KDTA_CHLT2
ID KDTA_CHLT2 Reviewed; 431 AA.
AC B0B9V8; P0C0Z9; Q46394; Q46395; Q46396; Q46401; Q57440;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
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:1382060};
DE EC=2.4.99.13 {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:1382060};
DE EC=2.4.99.14 {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:1382060};
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=CTL0460;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP MULTIFUNCTIONALITY.
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=1382060; DOI=10.1016/s0021-9258(19)37018-8;
RA Belunis C.J., Mdluli K.E., Raetz C.R.H., Nano F.E.;
RT "A novel 3-deoxy-D-manno-octulosonic acid transferase from Chlamydia
RT trachomatis required for expression of the genus-specific epitope.";
RL J. Biol. Chem. 267:18702-18707(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND TRIFUNCTIONALITY.
RC STRAIN=L2;
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:1382060}.
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:1382060};
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:1382060};
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:1382060};
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; M64618; AAA23139.1; -; Genomic_DNA.
DR EMBL; Z22659; CAA80374.1; -; Genomic_DNA.
DR EMBL; AM884176; CAP03899.1; -; Genomic_DNA.
DR PIR; S41168; S41168.
DR RefSeq; WP_009873639.1; NC_010287.1.
DR RefSeq; YP_001654536.1; NC_010287.1.
DR AlphaFoldDB; B0B9V8; -.
DR SMR; B0B9V8; -.
DR CAZy; GT30; Glycosyltransferase Family 30.
DR EnsemblBacteria; CAP03899; CAP03899; CTL0460.
DR KEGG; ctb:CTL0460; -.
DR PATRIC; fig|471472.4.peg.495; -.
DR HOGENOM; CLU_036146_2_1_0; -.
DR OMA; FIKYEFW; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000000795; 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..431
FT /note="3-deoxy-D-manno-octulosonic acid transferase"
FT /id="PRO_0000391796"
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 CONFLICT 301
FT /note="G -> A (in Ref. 1; AAA23139 and 2; CAA80374)"
FT /evidence="ECO:0000305"
FT CONFLICT 397..431
FT /note="RQAYIEKGKSFLKQEENSFQQTWEILKSQITCMKI -> PPSLY (in
FT Ref. 1; AAA23139)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 49497 MW; 664A7504F4E749AC 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 APLMFGPYIY
SQSVLAERLR EKEAGLSVNK ETLLDVVTDL LQNEKNRQAY IEKGKSFLKQ EENSFQQTWE
ILKSQITCMK I
