AckA
Revision as of 09:54, 17 April 2014 by 134.76.70.252 (talk)
- Description: acetate kinase
Gene name | ackA |
Synonyms | |
Essential | no |
Product | acetate kinase |
Function | overflow metabolism |
Gene expression levels in SubtiExpress: ackA | |
Metabolic function and regulation of this protein in SubtiPathways: ackA | |
MW, pI | 42 kDa, 5.191 |
Gene length, protein length | 1185 bp, 395 aa |
Immediate neighbours | moaB, ytxK |
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
ATP synthesis, carbon core metabolism, most abundant proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU29470
Phenotypes of a mutant
Database entries
- BsubCyc: BSU29470
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + acetate = ADP + acetyl phosphate (according to Swiss-Prot)
- Protein family: acetokinase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- BsubCyc: BSU29470
- Structure: 2IIR (from Thermotoga maritima, 54% identity, 73% similarity)
- UniProt: P37877
- KEGG entry: [3]
- E.C. number: 2.7.2.1
Additional information
Expression and regulation
- Regulation:
- Additional information:
- belongs to the 100 most abundant proteins PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium): 1613 PubMed
- number of protein molecules per cell (complex medium with amino acids, without glucose): 11040 PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Linc Sonenshein, Tufts University, Boston, MA, USA Homepage
Your additional remarks
References
Reviews
Original publications