P25740 (RFAG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipopolysaccharide core biosynthesis protein RfaG
EC=2.4.-.-

Alternative name(s):
Glucosyltransferase I

Gene names

Name:	rfaG
Synonyms:	pcsA, waaG
Ordered Locus Names:	b3631, JW3606

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	374 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the addition of the first glucose residue to the lipopolysaccharide core.
Pathway	Bacterial outer membrane biogenesis; LPS core biosynthesis.
Sequence similarities	Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.

Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lipopolysaccharide core region biosynthetic process Inferred from genetic interaction PubMed 1348243. Source: EcoCyc
Molecular_function	lipopolysaccharide glucosyltransferase I activity Inferred from genetic interaction PubMed 1348243. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 374

374

Lipopolysaccharide core biosynthesis protein RfaG

PRO_0000080305

Secondary structure

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374

Helix Strand Turn

Details...

Beta strand

3 – 6

4

Beta strand

8 – 10

3

Helix

15 – 29

15

Beta strand

34 – 41

8

Beta strand

50 – 53

4

Helix

61 – 78

18

Beta strand

82 – 88

7

Beta strand

94 – 97

4

Helix

103 – 110

8

Helix

113 – 116

4

Helix

119 – 132

14

Beta strand

139 – 143

5

Helix

145 – 155

11

Helix

159 – 161

3

Beta strand

162 – 164

3

Helix

171 – 173

3

Helix

175 – 177

3

Helix

182 – 189

8

Beta strand

197 – 202

6

Turn

206 – 210

5

Helix

211 – 219

9

Helix

223 – 227

5

Beta strand

229 – 237

9

Helix

240 – 248

9

Helix

252 – 254

3

Beta strand

255 – 259

5

Helix

264 – 270

7

Beta strand

272 – 276

5

Helix

285 – 293

9

Beta strand

297 – 300

4

Turn

304 – 306

3

Helix

307 – 312

6

Beta strand

315 – 318

4

Helix

324 – 336

13

Helix

338 – 354

17

Helix

360 – 369

10

Sequences

	Sequence		Length	Mass (Da)
	P25740 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 7F20AE577CBB80C2	FASTA	374	42,284
	10 20 30 40 50 60 MIVAFCLYKY FPFGGLQRDF MRIASTVAAR GHHVRVYTQS WEGDCPKAFE LIQVPVKSHT 70 80 90 100 110 120 NHGRNAEYYA WVQNHLKEHP ADRVVGFNKM PGLDVYFAAD VCYAEKVAQE KGFLYRLTSR 130 140 150 160 170 180 YRHYAAFERA TFEQGKSTKL MMLTDKQIAD FQKHYQTEPE RFQILPPGIY PDRKYSEQIP 190 200 210 220 230 240 NSREIYRQKN GIKEQQNLLL QVGSDFGRKG VDRSIEALAS LPESLRHNTL LFVVGQDKPR 250 260 270 280 290 300 KFEALAEKLG VRSNVHFFSG RNDVSELMAA ADLLLHPAYQ EAAGIVLLEA ITAGLPVLTT 310 320 330 340 350 360 AVCGYAHYIA DANCGTVIAE PFSQEQLNEV LRKALTQSPL RMAWAENARH YADTQDLYSL 370 PEKAADIITG GLDG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and sequences of the lipopolysaccharide core biosynthetic genes rfaQ, rfaP, and rfaG of Escherichia coli K-12." Parker C.T., Pradel E., Schnaitman C.A. J. Bacteriol. 174:930-934(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R. Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The gene coding for 3-deoxy-manno-octulosonic acid transferase and the rfaQ gene are transcribed from divergently arranged promoters in Escherichia coli." Clementz T. J. Bacteriol. 174:7750-7756(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-217.
[6]	"Identification by Tn10 transposon mutagenesis of host factors involved in the biosynthesis of K99 fimbriae of Escherichia coli: effect of LPS core mutations." Pilipcinec E., Huisman T.T., Willemsen P.T., Appelmelk B.J., Graaf F.K., Oudega B. FEMS Microbiol. Lett. 123:201-206(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M80599 Genomic DNA. Translation: AAA24082.1.
M86305 Genomic DNA. Translation: AAA03743.2.
U00039 Genomic DNA. Translation: AAB18608.1.
U00096 Genomic DNA. Translation: AAC76655.1.
AP009048 Genomic DNA. Translation: BAE77661.1.
S75736 Genomic DNA. Translation: AAD43826.1.

PIR

B42595.

RefSeq

NP_418088.1. NC_000913.2.
YP_491802.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IV7	X-ray	1.60	A	1-374	[»]
2IW1	X-ray	1.50	A	1-374	[»]

ProteinModelPortal

P25740.

SMR

P25740. Positions 2-371.

ModBase

Search...

Protein-protein interaction databases

IntAct

P25740. 10 interactions.

STRING

511145.b3631.

Protein family/group databases

CAZy

GT4. Glycosyltransferase Family 4.

Proteomic databases

PaxDb

P25740.

PRIDE

P25740.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76655; AAC76655; b3631.
BAE77661; BAE77661; BAE77661.

GeneID

12931875.
948149.

KEGG

ecj:Y75_p3543.
eco:b3631.

PATRIC

32122749. VBIEscCol129921_3751.

Organism-specific databases

EchoBASE

EB1315.

EcoGene

EG11339. rfaG.

Phylogenomic databases

eggNOG

COG0438.

HOGENOM

HOG000126226.

KO

K02844.

OMA

GLQRDFL.

ProtClustDB

CLSK869057.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11339-MONOMER.
ECOL316407:JW3606-MONOMER.
MetaCyc:EG11339-MONOMER.

UniPathway

UPA00958.

Gene expression databases

Genevestigator

P25740.

Family and domain databases

InterPro

IPR001296. Glyco_trans_1.
[Graphical view]

Pfam

PF00534. Glycos_transf_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P25740.

Entry information

Entry name

RFAG_ECOLI

Accession

Primary (citable) accession number: P25740
Secondary accession number(s): Q2M7U5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program