KDTA_ECOL6
ID KDTA_ECOL6 Reviewed; 425 AA.
AC P0AC76; P23282;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=3-deoxy-D-manno-octulosonic acid transferase;
DE Short=Kdo transferase;
DE EC=2.4.99.12;
DE EC=2.4.99.13;
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=c4457;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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:0000250|UniProtKB:P0AC75}.
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 -!- 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;
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.
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.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 30 subfamily. {ECO:0000305}.
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DR EMBL; AE014075; AAN82893.1; -; Genomic_DNA.
DR RefSeq; WP_000891564.1; NC_004431.1.
DR AlphaFoldDB; P0AC76; -.
DR SMR; P0AC76; -.
DR STRING; 199310.c4457; -.
DR CAZy; GT30; Glycosyltransferase Family 30.
DR EnsemblBacteria; AAN82893; AAN82893; c4457.
DR GeneID; 66672472; -.
DR KEGG; ecc:c4457; -.
DR eggNOG; COG1519; Bacteria.
DR HOGENOM; CLU_036146_2_0_6; -.
DR OMA; FIKYEFW; -.
DR BioCyc; ECOL199310:C4457-MON; -.
DR UniPathway; UPA00360; UER00483.
DR UniPathway; UPA00360; UER00484.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043842; F:Kdo transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Lipopolysaccharide biosynthesis;
KW Membrane; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..425
FT /note="3-deoxy-D-manno-octulosonic acid transferase"
FT /id="PRO_0000080288"
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
