KDTA_CHLMU
ID KDTA_CHLMU Reviewed; 430 AA.
AC Q9PKI5;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 EC=2.4.99.14;
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;
GN Name=waaA; Synonyms=kdtA; OrderedLocusNames=TC_0480;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
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).
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:0000250|UniProtKB:Q46222}.
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 -!- 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 -!- 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE002160; AAF39326.1; -; Genomic_DNA.
DR PIR; F81698; F81698.
DR AlphaFoldDB; Q9PKI5; -.
DR SMR; Q9PKI5; -.
DR STRING; 243161.TC_0480; -.
DR CAZy; GT30; Glycosyltransferase Family 30.
DR EnsemblBacteria; AAF39326; AAF39326; TC_0480.
DR KEGG; cmu:TC_0480; -.
DR eggNOG; COG1519; Bacteria.
DR HOGENOM; CLU_036146_2_1_0; -.
DR OMA; FIKYEFW; -.
DR OrthoDB; 1163086at2; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000000800; 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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Lipopolysaccharide biosynthesis;
KW Membrane; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..430
FT /note="3-deoxy-D-manno-octulosonic acid transferase"
FT /id="PRO_0000080282"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 274..275
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT BINDING 314..316
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT BINDING 341..344
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT SITE 137
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 215
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 430 AA; 48858 MW; FCB828B9FA796C8A CRC64;
MRRWLTSRLY DAFLVAAFLA AAPRIFYKVV FHGKYINSWK IRFGVEKPQV KGEGPLVWFH
GASVGEVSLL EPLLKKWRQE FPDWRFVVTA CSEAGVYTAQ RLYAPLGATV FVLPLDLSCI
INPVVRSLSP QVVIFSEGDC WLHFLMGAKK LGAKAFLING KLSENSCKRF AFLKRLGRSY
FAPLDLLVLQ DKVYKQRFMQ IGIPEDKIQI SGNLKTFIET ETSINNRSLW RKKLKLSPSD
RLIVLGSMHP KDVEVWADVA QHFNKFSTKI LWVPRHLEKL KEHARLLEKA GISFGLWSKE
DSLLQYDSLI VDAMGILKDL YSAADLAFVG GTFDPLVGGH NLLEPLQKEV PLMFGPHIHS
QSVLAELLRT KEVGVSVDKE NLLEAVENLL EDEKKRQAYI ERGKSFLKNA GTSFEHTWEI
LKSQIACIKI
