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BACSU:YMDB

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Species (Taxon ID) Bacillus subtilis (strain 168). (224308)
Gene Name(s) ymdB
Protein Name(s) Uncharacterized protein ymdB
External Links
UniProt O31775
EMBL AL009126
PIR G69884
RefSeq NP_389579.2
PDB 4B2O
PDBsum 4B2O
ProteinModelPortal O31775
SMR O31775
STRING 224308.BSU16970
PaxDb O31775
EnsemblBacteria CAB13570
GeneID 939441
KEGG bsu:BSU16970
PATRIC 18975201
GenoList BSU16970
eggNOG COG1692
HOGENOM HOG000011009
InParanoid O31775
KO K09769
OMA PTADAQI
OrthoDB EOG68DD2S
PhylomeDB O31775
BioCyc BSUB:BSU16970-MONOMER
RETL1328306-WGS:GSTH-3535-MONOMER
Proteomes UP000001570
GO GO:0016787
InterPro IPR004843
IPR005235
IPR029052
Pfam PF00149
PIRSF PIRSF004789
SUPFAM SSF56300
TIGRFAMs TIGR00282

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004113

2',3'-cyclic-nucleotide 3'-phosphodiesterase activity

PMID:24163345[1]

ECO:0000314

F

Table 4: Shows kinetics of YmdB against 2'3' cyclic mononucleotides

complete
CACAO 9127

GO:0004114

3',5'-cyclic-nucleotide phosphodiesterase activity

PMID:24163345[1]

ECO:0000314

F

Table 4: Shows kinetics with 3'5' cyclic mononucleotides

complete
CACAO 9129

GO:1902201

negative regulation of bacterial-type flagellar cell motility

PMID:21856853[2]

ECO:0000315

P

Fig. 1 Shows accumulation of flagellin Hag in YmdB deletion strain

complete
CACAO 9137

GO:1900192

positive regulation of single-species biofilm formation

PMID:21856853[2]

ECO:0000315

P

Fig 2: Shows visual effects of biofilm production using a YmdB deletion mutant. YmdB deletion mutants are unable to form biofilms.

complete
CACAO 9141

enables

GO:0004113

2',3'-cyclic-nucleotide 3'-phosphodiesterase activity

PMID:24163345[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004113

2',3'-cyclic-nucleotide 3'-phosphodiesterase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002190809
UniProtKB:O31775

F

Seeded From UniProt

complete

enables

GO:0008663

2',3'-cyclic-nucleotide 2'-phosphodiesterase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.4.16

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

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

Notes

References

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

  1. 1.0 1.1 1.2 Diethmaier, C et al. (2014) The YmdB phosphodiesterase is a global regulator of late adaptive responses in Bacillus subtilis. J. Bacteriol. 196 265-75 PubMed GONUTS page
  2. 2.0 2.1 Diethmaier, C et al. (2011) A novel factor controlling bistability in Bacillus subtilis: the YmdB protein affects flagellin expression and biofilm formation. J. Bacteriol. 193 5997-6007 PubMed GONUTS page
  3. Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page