RGTA_RHIL3
ID RGTA_RHIL3 Reviewed; 499 AA.
AC Q1MJ96; Q20DQ4;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Lipopolysaccharide core galacturonosyltransferase RgtA {ECO:0000303|PubMed:16497674};
DE Short=LPS core GalA transferase RgtA {ECO:0000303|PubMed:16497674};
DE EC=2.4.1.- {ECO:0000269|PubMed:16497671};
DE AltName: Full=Dodecaprenyl phosphate-beta-galacturonate:lipopolysaccharide core alpha-galacturonosyltransferase RgtA {ECO:0000305|PubMed:22110131};
DE Short=Dodecaprenyl-P-GalA:LPS core galacturonosyltransferase RgtA {ECO:0000305|PubMed:16497671, ECO:0000305|PubMed:22110131};
DE AltName: Full=Galacturonic acid transferase RgtA {ECO:0000303|PubMed:22110131};
DE Short=GalAT RgtA {ECO:0000303|PubMed:22110131};
GN Name=rgtA {ECO:0000303|PubMed:16497674, ECO:0000312|EMBL:ABC02169.1};
GN OrderedLocusNames=RL1469 {ECO:0000312|EMBL:CAK06964.1};
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP PATHWAY.
RC STRAIN=3841 {ECO:0000312|EMBL:ABC02169.1};
RX PubMed=16497674; DOI=10.1074/jbc.m513864200;
RA Kanjilal-Kolar S., Basu S.S., Kanipes M.I., Guan Z., Garrett T.A.,
RA Raetz C.R.H.;
RT "Expression cloning of three Rhizobium leguminosarum lipopolysaccharide
RT core galacturonosyltransferases.";
RL J. Biol. Chem. 281:12865-12878(2006).
RN [2]
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=3841;
RX PubMed=16497671; DOI=10.1074/jbc.m513865200;
RA Kanjilal-Kolar S., Raetz C.R.;
RT "Dodecaprenyl phosphate-galacturonic acid as a donor substrate for
RT lipopolysaccharide core glycosylation in Rhizobium leguminosarum.";
RL J. Biol. Chem. 281:12879-12887(2006).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
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: Involved in the modification of the lipopolysaccharide (LPS)
CC inner core. Catalyzes the transfer of a galacturonic acid (GalA)
CC residue to the 4-position of the outer Kdo (3-deoxy-D-manno-octulosonic
CC acid) residue of the LPS inner core, using dodecaprenyl phosphate-GalA
CC as the donor substrate. GalA addition by RgtA is required for RgtB
CC activity. {ECO:0000269|PubMed:16497671, ECO:0000269|PubMed:16497674,
CC ECO:0000269|PubMed:22110131}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC {ECO:0000269|PubMed:22110131, ECO:0000305|PubMed:16497674}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:16497671,
CC ECO:0000305|PubMed:16497674}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene produce a normal lipid A
CC structure with GalA at the 4'-position but a modified LPS core
CC structure as this gene deletion results in the complete absence of GalA
CC on both the 4- and 5-positions of the outer Kdo residue and incomplete
CC addition of GalA to the Man residue. The mutant cells are also more
CC susceptible to deoxycholic acid when compared with the parent strain,
CC and more resistant to the polycationic antimicrobial peptide PmxB.
CC {ECO:0000269|PubMed:22110131}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 83 family.
CC {ECO:0000305}.
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DR EMBL; DQ298016; ABC02169.1; -; Genomic_DNA.
DR EMBL; AM236080; CAK06964.1; -; Genomic_DNA.
DR RefSeq; WP_011651167.1; NC_008380.1.
DR AlphaFoldDB; Q1MJ96; -.
DR SMR; Q1MJ96; -.
DR STRING; 216596.RL1469; -.
DR CAZy; GT83; Glycosyltransferase Family 83.
DR PRIDE; Q1MJ96; -.
DR EnsemblBacteria; CAK06964; CAK06964; RL1469.
DR KEGG; rle:RL1469; -.
DR eggNOG; COG1807; Bacteria.
DR HOGENOM; CLU_039820_0_0_5; -.
DR OMA; YNFALMP; -.
DR OrthoDB; 854536at2; -.
DR UniPathway; UPA00958; -.
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:0008378; F:galactosyltransferase activity; IDA:CACAO.
DR GO; GO:0016758; F:hexosyltransferase activity; IMP:UniProtKB.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR038731; RgtA/B/C-like.
DR Pfam; PF13231; PMT_2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Glycosyltransferase;
KW Lipopolysaccharide biosynthesis; Membrane; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..499
FT /note="Lipopolysaccharide core galacturonosyltransferase
FT RgtA"
FT /id="PRO_0000436509"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 499 AA; 54261 MW; 818A47F74B248CE5 CRC64;
MLERATRTIK TAGLLLAAYF VLNIVLRIVL PHSLELDEAE QSFFSQYLLA GYGPQPPFYN
WMQYAVVSVT GISIGALIVP KNILLFLSYL FYGLAGRRVL KDEALAAVGM LALITLPQVS
YMAQQDLTHT TALLFASSLF LYGFFRTLDR PDMASYLLLG LATGIGLISK YNFALMPVVA
LIAILPDAEW RRRALDWRML AAITVALVIV LPHAVWLQGN LAFASSDTLV KMAAGSEPAG
AVRIGKGLLA FLVAIIAFAA LPVVIFAATF RRDFVRALSA GNRWTGMMER MMLASLAGIA
LIVLFTGSTT VRERWLDPFL LVLPIYFLAK MQAAGLDLSA GLRRFRPVLP VLMACVLIAL
GFRVVGAGLI GTYSRPNVPM AGFAREMTRQ AEPALVIASD TYIGGNMRLQ FPDVPVVIPD
FPAPGIPAYA EAKGPVLIVW RGKKTATAAD AVMPERFSSA LTAAGIALQE IGSLSLPYYF
GRQGDNFALG YAWVRPETR
