Difference between revisions of "LplD"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
− | {{SubtiWiki category|[[ | + | {{SubtiWiki category|[[utilization of specific carbon sources]]}}, |
{{SubtiWiki category|[[sporulation proteins]]}} | {{SubtiWiki category|[[sporulation proteins]]}} | ||
Revision as of 15:26, 16 August 2013
- Description: α-galacturonidase
Gene name | lplD |
Synonyms | |
Essential | no |
Product | α-galacturonidase |
Function | utilization of pectin |
Gene expression levels in SubtiExpress: lplD | |
MW, pI | 49 kDa, 5.356 |
Gene length, protein length | 1338 bp, 446 aa |
Immediate neighbours | lplC, yetF |
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
utilization of specific carbon sources, sporulation proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU07130
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- cleavage of α-1,4-di-galacturonate PubMed
- Protein family: glycosyl hydrolase 4 family PubMed
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- active site motif: CHEV PubMed
- Modification:
- Cofactor(s): NAD, Mn(2+) PubMed
- Effectors of protein activity:
Database entries
- Structure: 3FEF
- UniProt: P39130
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- 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
John Thompson, Andreas Pikis, Jamie Rich, Barry G Hall, Stephen G Withers
α-Galacturonidase(s): a new class of Family 4 glycoside hydrolases with strict specificity and a unique CHEV active site motif.
FEBS Lett: 2013, 587(6);799-803
[PubMed:23416295]
[WorldCat.org]
[DOI]
(I p)