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ECOLI:RFAC

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) rfaC (synonyms: rfa-2, waaC, yibC)
Protein Name(s) Lipopolysaccharide heptosyltransferase 1
External Links
UniProt P24173
EMBL M95398
X62530
U00039
U00096
AP009048
PIR A40619
RefSeq NP_418078.1
YP_491812.1
PDB 2H1H
PDBsum 2H1H
ProteinModelPortal P24173
SMR P24173
IntAct P24173
STRING 511145.b3621
CAZy GT9
EnsemblBacteria AAC76645
BAE77671
GeneID 12934310
948136
KEGG ecj:Y75_p3553
eco:b3621
PATRIC 32122729
EchoBASE EB1175
EcoGene EG11189
eggNOG COG0859
HOGENOM HOG000257134
InParanoid P24173
KO K02841
OMA WPESHWR
OrthoDB EOG6WQD45
PhylomeDB P24173
BioCyc EcoCyc:EG11189-MONOMER
ECOL316407:JW3596-MONOMER
MetaCyc:EG11189-MONOMER
UniPathway UPA00958
EvolutionaryTrace P24173
PRO PR:P24173
Proteomes UP000000318
UP000000625
Genevestigator P24173
GO GO:0008920
GO:0009244
InterPro IPR002201
IPR011908
Pfam PF01075
TIGRFAMs TIGR02193

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0008920

lipopolysaccharide heptosyltransferase activity

PMID:11054112[1]

ECO:0000314

F

Figure 3 - Product in the presence of RfaC contains an additional heptose attached to Kdo2. Product in the absence of RfaC only contains Kdo2.

complete
CACAO 4085

GO:0009244

lipopolysaccharide core region biosynthetic process

PMID:8478319[2]

ECO:0000315

P

Figure 4a - LPS profile of strains by SDS-PAGE. Mutant phenotype of rfa-2 mutant strain (lane 3) was restored to wildtype by complementing with an rfa-2 plasmid (lane 1).

complete
CACAO 4649

involved_in

GO:0009244

lipopolysaccharide core region biosynthetic process

PMID:8478319[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008920

lipopolysaccharide heptosyltransferase activity

PMID:11054112[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009244

lipopolysaccharide core region biosynthetic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11189
EcoGene:EG11341
EcoGene:EG11423
EcoGene:EG12210
PANTHER:PTN001575314
UniProtKB:G3XD35
UniProtKB:P26469
UniProtKB:P37421
UniProtKB:Q9HUF5

P

Seeded From UniProt

complete

enables

GO:0008713

ADP-heptose-lipopolysaccharide heptosyltransferase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12210
PANTHER:PTN001575314

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12210
PANTHER:PTN001575314

C

Seeded From UniProt

complete

involved_in

GO:0009244

lipopolysaccharide core region biosynthetic process

PMID:7024253[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009244

lipopolysaccharide core region biosynthetic process

PMID:3882666[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008920

lipopolysaccharide heptosyltransferase activity

PMID:9446588[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008920

lipopolysaccharide heptosyltransferase activity

PMID:22059588[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008920

lipopolysaccharide heptosyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011908

F

Seeded From UniProt

complete

involved_in

GO:0009244

lipopolysaccharide core region biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011908

P

Seeded From UniProt

complete

enables

GO:0016757

transferase activity, transferring glycosyl groups

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002201

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

involved_in

GO:0009103

lipopolysaccharide biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0448

P

Seeded From UniProt

complete

enables

GO:0016757

transferase activity, transferring glycosyl groups

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0328

F

Seeded From UniProt

complete

involved_in

GO:0009244

lipopolysaccharide core region biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00958

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Gronow, S et al. (2000) Comparative functional characterization in vitro of heptosyltransferase I (WaaC) and II (WaaF) from Escherichia coli. Eur. J. Biochem. 267 6602-11 PubMed GONUTS page
  2. 2.0 2.1 Chen, L & Coleman, WG Jr (1993) Cloning and characterization of the Escherichia coli K-12 rfa-2 (rfaC) gene, a gene required for lipopolysaccharide inner core synthesis. J. Bacteriol. 175 2534-40 PubMed GONUTS page
  3. 3.0 3.1 3.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. Beher, MG & Schnaitman, CA (1981) Regulation of the OmpA outer membrane protein of Escherichia coli. J. Bacteriol. 147 972-85 PubMed GONUTS page
  5. Coleman, WG Jr & Deshpande, KS (1985) New cysE-pyrE-linked rfa mutation in Escherichia coli K-12 that results in a heptoseless lipopolysaccharide. J. Bacteriol. 161 1209-14 PubMed GONUTS page
  6. Kadrmas, JL & Raetz, CR (1998) Enzymatic synthesis of lipopolysaccharide in Escherichia coli. Purification and properties of heptosyltransferase i. J. Biol. Chem. 273 2799-807 PubMed GONUTS page
  7. Czyzyk, DJ et al. (2011) Lipopolysaccharide biosynthesis without the lipids: recognition promiscuity of Escherichia coli heptosyltransferase I. Biochemistry 50 10570-2 PubMed GONUTS page