KDTA_CHLPN
ID KDTA_CHLPN Reviewed; 437 AA.
AC Q46222; Q46224; Q9JS00; Q9S6B4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 144.
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:8748024};
DE EC=2.4.99.13 {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:8748024};
DE EC=2.4.99.14 {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:8748024};
DE AltName: Full=Kdo(2)-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=Trifunctional Kdo transferase;
GN Name=waaA; Synonyms=gseA, kdtA;
GN OrderedLocusNames=CPn_0154, CP_0617, CpB0155;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP TRIFUNCTIONALITY.
RC STRAIN=TW-183;
RX PubMed=8748024; DOI=10.1111/j.1365-2958.1995.mmi_18030391.x;
RA Loebau S., Mamat U., Brabetz W., Brade H.;
RT "Molecular cloning, sequence analysis, and functional characterization of
RT the lipopolysaccharide biosynthetic gene kdtA encoding 3-deoxy-alpha-D-
RT manno-octulosonic acid transferase of Chlamydia pneumoniae strain TW-183.";
RL Mol. Microbiol. 18:391-399(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Koala type I;
RX PubMed=9765820; DOI=10.1016/s0923-2508(97)83872-7;
RA Girjes A., Carrick F.N., Lavin M.F.;
RT "Lipopolysaccharide biosynthesis genes in koala type I Chlamydia: cloning
RT and characterization.";
RL Res. Microbiol. 148:413-425(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-329.
RC STRAIN=AR3883;
RA Kaltenboeck B., Gao D.;
RT "PCR amplification and sequencing of the partial coding region of the Kdo
RT transferase of Chlamydia.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND TRIFUNCTIONALITY.
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).
CC -!- FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes
CC the transfer of three 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. Thus generates the genus-specific LPS epitope of
CC Chlamydia, composed of the trisaccharide alpha-Kdo-(2->8)-alpha-Kdo-
CC (2->4)-alpha-Kdo. {ECO:0000269|PubMed:10951204,
CC ECO:0000269|PubMed:8748024}.
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:8748024};
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:8748024};
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:8748024};
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; Z31593; CAA83470.1; -; Genomic_DNA.
DR EMBL; AE001363; AAD18307.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38432.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98364.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98088.1; -; Genomic_DNA.
DR EMBL; X80061; CAA56368.1; -; Genomic_DNA.
DR EMBL; AF111204; AAD20340.1; -; Genomic_DNA.
DR PIR; B86510; B86510.
DR PIR; E81557; E81557.
DR PIR; S70546; S70546.
DR RefSeq; NP_224362.1; NC_000922.1.
DR RefSeq; WP_010882804.1; NZ_LN847257.1.
DR AlphaFoldDB; Q46222; -.
DR SMR; Q46222; -.
DR STRING; 115711.CP_0617; -.
DR CAZy; GT30; Glycosyltransferase Family 30.
DR EnsemblBacteria; AAD18307; AAD18307; CPn_0154.
DR EnsemblBacteria; AAF38432; AAF38432; CP_0617.
DR GeneID; 45050199; -.
DR KEGG; cpa:CP_0617; -.
DR KEGG; cpj:gseA; -.
DR KEGG; cpn:CPn_0154; -.
DR KEGG; cpt:CpB0155; -.
DR PATRIC; fig|115713.3.peg.176; -.
DR eggNOG; COG1519; Bacteria.
DR HOGENOM; CLU_036146_2_0_0; -.
DR OrthoDB; 1163086at2; -.
DR BioCyc; MetaCyc:MON-15504; -.
DR BRENDA; 2.4.99.12; 1311.
DR BRENDA; 2.4.99.13; 1311.
DR BRENDA; 2.4.99.14; 1311.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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: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..437
FT /note="3-deoxy-D-manno-octulosonic acid transferase"
FT /id="PRO_0000080283"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 279..280
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT BINDING 319..321
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT BINDING 346..349
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"
FT VARIANT 6
FT /note="V -> I (in strain: Koala type I)"
FT VARIANT 183
FT /note="N -> T (in strain: Koala type I)"
FT VARIANT 201
FT /note="R -> P (in strain: Koala type I)"
FT VARIANT 234
FT /note="T -> A (in strain: Koala type I)"
FT VARIANT 249
FT /note="I -> V (in strain: Koala type I)"
FT VARIANT 311..312
FT /note="VP -> TS (in strain: Koala type I)"
FT VARIANT 368..369
FT /note="EL -> DV (in strain: Koala type I)"
FT VARIANT 401
FT /note="V -> M (in strain: Koala type I)"
FT VARIANT 413
FT /note="V -> L (in strain: Koala type I)"
FT CONFLICT 137
FT /note="V -> A (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..164
FT /note="RIGATTLVING -> TYRCNYSRHQW (in Ref. 6; CAA56368)"
FT /evidence="ECO:0000305"
FT CONFLICT 295..307
FT /note="LHIPYGLWSRGAN -> CTFLMGCGAVVHQ (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 319..321
FT /note="IGL -> NWLV (in Ref. 6; CAA56368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 49187 MW; 99BF3083E4858250 CRC64;
MMLRGVHRIF KCFYDVVLVC AFVIALPKLL YKMLVYGKYK KSLAVRFGLK KPHVPGEGPL
VWFHGASVGE VRLLLPVLEK FCEEFPGWRC LVTSCTELGV QVASQVFIPM GATVSILPLD
FSIIIKSVVA KLRPSLVVFS EGDCWLNFIE EAKRIGATTL VINGRISIDS SKRFKFLKRL
GKNYFSPVDG FLLQDEVQKQ RFLSLGIPEH KLQVTGNIKT YVAAQTALHL ERETWRDRLR
LPTDSKLVIL GSMHRSDAGK WLPVVQKLIK EGVSVLWVPR HVEKTKDVEE SLHRLHIPYG
LWSRGANFSY VPVVVVDEIG LLKQLYVAGD LAFVGGTFDP KIGGHNLLEP LQCEVPLIFG
PHITSQSELA QRLLLSGAGL CLDEIEPIID TVSFLLNNQE VREAYVQKGK VFVKAETASF
DRTWRALKSY IPLYKNS
