ID H0UKJ5_9BACT Unreviewed; 756 AA.
AC H0UKJ5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=JonanDRAFT_0826 {ECO:0000313|EMBL:EHM13204.1};
OS Jonquetella anthropi DSM 22815.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Jonquetella.
OX NCBI_TaxID=885272 {ECO:0000313|EMBL:EHM13204.1, ECO:0000313|Proteomes:UP000003806};
RN [1] {ECO:0000313|EMBL:EHM13204.1, ECO:0000313|Proteomes:UP000003806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22815 {ECO:0000313|EMBL:EHM13204.1,
RC ECO:0000313|Proteomes:UP000003806};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The Noncontiguous Finished genome of Jonquetella anthropi DSM 22815.";
RL Submitted (NOV-2011) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00409}.
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DR EMBL; CM001376; EHM13204.1; -; Genomic_DNA.
DR RefSeq; WP_008522891.1; NZ_CM001376.1.
DR AlphaFoldDB; H0UKJ5; -.
DR STRING; 885272.JonanDRAFT_0826; -.
DR eggNOG; COG1663; Bacteria.
DR eggNOG; COG4370; Bacteria.
DR HOGENOM; CLU_362436_0_0_0; -.
DR OrthoDB; 9789797at2; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000003806; 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 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; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 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:UP000003806};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00409}.
SQ SEQUENCE 756 AA; 82946 MW; 4CC83A88CEF3775E CRC64;
MSRLLQSYLQ YARGEVPGSA WALLRPLSWL TGKLSSARDW MYRHGVKRSM EAPLPVISVG
NLTTGGTNKT PFVEYLAKHM VRQGLVCGVV SRGYGGVSRT PLVFRNGRAK RSAVGDEPLL
LSNKLKEVVV AVSPDRFVGT EYLARCGCDV AVADDCFQHR RLDRDCDIVL VDATCPFGNG
QLLPGGILRE KISAISRAHL IVLSKVDQVT DGQLMEIERK LAQYVPLSRV FRSRLRIAQW
GNFESGRLAP SDFYPKDKKL AAFSAIGNPH SFLMTLQQAG VRVISSAQFK DHHRFTPSDL
NRIAANALRA GACGLTCTEK DTYNLPSGWK PPLPLWVPQV ETALEDEDRF WSYLTDCLKP
QLVVASNGHG EDAIGAVVAK KLKARLPDAQ VVAFPVVGMG SSYRAAGISV VPPPAVTPSG
GVVKYRFRDL IGDIRAGLFG HIRAQISCWR KLRYALRTPV CVGDSYMLLH ALWGQGRSPL
FVATAKTVHI SGHMKIERWL YRRNTRMIWT RDDATRQELA ENGGSVRFAG NPIMDLAEQV
PSMPSLWENG RRILVLPGSR DRAYRDLPLL LDALELVARK APVSAVLVVA STISTQRLVR
AASGWHFDET GSVPSLRKNG LTVKVFSGEV SQAARGAEVL LGLAGTANQI CAGLGIPVVS
VDEKGKRVQK KLLAGSEILV PKSPVALSDV VLGLLDDPQS MEKMAQIGRS RLGSSGMADD
LVNWAAEHLG WERRCQVWRS LQEKREETSK DVGENQ
//
