubMed=26629308;
RA Tiwari R., Howieson J., Yates R., Tian R., Held B., Tapia R., Han C.,
RA Seshadri R., Reddy T.B., Huntemann M., Pati A., Woyke T., Markowitz V.,
RA Ivanova N., Kyrpides N., Reeve W.;
RT "Genome sequence of Bradyrhizobium sp. WSM1253; a microsymbiont of
RT Ornithopus compressus from the Greek Island of Sifnos.";
RL Stand. Genomic Sci. 10:113-113(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; JH600073; EIG59268.1; -; Genomic_DNA.
DR RefSeq; WP_007596926.1; NZ_JH600073.1.
DR AlphaFoldDB; I2QHL2; -.
DR eggNOG; COG1663; Bacteria.
DR HOGENOM; CLU_038816_0_0_5; -.
DR OrthoDB; 9766423at2; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000005125; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00409}.
FT BINDING 51..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00409"
SQ SEQUENCE 338 AA; 36676 MW; C2068B48C6F14E9E CRC64;
MREPAFWYRP RSLESYALGP LGALYGAITE RRMLREGVDA GIPVICVGNY HVGGAGKTPT
VLALTKLLRE LGETPVVLSR GYGGSLKGPV MVDSMRHTAS DVGDEPLMMA RDVPVTVARD
RLDGVVLAKS QGATVILMDD GFQNPRLLKD TSLIVIDSER GLGNGKVFPA GPLRAPLKAQ
LARTDALVLI GGGRAADAVA AELARRNKPE LRARLKPDAG SVARLLGKPV FAFAGIGDPE
RFFRSLRTGG IEVARTRAFA DHHMFSNDEI ATLAAEAQRE QQTLVTTEKD LARLHGREGV
PDGIVPFAVQ LEFDDPATLR QLISDHLYKA RERRFGRR
//
