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STRPA:GTF1

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Species (Taxon ID) Streptococcus parasanguinis. (1318)
Gene Name(s) gtf1
Protein Name(s) Glycosyltransferase Gtf1
External Links
UniProt A1C3L9
EMBL DQ990875
ProteinModelPortal A1C3L9
IntAct A1C3L9
CAZy GT4
GO GO:0005737
GO:0005886
GO:0017122
GO:0016757
GO:0009058
HAMAP MF_01472
InterPro IPR015397
IPR001296
IPR014267
Pfam PF09318
PF00534
TIGRFAMs TIGR02918

Annotations

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

Contributes to

GO:0016262

protein N-acetylglucosaminyltransferase activity

PMID:20971868[1]

ECO:0000314

F

Figured 2C. GTF1 was tandem purified with GTF2 and assayed with proteins using radioactive labeled UDP-GlcNAc

complete
CACAO 3896

GO:0017122

protein N-acetylglucosaminyltransferase complex

PMID:20971868[1]

ECO:0000314

C

Figure 2-C GTF1 achieves maximal activity when complexed with GTF2. Figure 1 shows the results of SDS-PAGE electrophoresis after TAP purification of the protein complex, proteins co-purify together under native conditions.

complete
CACAO 3898

part_of

GO:0017122

protein N-acetylglucosaminyltransferase complex

PMID:20971868[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

contributes_to

GO:0016262

protein N-acetylglucosaminyltransferase activity

PMID:20971868[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016757

transferase activity, transferring glycosyl groups

PMID:21862581[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016757

transferase activity, transferring glycosyl groups

PMID:20971868[1]

ECO:0000314

direct assay evidence used in manual assertion

F

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:IPR014267

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000165363

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000165363

C

Seeded From UniProt

complete

enables

GO:0016757

transferase activity, transferring glycosyl groups

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000165363

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

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

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

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0039

C

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 1.2 1.3 1.4 Wu, R et al. (2010) Purification and characterization of an active N-acetylglucosaminyltransferase enzyme complex from Streptococci. Appl. Environ. Microbiol. 76 7966-71 PubMed GONUTS page
  2. Wu, R & Wu, H (2011) A molecular chaperone mediates a two-protein enzyme complex and glycosylation of serine-rich streptococcal adhesins. J. Biol. Chem. 286 34923-31 PubMed GONUTS page