KDTA_CHLP6
ID KDTA_CHLP6 Reviewed; 433 AA.
AC F0T4D1; Q06380;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
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:7744029};
DE EC=2.4.99.13 {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:7744029};
DE EC=2.4.99.14 {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:7744029};
DE EC=2.4.99.15 {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:7744029};
DE AltName: Full=Kdo(2)-lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase;
DE AltName: Full=Kdo(3)-lipid IV(A) 3-deoxy-D-manno-octulosonic acid 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;
DE AltName: Full=Multifunctional Kdo transferase;
GN Name=waaA; Synonyms=gseA; OrderedLocusNames=CPSIT_0652, G5O_0645;
OS Chlamydophila psittaci (strain ATCC VR-125 / 6BC) (Chlamydia psittaci).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=331636;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC VR-125 / 6BC;
RX PubMed=7523826; DOI=10.1111/j.1365-2958.1993.tb00965.x;
RA Mamat U., Baumann M., Schmidt G., Brade H.;
RT "The genus-specific lipopolysaccharide epitope of Chlamydia is assembled in
RT C. psittaci and C. trachomatis by glycosyltransferases of low homology.";
RL Mol. Microbiol. 10:935-941(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-125 / 6BC;
RX PubMed=21441521; DOI=10.1128/jb.00236-11;
RA Voigt A., Schofl G., Heidrich A., Sachse K., Saluz H.P.;
RT "Full-length de novo sequence of the Chlamydophila psittaci type strain,
RT 6BC.";
RL J. Bacteriol. 193:2662-2663(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-125 / 6BC;
RX PubMed=21622741; DOI=10.1128/jb.05277-11;
RA Grinblat-Huse V., Drabek E.F., Creasy H.H., Daugherty S.C., Jones K.M.,
RA Santana-Cruz I., Tallon L.J., Read T.D., Hatch T.P., Bavoil P., Myers G.S.;
RT "Genome sequences of the zoonotic pathogens Chlamydia psittaci 6BC and
RT Cal10.";
RL J. Bacteriol. 193:4039-4040(2011).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND MULTIFUNCTIONALITY.
RC STRAIN=ATCC VR-125 / 6BC;
RX PubMed=7744029; DOI=10.1111/j.1432-1033.1995.0194l.x;
RA Holst O., Bock K., Brade L., Brade H.;
RT "The structures of oligosaccharide bisphosphates isolated from the
RT lipopolysaccharide of a recombinant Escherichia coli strain expressing the
RT gene gseA [3-deoxy-D-manno-octulopyranosonic acid (Kdo) transferase] of
RT Chlamydia psittaci 6BC.";
RL Eur. J. Biochem. 229:194-200(1995).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND MULTIFUNCTIONALITY.
RC STRAIN=ATCC VR-125 / 6BC;
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).
CC -!- FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes
CC the transfer of predominantly four 3-deoxy-D-manno-octulosonate (Kdo)
CC residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-
CC bisphosphate precursor of lipid A. Thus generates the genus-specific
CC LPS epitope of Chlamydia, composed of the trisaccharide alpha-Kdo-
CC (2->8)-alpha-Kdo-(2->4)-alpha-Kdo. {ECO:0000269|PubMed:10951204,
CC ECO:0000269|PubMed:7523826, ECO:0000269|PubMed:7744029}.
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:7744029};
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:7744029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP-3-deoxy-
CC beta-D-manno-octulosonate = alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-
CC Kdo-(2->6)-lipid IVA + CMP + H(+); Xref=Rhea:RHEA:28154,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:60365, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:85987, ChEBI:CHEBI:86234; EC=2.4.99.14;
CC Evidence={ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:7744029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA +
CC CMP-3-deoxy-beta-D-manno-octulosonate = alpha-Kdo-(2->8)-[alpha-Kdo-
CC (2->4)]-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP + H(+);
CC Xref=Rhea:RHEA:28158, ChEBI:CHEBI:15378, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:85987, ChEBI:CHEBI:86234, ChEBI:CHEBI:86236;
CC EC=2.4.99.15; Evidence={ECO:0000269|PubMed:10951204,
CC ECO:0000269|PubMed:7744029};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA49233.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X69476; CAA49233.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002549; ADZ18468.1; -; Genomic_DNA.
DR EMBL; CP002586; AEB55626.1; -; Genomic_DNA.
DR AlphaFoldDB; F0T4D1; -.
DR SMR; F0T4D1; -.
DR CAZy; GT30; Glycosyltransferase Family 30.
DR KEGG; chb:G5O_0645; -.
DR KEGG; chp:CPSIT_0652; -.
DR PATRIC; fig|331636.3.peg.626; -.
DR HOGENOM; CLU_036146_2_1_0; -.
DR OMA; FIKYEFW; -.
DR BioCyc; MetaCyc:MON-15506; -.
DR BRENDA; 2.4.99.12; 1312.
DR BRENDA; 2.4.99.13; 1312.
DR BRENDA; 2.4.99.14; 1312.
DR UniPathway; UPA00958; -.
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: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; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..433
FT /note="3-deoxy-D-manno-octulosonic acid transferase"
FT /id="PRO_0000419173"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 277..278
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT BINDING 317..319
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT BINDING 344..347
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT SITE 141
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 219
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ 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
