KDTA_CHLTR
ID KDTA_CHLTR Reviewed; 431 AA.
AC P0CE14; P0C0Z9; Q46394; Q46395; Q46396; Q46401; Q57440;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 54.
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;
DE AltName: Full=Trifunctional Kdo transferase;
GN Name=waaA; Synonyms=gseA, kdtA; OrderedLocusNames=CT_208;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B/Tw-5/OT, Ba/Apache-2, BOUR, and D/UW-3/Cx;
RX PubMed=7861960; DOI=10.1006/mpat.1994.1055;
RA Mamat U., Loebau S., Persson K., Brade H.;
RT "Nucleotide sequence variations within the lipopolysaccharide biosynthesis
RT gene gseA (Kdo transferase) among the Chlamydia trachomatis serovars.";
RL Microb. Pathog. 17:87-97(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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}.
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DR EMBL; Z22653; CAA80368.1; -; Genomic_DNA.
DR EMBL; Z22654; CAA80369.1; -; Genomic_DNA.
DR EMBL; Z22655; CAA80370.1; -; Genomic_DNA.
DR EMBL; Z22656; CAA80371.1; -; Genomic_DNA.
DR EMBL; AE001273; AAC67800.1; -; Genomic_DNA.
DR PIR; I40894; I40894.
DR PIR; I40897; I40897.
DR PIR; I40898; I40898.
DR PIR; S41168; S41168.
DR RefSeq; NP_219712.1; NC_000117.1.
DR RefSeq; WP_009871554.1; NC_000117.1.
DR AlphaFoldDB; P0CE14; -.
DR SMR; P0CE14; -.
DR STRING; 813.O172_01125; -.
DR CAZy; GT30; Glycosyltransferase Family 30.
DR EnsemblBacteria; AAC67800; AAC67800; CT_208.
DR GeneID; 884918; -.
DR KEGG; ctr:CT_208; -.
DR PATRIC; fig|272561.5.peg.223; -.
DR HOGENOM; CLU_036146_2_0_0; -.
DR InParanoid; P0CE14; -.
DR OMA; FIKYEFW; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043842; F:Kdo transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IBA:GO_Central.
DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
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; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..431
FT /note="3-deoxy-D-manno-octulosonic acid transferase"
FT /id="PRO_0000080284"
FT TRANSMEM 5..27
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT ACT_SITE 67
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 275..276
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT BINDING 315..317
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT BINDING 342..345
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT SITE 138
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 216
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT VARIANT 249
FT /note="M -> V (in strain: Tw-5/OT and APa-2)"
FT VARIANT 321
FT /note="I -> V (in strain: BOUR)"
SQ SEQUENCE 431 AA; 49497 MW; 69D5856B6B0019B5 CRC64;
MIRRWLTSRL YDAFLVCAFF VSAPRIFYKV FFHGKYIDSW KIRFGVQKPF VKGEGPLVWF
HGASVGEVSL LAPLLNRWRE EFPEWRFVVT TCSEAGVHTA RRLYESLGAT VFVLPLDLSC
IIKSVVRKLA PDIVIFSEGD CWLHFLTESK RLGAKAFLIN GKLSEHSCKR FSFLKRLGRN
YFAPLDLLIL QDELYKQRFM QIGISSDKIH VTGNMKTFIE SSLATNRRDF WRAKLQISSQ
DRLIVLGSMH PKDVEVWAEV VSHFHNSSTK ILWVPRHLEK LKEHAKLLEK AGILFGLWSQ
GASFRQYNSL IMDAMGVLKD IYSAADIAFV GGTFDPSVGG HNLLEPLQKE VPLMFGPYIY
SQSVLAEKLR EKEAGLSVNK ETLLDVVTDL LQNEKNRQAY IEKGKSFLKQ EENSFQQTWE
ILKSQITCMK I
