KDTA_ECOLI
ID KDTA_ECOLI Reviewed; 425 AA.
AC P0AC75; P23282; Q2M7U7;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=3-deoxy-D-manno-octulosonic acid transferase;
DE Short=Kdo transferase;
DE EC=2.4.99.12 {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:1577828};
DE EC=2.4.99.13 {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:1577828};
DE AltName: Full=Bifunctional Kdo transferase;
DE AltName: Full=Kdo-lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase;
DE AltName: Full=Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase;
GN Name=waaA; Synonyms=kdtA; OrderedLocusNames=b3633, JW3608;
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=2033061; DOI=10.1016/s0021-9258(18)92875-9;
RA Clementz T., Raetz C.R.H.;
RT "A gene coding for 3-deoxy-D-manno-octulosonic-acid transferase in
RT Escherichia coli. Identification, mapping, cloning, and sequencing.";
RL J. Biol. Chem. 266:9687-9696(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
RC STRAIN=K12;
RX PubMed=1447141; DOI=10.1128/jb.174.23.7750-7756.1992;
RA Clementz T.;
RT "The gene coding for 3-deoxy-manno-octulosonic acid transferase and the
RT rfaQ gene are transcribed from divergently arranged promoters in
RT Escherichia coli.";
RL J. Bacteriol. 174:7750-7756(1992).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIFUNCTIONALITY, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP AND PATHWAY.
RC STRAIN=K12;
RX PubMed=1577828; DOI=10.1016/s0021-9258(19)50189-2;
RA Belunis C.J., Raetz C.R.;
RT "Biosynthesis of endotoxins. Purification and catalytic properties of 3-
RT deoxy-D-manno-octulosonic acid transferase from Escherichia coli.";
RL J. Biol. Chem. 267:9988-9997(1992).
RN [7]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / JM109 / ATCC 53323, and K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=7499229; DOI=10.1074/jbc.270.46.27646;
RA Belunis C.J., Clementz T., Carty S.M., Raetz C.R.;
RT "Inhibition of lipopolysaccharide biosynthesis and cell growth following
RT inactivation of the kdtA gene in Escherichia coli.";
RL J. Biol. Chem. 270:27646-27652(1995).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIFUNCTIONALITY.
RC STRAIN=TW-183;
RX PubMed=10951204; DOI=10.1046/j.1432-1327.2000.01619.x;
RA Brabetz W., Lindner B., Brade H.;
RT "Comparative analyses of secondary gene products of 3-deoxy-D-manno-oct-2-
RT ulosonic acid transferases from Chlamydiaceae in Escherichia coli K-12.";
RL Eur. J. Biochem. 267:5458-5465(2000).
RN [9]
RP SUBSTRATE FOR FTSH PROTEASE COMPLEX.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=18776015; DOI=10.1128/jb.00871-08;
RA Katz C., Ron E.Z.;
RT "Dual role of FtsH in regulating lipopolysaccharide biosynthesis in
RT Escherichia coli.";
RL J. Bacteriol. 190:7117-7122(2008).
RN [10]
RP DOMAIN.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=20394418; DOI=10.1021/bi100343e;
RA Chung H.S., Raetz C.R.;
RT "Interchangeable domains in the Kdo transferases of Escherichia coli and
RT Haemophilus influenzae.";
RL Biochemistry 49:4126-4137(2010).
CC -!- FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes
CC the transfer of two 3-deoxy-D-manno-octulosonate (Kdo) residues from
CC CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate
CC precursor of lipid A. {ECO:0000269|PubMed:10951204,
CC ECO:0000269|PubMed:1577828}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) =
CC alpha-Kdo-(2->6)-lipid IVA + CMP + H(+); Xref=Rhea:RHEA:28066,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58603, ChEBI:CHEBI:60364,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:85987; EC=2.4.99.12;
CC Evidence={ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:1577828};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Kdo-(2->6)-lipid IVA + CMP-3-deoxy-beta-D-manno-
CC octulosonate = alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP +
CC H(+); Xref=Rhea:RHEA:28062, ChEBI:CHEBI:15378, ChEBI:CHEBI:60364,
CC ChEBI:CHEBI:60365, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987;
CC EC=2.4.99.13; Evidence={ECO:0000269|PubMed:10951204,
CC ECO:0000269|PubMed:1577828};
CC -!- ACTIVITY REGULATION: Catalytic activity is inhibited by the antibiotic
CC polymixin B and by Re endotoxin. {ECO:0000269|PubMed:1577828}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=52 uM for lipid IV(A) (at pH 8) {ECO:0000269|PubMed:1577828};
CC KM=88 uM for CMP-Kdo (at pH 8) {ECO:0000269|PubMed:1577828};
CC Vmax=18 umol/min/mg enzyme (at pH 8) {ECO:0000269|PubMed:1577828};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:1577828};
CC -!- PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis; KDO(2)-
CC lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A): step
CC 1/4. {ECO:0000269|PubMed:1577828}.
