Tmk
- Description: thymidylate kinase
Gene name | tmk |
Synonyms | yaaP |
Essential | yes PubMed |
Product | thymidylate kinase |
Function | TTP biosynthesis |
Gene expression levels in SubtiExpress: tmk | |
Metabolic function and regulation of this protein in SubtiPathways: tmk | |
MW, pI | 23 kDa, 4.866 |
Gene length, protein length | 636 bp, 212 aa |
Immediate neighbours | yaaO, darA |
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
biosynthesis/ acquisition of nucleotides, essential genes
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU00280
Phenotypes of a mutant
essential PubMed
Database entries
- BsubCyc: BSU00280
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + dTMP = ADP + dTDP (according to Swiss-Prot)
- Protein family: thymidylate kinase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- BsubCyc: BSU00280
- UniProt: P37537
- KEGG entry: [2]
- E.C. number: 2.7.4.9
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: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Masayo Kotaka, Balvinder Dhaliwal, Jingshan Ren, Charles E Nichols, Richard Angell, Michael Lockyer, Alastair R Hawkins, David K Stammers
Structures of S. aureus thymidylate kinase reveal an atypical active site configuration and an intermediate conformational state upon substrate binding.
Protein Sci: 2006, 15(4);774-84
[PubMed:16522804]
[WorldCat.org]
[DOI]
(P p)