Difference between revisions of "YwaD"
| Line 20: | Line 20: | ||
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1365 bp, 455 aa | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1365 bp, 455 aa | ||
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[tyrZ]]'', ''[[ | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[tyrZ]]'', ''[[sasA]]'' |
|- | |- | ||
|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU38470 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU38470 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU38470 DNA_with_flanks] | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU38470 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU38470 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU38470 DNA_with_flanks] | ||
| Line 58: | Line 58: | ||
=== Additional information=== | === Additional information=== | ||
| − | |||
| − | |||
| − | |||
=The protein= | =The protein= | ||
| Line 76: | Line 73: | ||
* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
Revision as of 15:54, 6 February 2014
- Description: double-zinc aminopeptidase
| Gene name | ywaD |
| Synonyms | ipa-8r |
| Essential | no |
| Product | double-zinc aminopeptidase |
| Function | unknown |
| Gene expression levels in SubtiExpress: ywaD | |
| MW, pI | 49 kDa, 6.638 |
| Gene length, protein length | 1365 bp, 455 aa |
| Immediate neighbours | tyrZ, sasA |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
poorly characterized/ putative enzymes
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU38470
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: M28B subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization:
- extracellular (signal peptide) PubMed
Database entries
- Structure:
- UniProt: P25152
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: ywaD PubMed
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Xinxing Gao, Wenjing Cui, Ning Ding, Zhongmei Liu, Yaping Tian, Zhemin Zhou
Structure-based approach to alter the substrate specificity of Bacillus subtilis aminopeptidase.
Prion: 2013, 7(4);328-34
[PubMed:23787698]
[WorldCat.org]
[DOI]
(I p)
Xinxing Gao, Wenjing Cui, Yaping Tian, Zhemin Zhou
Over-expression, secretion, biochemical characterisation, and structure analysis of Bacillus subtilis aminopeptidase.
J Sci Food Agric: 2013, 93(11);2810-5
[PubMed:23426795]
[WorldCat.org]
[DOI]
(I p)
Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862]
[WorldCat.org]
[DOI]
(I p)
Yifat Fundoiano-Hershcovitz, Larisa Rabinovitch, Smadar Shulami, Vera Reiland, Gil Shoham, Yuval Shoham
The ywad gene from Bacillus subtilis encodes a double-zinc aminopeptidase.
FEMS Microbiol Lett: 2005, 243(1);157-63
[PubMed:15668014]
[WorldCat.org]
[DOI]
(P p)
