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3-deoxy-D-manno-octulosonic acid transferase (Kdo transferase) (EC 2.4.99.12) (EC 2.4.99.13) (Bifunctional Kdo transferase) (Kdo-lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase) (Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase)

 KDTA_ECOLI              Reviewed;         425 AA.
P0AC75; P23282; Q2M7U7;
08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
08-NOV-2005, sequence version 1.
07-NOV-2018, entry version 100.
RecName: Full=3-deoxy-D-manno-octulosonic acid transferase;
Short=Kdo transferase;
EC=2.4.99.12 {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:1577828};
EC=2.4.99.13 {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:1577828};
AltName: Full=Bifunctional Kdo transferase;
AltName: Full=Kdo-lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase;
AltName: Full=Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase;
Name=waaA; Synonyms=kdtA; OrderedLocusNames=b3633, JW3608;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=2033061;
Clementz T., Raetz C.R.H.;
"A gene coding for 3-deoxy-D-manno-octulosonic-acid transferase in
Escherichia coli. Identification, mapping, cloning, and sequencing.";
J. Biol. Chem. 266:9687-9696(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=8041620; DOI=10.1093/nar/22.13.2576;
Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
"Analysis of the Escherichia coli genome. V. DNA sequence of the
region from 76.0 to 81.5 minutes.";
Nucleic Acids Res. 22:2576-2586(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
STRAIN=K12;
PubMed=1447141; DOI=10.1128/jb.174.23.7750-7756.1992;
Clementz T.;
"The gene coding for 3-deoxy-manno-octulosonic acid transferase and
the rfaQ gene are transcribed from divergently arranged promoters in
Escherichia coli.";
J. Bacteriol. 174:7750-7756(1992).
[6]
FUNCTION, CATALYTIC ACTIVITY, BIFUNCTIONALITY, SUBSTRATE SPECIFICITY,
BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR
LOCATION, AND PATHWAY.
STRAIN=K12;
PubMed=1577828;
Belunis C.J., Raetz C.R.;
"Biosynthesis of endotoxins. Purification and catalytic properties of
3-deoxy-D-manno-octulosonic acid transferase from Escherichia coli.";
J. Biol. Chem. 267:9988-9997(1992).
[7]
DISRUPTION PHENOTYPE.
STRAIN=K12 / JM109 / ATCC 53323, and
K12 / MC1061 / ATCC 53338 / DSM 7140;
PubMed=7499229; DOI=10.1074/jbc.270.46.27646;
Belunis C.J., Clementz T., Carty S.M., Raetz C.R.;
"Inhibition of lipopolysaccharide biosynthesis and cell growth
following inactivation of the kdtA gene in Escherichia coli.";
J. Biol. Chem. 270:27646-27652(1995).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND BIFUNCTIONALITY.
STRAIN=TW-183;
PubMed=10951204; DOI=10.1046/j.1432-1327.2000.01619.x;
Brabetz W., Lindner B., Brade H.;
"Comparative analyses of secondary gene products of 3-deoxy-D-manno-
oct-2-ulosonic acid transferases from Chlamydiaceae in Escherichia
coli K-12.";
Eur. J. Biochem. 267:5458-5465(2000).
[9]
SUBSTRATE FOR FTSH PROTEASE COMPLEX.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=18776015; DOI=10.1128/JB.00871-08;
Katz C., Ron E.Z.;
"Dual role of FtsH in regulating lipopolysaccharide biosynthesis in
Escherichia coli.";
J. Bacteriol. 190:7117-7122(2008).
[10]
DOMAIN.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=20394418; DOI=10.1021/bi100343e;
Chung H.S., Raetz C.R.;
"Interchangeable domains in the Kdo transferases of Escherichia coli
and Haemophilus influenzae.";
Biochemistry 49:4126-4137(2010).
-!- FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis.
Catalyzes the transfer of two 3-deoxy-D-manno-octulosonate (Kdo)
residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-
1,4'-bisphosphate precursor of lipid A.
{ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:1577828}.
-!- CATALYTIC ACTIVITY: Lipid IV(A) + CMP-beta-Kdo = alpha-Kdo-(2->6)-
lipid IV(A) + CMP. {ECO:0000269|PubMed:10951204,
ECO:0000269|PubMed:1577828}.
-!- CATALYTIC ACTIVITY: Alpha-Kdo-(2->6)-lipid IV(A) + CMP-beta-Kdo =
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IV(A) + CMP.
{ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:1577828}.
-!- ACTIVITY REGULATION: Catalytic activity is inhibited by the
antibiotic polymixin B and by Re endotoxin.
