RGTC_RHIL3
ID RGTC_RHIL3 Reviewed; 497 AA.
AC Q1MJ94; Q20DQ2;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Lipopolysaccharide core galacturonosyltransferase RgtC {ECO:0000303|PubMed:16497674};
DE Short=LPS core GalA transferase RgtC {ECO:0000303|PubMed:16497674};
DE EC=2.4.1.- {ECO:0000269|PubMed:16497671};
DE AltName: Full=Dodecaprenyl phosphate-beta-galacturonate:lipopolysaccharide core alpha-galacturonosyltransferase RgtC {ECO:0000305|PubMed:22110131};
DE Short=Dodecaprenyl-P-GalA:LPS core galacturonosyltransferase RgtC {ECO:0000305|PubMed:16497671, ECO:0000305|PubMed:22110131};
DE AltName: Full=Galacturonic acid transferase RgtC {ECO:0000303|PubMed:22110131};
DE Short=GalAT RgtC {ECO:0000303|PubMed:22110131};
GN Name=rgtC {ECO:0000303|PubMed:16497674, ECO:0000312|EMBL:ABC02171.1};
GN OrderedLocusNames=RL1471 {ECO:0000312|EMBL:CAK06966.1};
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:ABC02171.1};
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 mannose residue of the LPS inner core,
CC using dodecaprenyl phosphate-GalA as the donor substrate. Seems to act
CC after the other GalA transferases RgtA and RgtB.
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 elimination of the addition
CC of GalA to the Man residue, but does not affect the addition of GalA to
CC the 4- and 5-positions of outer Kdo. The mutant cells are also 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; DQ298018; ABC02171.1; -; Genomic_DNA.
DR EMBL; AM236080; CAK06966.1; -; Genomic_DNA.
DR RefSeq; WP_011651168.1; NC_008380.1.
DR AlphaFoldDB; Q1MJ94; -.
DR STRING; 216596.RL1471; -.
DR CAZy; GT83; Glycosyltransferase Family 83.
DR EnsemblBacteria; CAK06966; CAK06966; RL1471.
DR KEGG; rle:RL1471; -.
DR eggNOG; COG1807; Bacteria.
DR HOGENOM; CLU_039820_0_0_5; -.
DR OMA; IHERWLD; -.
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..497
FT /note="Lipopolysaccharide core galacturonosyltransferase
FT RgtC"
FT /id="PRO_0000436511"
FT TRANSMEM 14..34
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 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 497 AA; 54597 MW; EB8BF2ED44FB5E06 CRC64;
MLERITRSIT SASIFLAAYF LLNIALRIAL PHTLDLDEAE QSFYSQYLLA GYGPQPPFYN
WIQYAIVSVT GISMWVLSVP KNIILFGCYL FYGLAAREVL KSRSLAALAM LSLITLPQVG
LMAQRELTHT VALLFATSLF LFGFFRTLRQ PTIGSYLLIG IATGIGLISK YNFAILPFAA
LIAVLPEREW RSRLIDWRLL PAAVLAILIV LPHALWLPDN LASASAPTLE RMTAEHLAPA
GLPRIGQGLL SLVIAVLGFV ALPIVLIAAA FRRDFFRALS SSSPMIRVIE RMMVISLLAF
VGVVLFAGAS DIHERWLDPC LLVLLIYLFL KLETADIDLS AGLARFRPVV PVFMVVILSI
LLFRIVGIQY IGTYTRTNVP FSGYVAELTA TRKPVLIVAG TKFIAGNMRL QFPDVPVVIP
FFPGPGVPEY ADAKGPVLVI WRGETADDPT ISPGFANDLV KSGIHLPELK TLTLPYLFGD
GKRSFSIGYS WVEGGAK
