Difference between revisions of "HtrA"
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* '''Additional information:''' | * '''Additional information:''' | ||
** [[HtrA]] is subject to degradation by [[WprA]] and other extracellular proteases {{PubMed|24362423}} | ** [[HtrA]] is subject to degradation by [[WprA]] and other extracellular proteases {{PubMed|24362423}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium): 91 {{PubMed|24696501}} | ||
=Biological materials = | =Biological materials = |
Revision as of 09:59, 17 April 2014
- Description: membrane-anchored protein quality control protease, serine protease Do
Gene name | htrA |
Synonyms | ykdA |
Essential | no |
Product | serine protease Do |
Function | protein quality control |
Gene expression levels in SubtiExpress: htrA | |
Metabolic function and regulation of this protein in SubtiPathways: htrA | |
MW, pI | 47 kDa, 4.699 |
Gene length, protein length | 1347 bp, 449 aa |
Immediate neighbours | ykcC, proG |
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
proteolysis, heat shock proteins, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU12900
Phenotypes of a mutant
Database entries
- BsubCyc: BSU12900
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Protein family: PDZ (DHR) domain (according to Swiss-Prot)
- Paralogous protein(s): HtrC
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- BsubCyc: BSU12900
- Structure:
- UniProt: O34358
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: htrA (according to DBTBS)
- Regulation:
- Additional information:
Biological materials
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Original publications