Difference between revisions of "DacA"
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|style="background:#ABCDEF;" align="center"|'''Function''' || carboxypeptidase | |style="background:#ABCDEF;" align="center"|'''Function''' || carboxypeptidase | ||
|- | |- | ||
| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU00100 dacA] |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 48 kDa, 5.668 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 48 kDa, 5.668 | ||
| Line 22: | Line 22: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[guaB]]'', ''[[pdxS]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[guaB]]'', ''[[pdxS]]'' | ||
|- | |- | ||
| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU00100 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU00100 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU00100 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:dacA_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:dacA_context.gif]] | ||
Revision as of 11:52, 13 May 2013
- Description: penicillin-binding protein 5*, D-alanyl-D-alanine carboxypeptidase
| Gene name | dacA |
| Synonyms | |
| Essential | no |
| Product | penicillin-binding protein 5*, D-alanyl-D-alanine carboxypeptidase |
| Function | carboxypeptidase |
| Gene expression levels in SubtiExpress: dacA | |
| MW, pI | 48 kDa, 5.668 |
| Gene length, protein length | 1329 bp, 443 aa |
| Immediate neighbours | guaB, pdxS |
| Sequences | Protein DNA Advanced_DNA |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
cell wall synthesis, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU00100
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala (according to Swiss-Prot)
- Protein family: peptidase S11 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- secreted (according to Swiss-Prot), membrane associated PubMed
Database entries
- Structure:
- UniProt: P08750
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Elitza I Tocheva, Javier López-Garrido, H Velocity Hughes, Jennifer Fredlund, Erkin Kuru, Michael S Vannieuwenhze, Yves V Brun, Kit Pogliano, Grant J Jensen
Peptidoglycan transformations during Bacillus subtilis sporulation.
Mol Microbiol: 2013, 88(4);673-86
[PubMed:23531131]
[WorldCat.org]
[DOI]
(I p)
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[WorldCat.org]
[DOI]
(I p)
D L Popham, M E Gilmore, P Setlow
Roles of low-molecular-weight penicillin-binding proteins in Bacillus subtilis spore peptidoglycan synthesis and spore properties.
J Bacteriol: 1999, 181(1);126-32
[PubMed:9864321]
[WorldCat.org]
[DOI]
(P p)
