RFAG_ECOLI
ID RFAG_ECOLI Reviewed; 374 AA.
AC P25740; Q2M7U5;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Lipopolysaccharide core biosynthesis protein RfaG;
DE EC=2.4.-.-;
DE AltName: Full=Glucosyltransferase I;
GN Name=rfaG; Synonyms=pcsA, waaG; OrderedLocusNames=b3631, JW3606;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1732225; DOI=10.1128/jb.174.3.930-934.1992;
RA Parker C.T., Pradel E., Schnaitman C.A.;
RT "Identification and sequences of the lipopolysaccharide core biosynthetic
RT genes rfaQ, rfaP, and rfaG of Escherichia coli K-12.";
RL J. Bacteriol. 174:930-934(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-217.
RX PubMed=1447141; DOI=10.1128/jb.174.23.7750-7756.1992;
RA Clementz T.;
RT "The gene coding for 3-deoxy-manno-octulosonic acid transferase and the
RT rfaQ gene are transcribed from divergently arranged promoters in
RT Escherichia coli.";
RL J. Bacteriol. 174:7750-7756(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
RX PubMed=7988890; DOI=10.1016/0378-1097(94)90295-x;
RA Pilipcinec E., Huisman T.T., Willemsen P.T., Appelmelk B.J., Graaf F.K.,
RA Oudega B.;
RT "Identification by Tn10 transposon mutagenesis of host factors involved in
RT the biosynthesis of K99 fimbriae of Escherichia coli: effect of LPS core
RT mutations.";
RL FEMS Microbiol. Lett. 123:201-206(1994).
CC -!- FUNCTION: Involved in the addition of the first glucose residue to the
CC lipopolysaccharide core.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; M80599; AAA24082.1; -; Genomic_DNA.
DR EMBL; M86305; AAA03743.2; -; Genomic_DNA.
DR EMBL; U00039; AAB18608.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76655.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77661.1; -; Genomic_DNA.
DR EMBL; S75736; AAD43826.1; -; Genomic_DNA.
DR PIR; B42595; B42595.
DR RefSeq; NP_418088.1; NC_000913.3.
DR RefSeq; WP_000634283.1; NZ_LN832404.1.
DR PDB; 2IV7; X-ray; 1.60 A; A=1-374.
DR PDB; 2IW1; X-ray; 1.50 A; A=1-374.
DR PDB; 2N58; NMR; -; A=103-132.
DR PDBsum; 2IV7; -.
DR PDBsum; 2IW1; -.
DR PDBsum; 2N58; -.
DR AlphaFoldDB; P25740; -.
DR BMRB; P25740; -.
DR SMR; P25740; -.
DR BioGRID; 4260869; 275.
DR IntAct; P25740; 10.
DR STRING; 511145.b3631; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR jPOST; P25740; -.
DR PaxDb; P25740; -.
DR PRIDE; P25740; -.
DR EnsemblBacteria; AAC76655; AAC76655; b3631.
DR EnsemblBacteria; BAE77661; BAE77661; BAE77661.
DR GeneID; 948149; -.
DR KEGG; ecj:JW3606; -.
DR KEGG; eco:b3631; -.
DR PATRIC; fig|1411691.4.peg.3075; -.
DR EchoBASE; EB1315; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_009583_44_2_6; -.
DR InParanoid; P25740; -.
DR OMA; YRRWGRY; -.
DR PhylomeDB; P25740; -.
DR BioCyc; EcoCyc:EG11339-MON; -.
DR BioCyc; MetaCyc:EG11339-MON; -.
DR BRENDA; 2.4.1.B64; 2026.
DR UniPathway; UPA00958; -.
DR EvolutionaryTrace; P25740; -.
DR PRO; PR:P25740; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008919; F:lipopolysaccharide glucosyltransferase I activity; IDA:EcoCyc.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IMP:EcoCyc.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Lipopolysaccharide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..374
FT /note="Lipopolysaccharide core biosynthesis protein RfaG"
FT /id="PRO_0000080305"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2IW1"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:2IW1"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:2IW1"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 61..78
FT /evidence="ECO:0007829|PDB:2IW1"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:2IW1"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:2IW1"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:2IW1"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:2IW1"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:2IW1"
FT TURN 206..210
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:2IW1"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 240..248
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:2IW1"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 264..270
FT /evidence="ECO:0007829|PDB:2IW1"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 285..293
FT /evidence="ECO:0007829|PDB:2IW1"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:2IW1"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:2IW1"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 338..354
FT /evidence="ECO:0007829|PDB:2IW1"
FT HELIX 360..369
FT /evidence="ECO:0007829|PDB:2IW1"
SQ SEQUENCE 374 AA; 42284 MW; 7F20AE577CBB80C2 CRC64;
MIVAFCLYKY FPFGGLQRDF MRIASTVAAR GHHVRVYTQS WEGDCPKAFE LIQVPVKSHT
NHGRNAEYYA WVQNHLKEHP ADRVVGFNKM PGLDVYFAAD VCYAEKVAQE KGFLYRLTSR
YRHYAAFERA TFEQGKSTKL MMLTDKQIAD FQKHYQTEPE RFQILPPGIY PDRKYSEQIP
NSREIYRQKN GIKEQQNLLL QVGSDFGRKG VDRSIEALAS LPESLRHNTL LFVVGQDKPR
KFEALAEKLG VRSNVHFFSG RNDVSELMAA ADLLLHPAYQ EAAGIVLLEA ITAGLPVLTT
AVCGYAHYIA DANCGTVIAE PFSQEQLNEV LRKALTQSPL RMAWAENARH YADTQDLYSL
PEKAADIITG GLDG
