WBPD_PSEAE
ID WBPD_PSEAE Reviewed; 191 AA.
AC G3XD01; P72135;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronate N-acetyltransferase;
DE Short=UDP-D-GlcNAc3NA N-acetyltransferase;
DE EC=2.3.1.201;
DE AltName: Full=UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronic acid 3-N-acetyltransferase;
GN Name=wbpD {ECO:0000312|EMBL:AAG06544.1}; OrderedLocusNames=PA3156;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC45855.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000312|EMBL:AAC45855.1};
RX PubMed=8939432; DOI=10.1046/j.1365-2958.1996.1351503.x;
RA Burrows L.L., Charter D.F., Lam J.S.;
RT "Molecular characterization of the Pseudomonas aeruginosa serotype O5
RT (PAO1) B-band lipopolysaccharide gene cluster.";
RL Mol. Microbiol. 22:481-495(1996).
RN [2] {ECO:0000312|EMBL:AAG06544.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3] {ECO:0000305}
RP FUNCTION, ROLE IN B-BAND O-ANTIGEN BIOSYNTHESIS, PATHWAY, SUBUNIT,
RP IDENTIFICATION BY MASS SPECTROMETRY, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF LYS-136.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000269|PubMed:16102001};
RX PubMed=16102001; DOI=10.1111/j.1365-2958.2004.04767.x;
RA Wenzel C.Q., Daniels C., Keates R.A., Brewer D., Lam J.S.;
RT "Evidence that WbpD is an N-acetyltransferase belonging to the hexapeptide
RT acyltransferase superfamily and an important protein for O-antigen
RT biosynthesis in Pseudomonas aeruginosa PAO1.";
RL Mol. Microbiol. 57:1288-1303(2005).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000269|PubMed:19348502};
RX PubMed=19348502; DOI=10.1021/bi900186u;
RA Larkin A., Imperiali B.;
RT "Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the
RT Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa
RT PAO1.";
RL Biochemistry 48:5446-5455(2009).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000269|PubMed:19282284};
RX PubMed=19282284; DOI=10.1074/jbc.m808583200;
RA Westman E.L., McNally D.J., Charchoglyan A., Brewer D., Field R.A.,
RA Lam J.S.;
RT "Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway
RT for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
RT in Pseudomonas aeruginosa.";
RL J. Biol. Chem. 284:11854-11862(2009).
CC -!- FUNCTION: Plays a role in the biosynthesis of B-band O antigen for
CC serotype O5. Catalyzes the transfer of an acetyl group to the C-3 amino
CC position of UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
CC (UDP-D-GlcNAc3NA). {ECO:0000269|PubMed:16102001,
CC ECO:0000269|PubMed:19282284, ECO:0000269|PubMed:19348502}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-
CC glucuronate = CoA + H(+) + UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-
CC glucuronate; Xref=Rhea:RHEA:33587, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58745,
CC ChEBI:CHEBI:62245; EC=2.3.1.201;
CC Evidence={ECO:0000269|PubMed:19282284, ECO:0000269|PubMed:19348502};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=107 uM for UDP-D-GlcNAc3NA {ECO:0000269|PubMed:19348502};
CC Note=kcat is 2900 min(-1).;
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000269|PubMed:16102001,
CC ECO:0000269|PubMed:19282284, ECO:0000269|PubMed:19348502,
CC ECO:0000269|PubMed:8939432}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:16102001}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are incapable of
CC producing either long-chain B-band O antigen (> or = 2 repeating units)
CC or semi-rough LPS (lipid A-core + one O antigen repeat).
CC {ECO:0000269|PubMed:16102001}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC45855.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U50396; AAC45855.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE004091; AAG06544.1; -; Genomic_DNA.
DR PIR; F83251; F83251.
DR RefSeq; NP_251846.1; NC_002516.2.
DR RefSeq; WP_003113426.1; NZ_QZGE01000023.1.
DR AlphaFoldDB; G3XD01; -.
DR SMR; G3XD01; -.
DR STRING; 208964.PA3156; -.
DR PaxDb; G3XD01; -.
DR DNASU; 882593; -.
DR EnsemblBacteria; AAG06544; AAG06544; PA3156.
DR GeneID; 882593; -.
DR KEGG; pae:PA3156; -.
DR PATRIC; fig|208964.12.peg.3300; -.
DR PseudoCAP; PA3156; -.
DR HOGENOM; CLU_051638_9_1_6; -.
DR InParanoid; G3XD01; -.
DR OMA; QIGWMSE; -.
DR PhylomeDB; G3XD01; -.
DR BioCyc; MetaCyc:MON-17575; -.
DR BioCyc; PAER208964:G1FZ6-3216-MON; -.
DR BRENDA; 2.3.1.201; 5087.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016407; F:acetyltransferase activity; EXP:PseudoCAP.
DR GO; GO:0016746; F:acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009243; P:O antigen biosynthetic process; IDA:UniProtKB.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IDA:PseudoCAP.
DR GO; GO:0070206; P:protein trimerization; IDA:UniProtKB.
DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; EXP:PseudoCAP.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 3.
DR SUPFAM; SSF51161; SSF51161; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell wall biogenesis/degradation;
KW Lipopolysaccharide biosynthesis; Reference proteome; Repeat; Transferase.
FT CHAIN 1..191
FT /note="UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronate N-
FT acetyltransferase"
FT /id="PRO_0000419619"
FT MUTAGEN 136
FT /note="K->A: Reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:16102001"
FT MUTAGEN 136
FT /note="K->R: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:16102001"
FT CONFLICT 128
FT /note="V -> L (in Ref. 1; AAC45855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 191 AA; 20562 MW; 65F76DFA1366F195 CRC64;
MSYYQHPSAI VDDGAQIGSD SRVWHFVHIC AGARIGAGVS LGQNVFVGNK VVIGDRCKIQ
NNVSVYDNVT LEEGVFCGPS MVFTNVYNPR SLIERKDQYR NTLVKKGATL GANCTIVCGV
TIGEYAFVGA GAVINKNVPS YALMVGVPAR QIGWMSEFGE QLQLNEQGEA VCSHSGARYV
LNGKILSKVD V
