RGTD_RHIL3
ID RGTD_RHIL3 Reviewed; 473 AA.
AC Q1MLH5;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Lipid A galacturonosyltransferase RgtD {ECO:0000305|PubMed:22110131};
DE Short=Lipid A GalA transferase RgtD {ECO:0000305|PubMed:22110131};
DE EC=2.4.1.- {ECO:0000305|PubMed:22110131};
DE AltName: Full=Galacturonic acid transferase RgtD {ECO:0000303|PubMed:22110131};
DE Short=GalAT RgtD {ECO:0000303|PubMed:22110131};
GN Name=rgtD {ECO:0000303|PubMed:22110131};
GN OrderedLocusNames=RL0684 {ECO:0000312|EMBL:CAK06178.1};
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 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 lipid A moiety. Catalyzes the transfer of a galacturonic acid (GalA)
CC residue to the 4'-position of 4'-dephosphorylated lipid A, using
CC dodecaprenyl phosphate-GalA as the donor substrate. Acts before the
CC other GalA transferases RgtA, RgtB and RgtC.
CC {ECO:0000269|PubMed:22110131}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000269|PubMed:22110131}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene produce lipid A that
CC lacks any detectable GalA. Inactivation of this gene also results in a
CC product that is affected in the addition of GalA to all positions in
CC the LPS core oligosaccharide, possibly by acting as a less than an
CC optimal substrate for RgtA, RgtB and RgtC. The mutant strains are more
CC susceptible to deoxycholic acid and to the polycationic antimicrobial
CC peptide PmxB when compared with the parent strain.
CC {ECO:0000269|PubMed:22110131}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM236080; CAK06178.1; -; Genomic_DNA.
DR RefSeq; WP_011650458.1; NC_008380.1.
DR AlphaFoldDB; Q1MLH5; -.
DR SMR; Q1MLH5; -.
DR STRING; 216596.RL0684; -.
DR EnsemblBacteria; CAK06178; CAK06178; RL0684.
DR KEGG; rle:RL0684; -.
DR eggNOG; COG1807; Bacteria.
DR HOGENOM; CLU_016165_3_0_5; -.
DR OMA; EAQYWFW; -.
DR OrthoDB; 854536at2; -.
DR UniPathway; UPA00973; -.
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:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR038731; RgtA/B/C-like.
DR Pfam; PF13231; PMT_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycosyltransferase; Lipid A biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Lipopolysaccharide biosynthesis;
KW Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..473
FT /note="Lipid A galacturonosyltransferase RgtD"
FT /id="PRO_0000436512"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 473 AA; 52334 MW; 2EFE619F8DBF2448 CRC64;
MSPRSGLLIV LGFTLWRVVM LNFDATDFFV DEAQYWFWSQ NLDLGYYSKP PMIAWVIRAM
TELSGSNAIY WIRLLGPLIH MAAALVLMKT AKRFVGPEIE GWTGATYITL PGVALSSVFF
STDVILLFFI AIALLAYFGL TQRRSVGLAL VMGLGVGLAF LTKYAVLFVV PGGAIALLLI
PAARIAVRDV IIAVAVAAVV ALPNLWWNLQ HDNTTVRHTQ DIAHWSELGI NLRRGLEFFA
AQFGVVGPII FFAMLWAVYR MIRGRSDDRE KMLVWLSMPV VLLITLQATV AKAYANWAVT
AYVAGTILAV WLLYLKWPKG LRLSLTINGI ASLLFPLATI FPHQLLLPNG DALMKRYLGR
AEVSREAAAL ATQAGTDIIV TDNRDMVADL FYTLRDASYR IYARAPAGLP ESYYEQEFAL
PADITGKVLF LTDGAFTCAT ETPEVLKNWQ PTEGNYKGKT LSIYKVSATC LAP
