Difference between revisions of "Lip"
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'''Additional publications:''' {{PubMed|21477088,22246996}} | '''Additional publications:''' {{PubMed|21477088,22246996}} | ||
− | <pubmed> 22267088 </pubmed> | + | <pubmed>22996591 22267088 </pubmed> |
<big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J'' </big> | <big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J'' </big> | ||
<big>'''RNA processing in ''Bacillus subtilis'': identification of targets of the essential RNase Y.''' </big> | <big>'''RNA processing in ''Bacillus subtilis'': identification of targets of the essential RNase Y.''' </big> |
Revision as of 09:27, 22 September 2012
- Description: extracellular lipase
Gene name | lip |
Synonyms | lipA |
Essential | no |
Product | extracellular lipase |
Function | lipid degradation |
Gene expression levels in SubtiExpress: lip | |
MW, pI | 22 kDa, 10.059 |
Gene length, protein length | 636 bp, 212 aa |
Immediate neighbours | ansZ, yczC |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU02700
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:
- Paralogous protein(s): LipB
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure: 2QXT
- UniProt: P37957
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- 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
Additional publications: PubMed
Wojciech Augustyniak, Hans Wienk, Rolf Boelens, Manfred T Reetz
¹H, ¹³C and ¹⁵N resonance assignments of wild-type Bacillus subtilis Lipase A and its mutant evolved towards thermostability.
Biomol NMR Assign: 2013, 7(2);249-52
[PubMed:22996591]
[WorldCat.org]
[DOI]
(I p)
Wojciech Augustyniak, Agnieszka A Brzezinska, Tjaard Pijning, Hans Wienk, Rolf Boelens, Bauke W Dijkstra, Manfred T Reetz
Biophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: factors contributing to increased activity retention.
Protein Sci: 2012, 21(4);487-97
[PubMed:22267088]
[WorldCat.org]
[DOI]
(I p)
Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. Mol Microbiol. 2011 81(6): 1459-1473. PubMed:21815947