LPXK_ECOLI
ID LPXK_ECOLI Reviewed; 328 AA.
AC P27300; P75842; Q9R7Q6;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Tetraacyldisaccharide 4'-kinase;
DE EC=2.7.1.130 {ECO:0000269|PubMed:9268317};
DE AltName: Full=Lipid A 4'-kinase;
GN Name=lpxK; Synonyms=ycaH; OrderedLocusNames=b0915, JW0898;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8094880; DOI=10.1111/j.1365-2958.1993.tb01098.x;
RA Karow M.L., Georgopoulos C.;
RT "The essential Escherichia coli msbA gene, a multicopy suppressor of null
RT mutations in the htrB gene, is related to the universally conserved family
RT of ATP-dependent translocators.";
RL Mol. Microbiol. 7:69-79(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9268317; DOI=10.1074/jbc.272.35.21855;
RA Garrett T.A., Kadrmas J.L., Raetz C.R.H.;
RT "Identification of the gene encoding the Escherichia coli lipid A 4'-
RT kinase. Facile phosphorylation of endotoxin analogs with recombinant
RT LpxK.";
RL J. Biol. Chem. 272:21855-21864(1997).
RN [6]
RP FUNCTION, AND CHARACTERIZATION.
RX PubMed=9575203; DOI=10.1074/jbc.273.20.12457;
RA Garrett T.A., Que N.L., Raetz C.R.H.;
RT "Accumulation of a lipid A precursor lacking the 4'-phosphate following
RT inactivation of the Escherichia coli lpxK gene.";
RL J. Biol. Chem. 273:12457-12465(1998).
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:0000269|PubMed:9268317, ECO:0000269|PubMed:9575203}.
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:0000269|PubMed:9268317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + lipid A disaccharide (E. coli) = ADP + H(+) + lipid IVA
CC (E. coli); Xref=Rhea:RHEA:20700, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58466, ChEBI:CHEBI:58603,
CC ChEBI:CHEBI:456216; EC=2.7.1.130;
CC Evidence={ECO:0000269|PubMed:9268317};
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.
CC -!- SIMILARITY: Belongs to the LpxK family. {ECO:0000305}.
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DR EMBL; Z11796; CAA77840.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74001.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35661.1; -; Genomic_DNA.
DR PIR; B64831; B64831.
DR RefSeq; NP_415435.1; NC_000913.3.
DR RefSeq; WP_000570539.1; NZ_SSZK01000002.1.
DR RefSeq; WP_000570544.1; NZ_LN832404.1.
DR AlphaFoldDB; P27300; -.
DR SMR; P27300; -.
DR BioGRID; 4260014; 329.
DR DIP; DIP-10126N; -.
DR IntAct; P27300; 1.
DR STRING; 511145.b0915; -.
DR PaxDb; P27300; -.
DR PRIDE; P27300; -.
DR EnsemblBacteria; AAC74001; AAC74001; b0915.
DR EnsemblBacteria; BAA35661; BAA35661; BAA35661.
DR GeneID; 945526; -.
DR KEGG; ecj:JW0898; -.
DR KEGG; eco:b0915; -.
DR PATRIC; fig|511145.12.peg.946; -.
DR EchoBASE; EB1381; -.
DR eggNOG; COG1663; Bacteria.
DR HOGENOM; CLU_038816_2_0_6; -.
DR InParanoid; P27300; -.
DR OMA; MDDGFQN; -.
DR PhylomeDB; P27300; -.
DR BioCyc; EcoCyc:TETRAACYLDISACC4KIN-MON; -.
DR BioCyc; MetaCyc:TETRAACYLDISACC4KIN-MON; -.
DR BRENDA; 2.7.1.130; 2026.
DR UniPathway; UPA00359; UER00482.
DR PRO; PR:P27300; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IDA:EcoCyc.
DR GO; GO:0009029; F:tetraacyldisaccharide 4'-kinase activity; IDA:EcoliWiki.
DR GO; GO:0009245; P:lipid A biosynthetic process; IDA:EcoliWiki.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IMP:EcoCyc.
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 PANTHER; PTHR42724; PTHR42724; 1.
DR Pfam; PF02606; LpxK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00682; lpxK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..328
FT /note="Tetraacyldisaccharide 4'-kinase"
FT /id="PRO_0000190924"
FT BINDING 55..62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 158
FT /note="D -> N (in Ref. 1; CAA77840)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 35589 MW; B9692F479F22305D CRC64;
MIEKIWSGES PLWRLLLPLS WLYGLVSGAI RLCYKLKLKR AWRAPVPVVV VGNLTAGGNG
KTPVVVWLVE QLQQRGIRVG VVSRGYGGKA ESYPLLLSAD TTTAQAGDEP VLIYQRTDAP
VAVSPVRSDA VKAILAQHPD VQIIVTDDGL QHYRLARDVE IVVIDGVRRF GNGWWLPAGP
MRERAGRLKS VDAVIVNGGV PRSGEIPMHL LPGQAVNLRT GTRCDVAQLE HVVAMAGIGH
PPRFFATLKM CGVQPEKCVP LADHQSLNHA DVSALVSAGQ TLVMTEKDAV KCRAFAEENW
WYLPVDAQLS GDEPAKLLTQ LTLLASGN
