RGTE_RHIL3
ID RGTE_RHIL3 Reviewed; 338 AA.
AC Q1MJ95;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Dodecaprenyl-phosphate galacturonate synthase {ECO:0000305|PubMed:22110131};
DE Short=Dod-P-GalA synthase {ECO:0000305|PubMed:22110131};
DE EC=2.4.1.- {ECO:0000305|PubMed:22110131};
DE AltName: Full=Dodecaprenyl-phosphate galacturonosyltransferase RgtE {ECO:0000305|PubMed:22110131};
DE AltName: Full=Galacturonic acid transferase RgtE {ECO:0000303|PubMed:22110131};
DE Short=GalA transferase RgtE {ECO:0000303|PubMed:22110131};
DE Short=GalAT RgtE {ECO:0000303|PubMed:22110131};
GN Name=rgtE {ECO:0000303|PubMed:22110131};
GN OrderedLocusNames=RL1470 {ECO:0000312|EMBL:CAK06965.1};
OS Rhizobium leguminosarum bv. viciae (strain 3841).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=216596;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3841;
RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT components.";
RL Genome Biol. 7:R34.1-R34.20(2006).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RC STRAIN=3841;
RX PubMed=22110131; DOI=10.1074/jbc.m111.311571;
RA Brown D.B., Forsberg L.S., Kannenberg E.L., Carlson R.W.;
RT "Characterization of galacturonosyl transferase genes rgtA, rgtB, rgtC,
RT rgtD, and rgtE responsible for lipopolysaccharide synthesis in nitrogen-
RT fixing endosymbiont Rhizobium leguminosarum: lipopolysaccharide core and
RT lipid galacturonosyl residues confer membrane stability.";
RL J. Biol. Chem. 287:935-949(2012).
CC -!- FUNCTION: Glycosyltransferase that catalyzes the synthesis of
CC dodecaprenyl-phosphate galacturonate (Dod-P-GalA), likely from UDP-GalA
CC and dodecaprenyl-phosphate. Dod-P-GalA is the lipid donor required for
CC GalA transfer to lipopolysaccharide (LPS) specific residues catalyzed
CC by the GalA transferases RgtA, RgtB, RgtC and RgtD.
CC {ECO:0000269|PubMed:22110131}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,nona-cis-dodecaprenyl phosphate + UDP-alpha-D-
CC galacturonate = beta-D-galacturonosyl di-trans,nona-cis-dodecaprenyl
CC phosphate + UDP; Xref=Rhea:RHEA:26006, ChEBI:CHEBI:57635,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:142217, ChEBI:CHEBI:142345;
CC Evidence={ECO:0000305|PubMed:22110131};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Lack of Dod-P-GalA in total lipid extracts. The
CC membranes of the rgtE mutant are unable to provide the substrate for
CC heterologously expressed RgtA activity. Cells lacking this gene produce
CC an LPS that is devoid of GalA. They are also more susceptible to
CC deoxycholic acid and to the polycationic antimicrobial peptide PmxB
CC when compared with the parent strain. Pea plants inoculated with rgtE-
CC deficient mutant show discoloration and wilting of the early leaves.
CC {ECO:0000269|PubMed:22110131}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AM236080; CAK06965.1; -; Genomic_DNA.
DR RefSeq; WP_003546851.1; NC_008380.1.
DR AlphaFoldDB; Q1MJ95; -.
DR SMR; Q1MJ95; -.
DR STRING; 216596.RL1470; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblBacteria; CAK06965; CAK06965; RL1470.
DR KEGG; rle:RL1470; -.
DR eggNOG; COG0463; Bacteria.
DR HOGENOM; CLU_033536_0_0_5; -.
DR OMA; DLVSGWK; -.
DR OrthoDB; 1064289at2; -.
DR Proteomes; UP000006575; 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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0030259; P:lipid glycosylation; IMP:UniProtKB.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycosyltransferase; Lipopolysaccharide biosynthesis;
KW Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..338
FT /note="Dodecaprenyl-phosphate galacturonate synthase"
FT /id="PRO_0000436513"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 338 AA; 37800 MW; E1F9798E0715D4D4 CRC64;
MQTTVEPIRG TNDPVQSLEL SLVVPIFNEE QSVGPLVERV AAAMVSYPHR WELILVDDGS
TDATLVNARK YVGREGLALR IVELQRNFGQ TAAMQAGIDT ARGRLIATMD GDLQNDPKDI
PSMVSELERR ELDLLVGWRK NRKDGLFLRK IPSWCANYLI GRITGVKLHD YGCSLKIYRA
SIIKQVKLMG EMHRFIPAWV AGVVPSSRIG EMAVTHHARE HGVSKYGISR TFRVILDLLS
VMFFMRYKAR PGHFFGSLGL GLGALAMLIL LYLGFDKFIL GNDIGTRPML MVGVVLLLSS
VQMITTGILA EMIARTYYRD DASPNYIVRQ IFDDQSQA
