RGTB_RHIL3
ID RGTB_RHIL3 Reviewed; 494 AA.
AC Q1MJ97; Q20DQ3;
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 RgtB {ECO:0000303|PubMed:16497674};
DE Short=LPS core GalA transferase RgtB {ECO:0000303|PubMed:16497674};
DE EC=2.4.1.- {ECO:0000269|PubMed:16497671};
DE AltName: Full=Dodecaprenyl phosphate-beta-galacturonate:lipopolysaccharide core alpha-galacturonosyltransferase RgtB {ECO:0000305|PubMed:22110131};
DE Short=Dodecaprenyl-P-GalA:LPS core galacturonosyltransferase RgtB {ECO:0000305|PubMed:16497671, ECO:0000305|PubMed:22110131};
DE AltName: Full=Galacturonic acid transferase RgtB {ECO:0000303|PubMed:22110131};
DE Short=GalAT RgtB {ECO:0000303|PubMed:22110131};
GN Name=rgtB {ECO:0000303|PubMed:16497674, ECO:0000312|EMBL:ABC02170.1};
GN OrderedLocusNames=RL1468 {ECO:0000312|EMBL:CAK06963.1};
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:ABC02170.1};
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 5-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. Acts after the other GalA transferase RgtA.
CC {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 addition of GalA to the
CC 4- but not the 5-position of the outer Kdo and nearly complete addition
CC of GalA to the Man residue. The mutant cells are also more susceptible
CC to deoxycholic acid when compared with the parent strain, and more
CC 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; DQ298017; ABC02170.1; -; Genomic_DNA.
DR EMBL; AM236080; CAK06963.1; -; Genomic_DNA.
DR RefSeq; WP_011651166.1; NC_008380.1.
DR AlphaFoldDB; Q1MJ97; -.
DR SMR; Q1MJ97; -.
DR STRING; 216596.RL1468; -.
DR CAZy; GT83; Glycosyltransferase Family 83.
DR EnsemblBacteria; CAK06963; CAK06963; RL1468.
DR KEGG; rle:RL1468; -.
DR eggNOG; COG1807; Bacteria.
DR HOGENOM; CLU_039820_0_0_5; -.
DR OMA; THIRAKW; -.
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: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..494
FT /note="Lipopolysaccharide core galacturonosyltransferase
FT RgtB"
FT /id="PRO_0000436510"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
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 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 494 AA; 54015 MW; 409E2CF77A7C5B1F CRC64;
MTESNRRDIS WIFALLAAYF VLQVGVRLAT SHSLDLDEAE QAFRSQWLAA GYGPQPPFYN
WLQYTVFQFA GVSLTALSIV KNLLLFISYL LYGLTARLVL RDKALVAIAT LGLLTIPQMA
FEMQRDLTHT VAVFFSASIF FYGFIRSLKQ PSLASYLIAG IGIGFGLLAK YNFAILPAAA
LIAALSDARL RPRIFDWRLG LTAAVALVIT LPHLFWLKDN LDFATARTLE KMTASGDASY
LTQVAMGVSS LALAIISFAA LTVAVFAIVF GKSLRPALGS GSEWTRLLER MMLVFLAGIL
LLIVFGGAAG IKDRWLVPML FILPLYFCLK IEAAGVETGK ALRRFIPVVA VIMIGVPAAL
YGSVAAARFT GHYERLNRPY AGMLEILRKQ AEPAAILAGD SLLAGNLRQD IPGVPILSAD
YPGFNPDLTS RRPLLLVWLL PKGGSEALPP DMAEWLQANL GTSAPEASVI DVPYFYGRGD
DRYRFGYAWV NQPG
