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3-deoxy-D-manno-octulosonic acid transferase (Kdo transferase) (EC 2.4.99.12) (EC 2.4.99.13) (EC 2.4.99.14) (EC 2.4.99.15) (Kdo(2)-lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase) (Kdo(3)-lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase) (Kdo-lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase) (Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase) (Multifunctional Kdo transferase)

 KDTA_CHLP6              Reviewed;         433 AA.
F0T4D1; Q06380;
03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
03-MAY-2011, sequence version 1.
20-JUN-2018, entry version 38.
RecName: Full=3-deoxy-D-manno-octulosonic acid transferase;
Short=Kdo transferase;
EC=2.4.99.12 {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:7744029};
EC=2.4.99.13 {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:7744029};
EC=2.4.99.14 {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:7744029};
EC=2.4.99.15 {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:7744029};
AltName: Full=Kdo(2)-lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase;
AltName: Full=Kdo(3)-lipid IV(A) 3-deoxy-D-manno-octulosonic acid 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;
AltName: Full=Multifunctional Kdo transferase;
Name=waaA; Synonyms=gseA; OrderedLocusNames=CPSIT_0652, G5O_0645;
Chlamydophila psittaci (strain ATCC VR-125 / 6BC) (Chlamydia
psittaci).
Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
Chlamydia/Chlamydophila group; Chlamydia.
NCBI_TaxID=331636;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=ATCC VR-125 / 6BC;
PubMed=7523826; DOI=10.1111/j.1365-2958.1993.tb00965.x;
Mamat U., Baumann M., Schmidt G., Brade H.;
"The genus-specific lipopolysaccharide epitope of Chlamydia is
assembled in C. psittaci and C. trachomatis by glycosyltransferases of
low homology.";
Mol. Microbiol. 10:935-941(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC VR-125 / 6BC;
PubMed=21441521; DOI=10.1128/JB.00236-11;
Voigt A., Schofl G., Heidrich A., Sachse K., Saluz H.P.;
"Full-length de novo sequence of the Chlamydophila psittaci type
strain, 6BC.";
J. Bacteriol. 193:2662-2663(2011).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC VR-125 / 6BC;
PubMed=21622741; DOI=10.1128/JB.05277-11;
Grinblat-Huse V., Drabek E.F., Creasy H.H., Daugherty S.C.,
Jones K.M., Santana-Cruz I., Tallon L.J., Read T.D., Hatch T.P.,
Bavoil P., Myers G.S.;
"Genome sequences of the zoonotic pathogens Chlamydia psittaci 6BC and
Cal10.";
J. Bacteriol. 193:4039-4040(2011).
[4]
FUNCTION, CATALYTIC ACTIVITY, AND MULTIFUNCTIONALITY.
STRAIN=ATCC VR-125 / 6BC;
PubMed=7744029; DOI=10.1111/j.1432-1033.1995.0194l.x;
Holst O., Bock K., Brade L., Brade H.;
"The structures of oligosaccharide bisphosphates isolated from the
lipopolysaccharide of a recombinant Escherichia coli strain expressing
the gene gseA [3-deoxy-D-manno-octulopyranosonic acid (Kdo)
transferase] of Chlamydia psittaci 6BC.";
Eur. J. Biochem. 229:194-200(1995).
[5]
FUNCTION, CATALYTIC ACTIVITY, AND MULTIFUNCTIONALITY.
STRAIN=ATCC VR-125 / 6BC;
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).
-!- FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis.
Catalyzes the transfer of predominantly four 3-deoxy-D-manno-
octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the
tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Thus
generates the genus-specific LPS epitope of Chlamydia, composed of
the trisaccharide alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo.
{ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:7523826,
ECO:0000269|PubMed:7744029}.
-!- CATALYTIC ACTIVITY: Lipid IV(A) + CMP-beta-Kdo = alpha-Kdo-(2->6)-
lipid IV(A) + CMP. {ECO:0000269|PubMed:10951204,
ECO:0000269|PubMed:7744029}.
