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BACSU:SRFAC
Contents
Species (Taxon ID) | Bacillus subtilis (strain 168). (224308) | |
Gene Name(s) | srfAC (synonyms: srfA3) | |
Protein Name(s) | Surfactin synthase subunit 3 | |
External Links | ||
UniProt | Q08787 | |
EMBL | X70356 D50453 AL009126 | |
PIR | I40487 | |
RefSeq | NP_388233.2 | |
PDB | 1JMK 2VSQ | |
PDBsum | 1JMK 2VSQ | |
ProteinModelPortal | Q08787 | |
SMR | Q08787 | |
IntAct | Q08787 | |
MINT | MINT-8365036 | |
STRING | 224308.BSU03510 | |
PhosSite | P0802245 | |
PaxDb | Q08787 | |
EnsemblBacteria | CAB12145 | |
GeneID | 938308 | |
KEGG | bsu:BSU03510 | |
PATRIC | 18972265 | |
GenoList | BSU03510 | |
eggNOG | COG3319 | |
HOGENOM | HOG000229993 | |
InParanoid | Q08787 | |
KO | K15656 | |
OMA | HQYVPLY | |
OrthoDB | EOG6XHC08 | |
PhylomeDB | Q08787 | |
BioCyc | BSUB:BSU03510-MONOMER | |
UniPathway | UPA00181 | |
EvolutionaryTrace | Q08787 | |
Proteomes | UP000001570 | |
GO | GO:0016788 GO:0016874 GO:0017000 GO:0030435 | |
Gene3D | 1.10.1200.10 3.40.50.1820 | |
InterPro | IPR010071 IPR029058 IPR009081 IPR025110 IPR020845 IPR000873 IPR001242 IPR006162 IPR001031 | |
Pfam | PF00501 PF13193 PF00668 PF00550 PF00975 | |
SUPFAM | SSF47336 SSF53474 | |
TIGRFAMs | TIGR01733 | |
PROSITE | PS50075 PS00455 PS00012 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0016790 |
thiolester hydrolase activity |
ECO:0000247 |
UniProtKB:C0ZDA7 UniProtKB:P0C064
|
F |
Figure 3. |
complete | ||||
involved_in |
GO:0044550 |
secondary metabolite biosynthetic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10264 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0043041 |
amino acid activation for nonribosomal peptide biosynthetic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10264 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0031177 |
phosphopantetheine binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10264 |
F |
Seeded From UniProt |
complete | ||
part_of |
GO:0005829 |
cytosol |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10264 |
C |
Seeded From UniProt |
complete | ||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10264 |
C |
Seeded From UniProt |
complete | ||
enables |
GO:0003824 |
catalytic activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0009058 |
biosynthetic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0016788 |
hydrolase activity, acting on ester bonds |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0031177 |
phosphopantetheine binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0017000 |
antibiotic biosynthetic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0030435 |
sporulation resulting in formation of a cellular spore |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0016874 |
ligase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Bruner, SD et al. (2002) Structural basis for the cyclization of the lipopeptide antibiotic surfactin by the thioesterase domain SrfTE. Structure 10 301-10 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 2.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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