ID I8TVV1_9FIRM Unreviewed; 388 AA.
AC I8TVV1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
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=JBW_00614 {ECO:0000313|EMBL:AJQ25966.1};
OS Pelosinus fermentans JBW45.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Pelosinus.
OX NCBI_TaxID=1192197 {ECO:0000313|EMBL:AJQ25966.1, ECO:0000313|Proteomes:UP000005361};
RN [1] {ECO:0000313|EMBL:AJQ25966.1, ECO:0000313|Proteomes:UP000005361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBW45 {ECO:0000313|EMBL:AJQ25966.1,
RC ECO:0000313|Proteomes:UP000005361};
RX PubMed=26404608;
RA De Leon K.B., Utturkar S.M., Camilleri L.B., Elias D.A., Arkin A.P.,
RA Fields M.W., Brown S.D., Wall J.D.;
RT "Complete Genome Sequence of Pelosinus fermentans JBW45, a Member of a
RT Remarkably Competitive Group of Negativicutes in the Firmicutes Phylum.";
RL Genome Announc. 3:e01090-e01015(2015).
RN [2] {ECO:0000313|Proteomes:UP000005361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBW45 {ECO:0000313|Proteomes:UP000005361};
RA De Leon K.B., Utturkar S.M., Camilleri L.B., Arkin A.P., Fields M.W.,
RA Brown S.D., Wall J.D.;
RT "Complete Genome Sequence of Pelosinus fermentans JBW45.";
RL Submitted (FEB-2015) 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; CP010978; AJQ25966.1; -; Genomic_DNA.
DR RefSeq; WP_007958965.1; NZ_CP010978.1.
DR AlphaFoldDB; I8TVV1; -.
DR STRING; 1192197.JBW_00614; -.
DR KEGG; pft:JBW_00614; -.
DR HOGENOM; CLU_038816_6_0_9; -.
DR OrthoDB; 9789797at2; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000005361; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 CDD; cd01983; SIMIBI; 1.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00409}; Reference proteome {ECO:0000313|Proteomes:UP000005361};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00409}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 70..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00409"
SQ SEQUENCE 388 AA; 43656 MW; 9DE0B47591F178B7 CRC64;
MRQREEIQLY LYRLIHGEEP GILTDFLLGV LHIFSVIYGW AVLCKLALYK YGILTQHKLA
CHVISLGNIT VGGTGKTPTA QRLATIIRDM GYRVVILNRG YRAGWRGQIG LVSDGEKIYM
SAAEAGDEAY LLAKSLPKVS VVIGSNRIIT GEYAVNELKA DVIILDDGFQ HWQLARDLDI
VLIDSLNMFG NQFMLPRGTL REPLSNLSRA QIFLLTKIDQ SSLEAKEMIY STLNQYNKKA
LVVESIHKPR CFVEIEEWYK GTIGRKNVAL ESVRGHKVLA FSAIGNPSSF EQTILDLGVS
DVCGVRYVDH HDYTMAEMQY IMQKAVDEKV YALVTTEKDA VKIPAEFIHS DRPLPLYVLS
IAVFFTEGYE DLMDLIKKVE NKQDAAAD
//