{ECO:0000269|PubMed:1577828}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=52 uM for lipid IV(A) (at pH 8) {ECO:0000269|PubMed:1577828};
KM=88 uM for CMP-Kdo (at pH 8) {ECO:0000269|PubMed:1577828};
Vmax=18 umol/min/mg enzyme (at pH 8)
{ECO:0000269|PubMed:1577828};
pH dependence:
Optimum pH is 7. {ECO:0000269|PubMed:1577828};
-!- PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis;
KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid
IV(A): step 1/4. {ECO:0000269|PubMed:1577828}.
-!- PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis;
KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid
IV(A): step 2/4. {ECO:0000269|PubMed:1577828}.
-!- PATHWAY: Bacterial outer membrane biogenesis; LPS core
biosynthesis. {ECO:0000269|PubMed:1577828}.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000305|PubMed:1577828}; Single-pass membrane protein
{ECO:0000305|PubMed:1577828}; Cytoplasmic side
{ECO:0000305|PubMed:1577828}.
-!- DOMAIN: The N-terminal half of KdtA is responsible for determining
the number of Kdo residues that are transferred to lipid IVA.
{ECO:0000269|PubMed:20394418}.
-!- PTM: Degraded by the protease FtsH; therefore FtsH regulates the
addition of the sugar moiety to the LPS and thus the maturation of
the LPS precursor. {ECO:0000269|PubMed:18776015}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene display growth
defects, absence of Kdo transferase activity, and accumulate
massive amounts of lipid IV(A). {ECO:0000269|PubMed:7499229}.
-!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
Glycosyltransferase 30 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M60670; AAA24043.1; -; Genomic_DNA.
EMBL; M86305; AAA03745.1; -; Genomic_DNA.
EMBL; U00039; AAB18610.1; -; Genomic_DNA.
EMBL; U00096; AAC76657.1; -; Genomic_DNA.
EMBL; AP009048; BAE77659.1; -; Genomic_DNA.
PIR; JU0467; JU0467.
RefSeq; NP_418090.1; NC_000913.3.
RefSeq; WP_000891564.1; NZ_LN832404.1.
ProteinModelPortal; P0AC75; -.
SMR; P0AC75; -.
BioGrid; 4263240; 354.
DIP; DIP-48036N; -.
IntAct; P0AC75; 16.
STRING; 316385.ECDH10B_3815; -.
PaxDb; P0AC75; -.
PRIDE; P0AC75; -.
EnsemblBacteria; AAC76657; AAC76657; b3633.
EnsemblBacteria; BAE77659; BAE77659; BAE77659.
GeneID; 949048; -.
KEGG; ecj:JW3608; -.
KEGG; eco:b3633; -.
PATRIC; fig|1411691.4.peg.3073; -.
EchoBASE; EB0515; -.
EcoGene; EG10520; waaA.
eggNOG; ENOG4105D8A; Bacteria.
eggNOG; COG1519; LUCA.
HOGENOM; HOG000257156; -.
InParanoid; P0AC75; -.
KO; K02527; -.
PhylomeDB; P0AC75; -.
BioCyc; EcoCyc:KDOTRANS-MONOMER; -.
BioCyc; MetaCyc:KDOTRANS-MONOMER; -.
BRENDA; 2.4.99.12; 2026.
BRENDA; 2.4.99.13; 2026.
SABIO-RK; P0AC75; -.
UniPathway; UPA00360; UER00483.
UniPathway; UPA00360; UER00484.
UniPathway; UPA00958; -.
PRO; PR:P0AC75; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:EcoliWiki.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0016740; F:transferase activity; IDA:EcoCyc.
GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009245; P:lipid A biosynthetic process; IMP:EcoliWiki.
GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.50.11720; -; 1.
InterPro; IPR001296; Glyco_trans_1.
InterPro; IPR007507; Glycos_transf_N.
InterPro; IPR038107; Glycos_transf_N_sf.
InterPro; IPR039901; Kdotransferase.
PANTHER; PTHR42755; PTHR42755; 1.
Pfam; PF00534; Glycos_transf_1; 1.
Pfam; PF04413; Glycos_transf_N; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Complete proteome;
Lipopolysaccharide biosynthesis; Membrane; Reference proteome;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 425 3-deoxy-D-manno-octulosonic acid
transferase.
/FTId=PRO_0000080286.
TRANSMEM 3 23 Helical; Signal-anchor. {ECO:0000255}.
REGION 268 269 CMP-Kdo binding. {ECO:0000250}.
REGION 309 311 CMP-Kdo binding. {ECO:0000250}.
REGION 335 338 CMP-Kdo binding. {ECO:0000250}.
ACT_SITE 60 60 Proton acceptor. {ECO:0000250}.
SITE 130 130 Transition state stabilizer.
{ECO:0000250}.
SITE 208 208 Transition state stabilizer.
{ECO:0000250}.
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


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