-!- 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:7744029}.
-!- CATALYTIC ACTIVITY: Alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IV(A)
+ CMP-beta-Kdo = alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-
(2->6)-lipid IV(A) + CMP. {ECO:0000269|PubMed:10951204,
ECO:0000269|PubMed:7744029}.
-!- CATALYTIC ACTIVITY: Alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-
(2->6)-lipid IV(A) + CMP-beta-Kdo = alpha-Kdo-(2->8)-(alpha-Kdo-
(2->4))-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IV(A) + CMP.
{ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:7744029}.
-!- PATHWAY: Bacterial outer membrane biogenesis; LPS core
biosynthesis.
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-
pass membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
Glycosyltransferase 30 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA49233.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X69476; CAA49233.1; ALT_INIT; Genomic_DNA.
EMBL; CP002549; ADZ18468.1; -; Genomic_DNA.
EMBL; CP002586; AEB55626.1; -; Genomic_DNA.
SMR; F0T4D1; -.
CAZy; GT30; Glycosyltransferase Family 30.
EnsemblBacteria; ADZ18468; ADZ18468; CPSIT_0652.
EnsemblBacteria; AEB55626; AEB55626; G5O_0645.
KEGG; chb:G5O_0645; -.
KEGG; chp:CPSIT_0652; -.
PATRIC; fig|331636.3.peg.626; -.
eggNOG; ENOG4105D8A; Bacteria.
eggNOG; COG1519; LUCA.
KO; K02527; -.
OMA; FIKYEFW; -.
BioCyc; MetaCyc:MONOMER-15506; -.
BRENDA; 2.4.99.12; 1312.
BRENDA; 2.4.99.13; 1312.
BRENDA; 2.4.99.14; 1312.
UniPathway; UPA00958; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.50.11720; -; 1.
InterPro; IPR007507; Glycos_transf_N.
InterPro; IPR038107; Glycos_transf_N_sf.
Pfam; PF04413; Glycos_transf_N; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Lipopolysaccharide biosynthesis;
Membrane; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 433 3-deoxy-D-manno-octulosonic acid
transferase.
/FTId=PRO_0000419173.
TRANSMEM 11 31 Helical; Signal-anchor. {ECO:0000255}.
REGION 277 278 CMP-Kdo binding. {ECO:0000250}.
REGION 317 319 CMP-Kdo binding. {ECO:0000250}.
REGION 344 347 CMP-Kdo binding. {ECO:0000250}.
ACT_SITE 70 70 Proton acceptor. {ECO:0000250}.
SITE 141 141 Transition state stabilizer.
{ECO:0000250}.
SITE 219 219 Transition state stabilizer.
{ECO:0000250}.
SEQUENCE 433 AA; 49322 MW; 6DFD04C3A2885F0B CRC64;
MIKGRRTKLH TFLYDCFLIF AFMVGLPRIL YKRFVHGKYT KSLGIRFGFK KPEVPGTGPV
AWFHGASVGE TALLLPLLKR FMKEYPEWRC VVTSCTESGH ENAHRLFGPL GVTTFILPLD
LSIIIKPVVR AISPSLLVFS EGDCWLNFIE EAKRLGATAV IINGKLSANS CKRFTILKRF
GRNYFSPVDG FLLQDEQHKA RFLQLGVDKE KIQVTGNIKT YTETLSENNQ RDYWREKLQL
AQDTELLVLG SVHPKDVEVW LPVVRELRRN LKVLWVPRHI ERSKELEALL SKENISYGLW
SKEATFAQHD AIIVDAIGWL KQLYSAADLA FVGGTFDDRI GGHNLLEPLQ CGVPLIFGPH
IQSQSDLAER LLSMGAGCCL DKTNIVKVIT FLLDHPEERA AYIQKGAMFL HEEKVAFDRT
WESFKRYIPC VKI


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