LPXK_PELUB
ID LPXK_PELUB Reviewed; 314 AA.
AC Q4FPB7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Tetraacyldisaccharide 4'-kinase {ECO:0000255|HAMAP-Rule:MF_00409};
DE EC=2.7.1.130 {ECO:0000255|HAMAP-Rule:MF_00409};
DE AltName: Full=Lipid A 4'-kinase {ECO:0000255|HAMAP-Rule:MF_00409};
GN Name=lpxK {ECO:0000255|HAMAP-Rule:MF_00409}; OrderedLocusNames=SAR11_0149;
OS Pelagibacter ubique (strain HTCC1062).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC Pelagibacteraceae; Candidatus Pelagibacter.
OX NCBI_TaxID=335992;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC1062;
RX PubMed=16109880; DOI=10.1126/science.1114057;
RA Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA Carrington J.C., Mathur E.J.;
RT "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL Science 309:1242-1245(2005).
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:0000255|HAMAP-Rule:MF_00409}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + {2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-
CC glucosaminyl}-(1->6)-{2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-
CC D-glucosaminyl phosphate} = ADP + {2-N,3-O-bis[(3R)-3-
CC hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl}-(1->6)-{2-N,3-
CC O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate}.;
CC EC=2.7.1.130; Evidence={ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00409}.
CC -!- SIMILARITY: Belongs to the LpxK family. {ECO:0000255|HAMAP-
CC Rule:MF_00409}.
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DR EMBL; CP000084; AAZ20972.1; -; Genomic_DNA.
DR RefSeq; WP_011281505.1; NC_007205.1.
DR AlphaFoldDB; Q4FPB7; -.
DR SMR; Q4FPB7; -.
DR STRING; 335992.SAR11_0149; -.
DR EnsemblBacteria; AAZ20972; AAZ20972; SAR11_0149.
DR GeneID; 66294650; -.
DR KEGG; pub:SAR11_0149; -.
DR eggNOG; COG1663; Bacteria.
DR HOGENOM; CLU_038816_0_0_5; -.
DR OrthoDB; 1382484at2; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000002528; 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 PANTHER; PTHR42724; PTHR42724; 1.
DR Pfam; PF02606; LpxK; 1.
DR TIGRFAMs; TIGR00682; lpxK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..314
FT /note="Tetraacyldisaccharide 4'-kinase"
FT /id="PRO_0000340845"
FT BINDING 54..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
SQ SEQUENCE 314 AA; 36175 MW; 63DC161F477DEA65 CRC64;
MKLKKPKFWD HKKPSFFSYL LLPFSIILGL ITKIKSKPKF SNSKIKTICV GNIYIGGTGK
TSLAIKIKEI LDKNNIRACF IKKFYPNQTD EQKLLSKNGV LFSNLKRITA LNEAISEGFE
VAIFDDGLQD STIKYDLEIV CFNNLNWIGN GLTLPSGPLR ENINNLKSYE NVFLNGNEES
LIAIKEQIKR INPNININSG KYIPLNIDEF DKDQNYLVFS GIGNHKTFVE MLKNNKLKIV
SDLEYPDHYQ YSKKDFDEII INAKKFNAHI ITTEKDYLRL ENLNKNEIFY VKSSLDISDE
KNLTNKLIKL NEKN