CC -!- PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis; KDO(2)-
CC lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A): step
CC 2/4. {ECO:0000269|PubMed:1577828}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC {ECO:0000269|PubMed:1577828}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:1577828};
CC Single-pass membrane protein {ECO:0000305|PubMed:1577828}; Cytoplasmic
CC side {ECO:0000305|PubMed:1577828}.
CC -!- DOMAIN: The N-terminal half of KdtA is responsible for determining the
CC number of Kdo residues that are transferred to lipid IVA.
CC {ECO:0000269|PubMed:20394418}.
CC -!- PTM: Degraded by the protease FtsH; therefore FtsH regulates the
CC addition of the sugar moiety to the LPS and thus the maturation of the
CC LPS precursor. {ECO:0000269|PubMed:18776015}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display growth defects,
CC absence of Kdo transferase activity, and accumulate massive amounts of
CC lipid IV(A). {ECO:0000269|PubMed:7499229}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 30 subfamily. {ECO:0000305}.
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DR EMBL; M60670; AAA24043.1; -; Genomic_DNA.
DR EMBL; M86305; AAA03745.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18610.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76657.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77659.1; -; Genomic_DNA.
DR PIR; JU0467; JU0467.
DR RefSeq; NP_418090.1; NC_000913.3.
DR RefSeq; WP_000891564.1; NZ_STEB01000024.1.
DR AlphaFoldDB; P0AC75; -.
DR SMR; P0AC75; -.
DR BioGRID; 4263240; 354.
DR BioGRID; 853292; 1.
DR DIP; DIP-48036N; -.
DR IntAct; P0AC75; 16.
DR STRING; 511145.b3633; -.
DR jPOST; P0AC75; -.
DR PaxDb; P0AC75; -.
DR PRIDE; P0AC75; -.
DR DNASU; 949048; -.
DR EnsemblBacteria; AAC76657; AAC76657; b3633.
DR EnsemblBacteria; BAE77659; BAE77659; BAE77659.
DR GeneID; 66672472; -.
DR GeneID; 949048; -.
DR KEGG; ecj:JW3608; -.
DR KEGG; eco:b3633; -.
DR PATRIC; fig|1411691.4.peg.3073; -.
DR EchoBASE; EB0515; -.
DR eggNOG; COG1519; Bacteria.
DR HOGENOM; CLU_036146_2_0_6; -.
DR InParanoid; P0AC75; -.
DR OMA; FIKYEFW; -.
DR PhylomeDB; P0AC75; -.
DR BioCyc; EcoCyc:KDOTRANS-MON; -.
DR BioCyc; MetaCyc:KDOTRANS-MON; -.
DR BRENDA; 2.4.99.12; 2026.
DR BRENDA; 2.4.99.13; 2026.
DR SABIO-RK; P0AC75; -.
DR UniPathway; UPA00360; UER00483.
DR UniPathway; UPA00360; UER00484.
DR UniPathway; UPA00958; -.
DR PRO; PR:P0AC75; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0043842; F:Kdo transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IDA:EcoCyc.
DR GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009245; P:lipid A biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.11720; -; 1.
DR InterPro; IPR007507; Glycos_transf_N.
DR InterPro; IPR038107; Glycos_transf_N_sf.
DR InterPro; IPR039901; Kdotransferase.
DR PANTHER; PTHR42755; PTHR42755; 1.
DR Pfam; PF04413; Glycos_transf_N; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Lipopolysaccharide biosynthesis;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..425
FT /note="3-deoxy-D-manno-octulosonic acid transferase"
FT /id="PRO_0000080286"
FT TRANSMEM 3..23
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 268..269
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT BINDING 309..311
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT BINDING 335..338
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT SITE 130
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 208
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 425 AA; 47291 MW; B063850A1FF392AF CRC64;
MLELLYTALL YLIQPLIWIR LWVRGRKAPA YRKRWGERYG FYRHPLKPGG IMLHSVSVGE
TLAAIPLVRA LRHRYPDLPI TVTTMTPTGS ERVQSAFGKD VQHVYLPYDL PDALNRFLNK
VDPKLVLIME TELWPNLIAA LHKRKIPLVI ANARLSARSA AGYAKLGKFV RRLLRRITLI
AAQNEEDGAR FVALGAKNNQ VTVTGSLKFD ISVTPQLAAK AVTLRRQWAP HRPVWIATST
HEGEESVVIA AHQALLQQFP NLLLILVPRH PERFPDAINL VRQAGLSYIT RSSGEVPSTS
TQVVVGDTMG ELMLLYGIAD LAFVGGSLVE RGGHNPLEAA AHAIPVLMGP HTFNFKDICA
RLEQASGLIT VTDATTLAKE VSSLLTDADY RSFYGRHAVE VLYQNQGALQ RLLQLLEPYL
PPKTH
