Difference between revisions of "CtaO"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU12080&redirect=T BSU12080] | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU12080&redirect=T BSU12080] | ||
* '''Structure:''' | * '''Structure:''' |
Revision as of 13:27, 2 April 2014
- Description: heme O synthase (minor enzyme)
Gene name | ctaO |
Synonyms | yjdK |
Essential | no |
Product | heme O synthase (minor enzyme) |
Function | heme biosynthesis |
Gene expression levels in SubtiExpress: ctaO | |
MW, pI | 36 kDa, 10.121 |
Gene length, protein length | 987 bp, 329 aa |
Immediate neighbours | yjdJ, cotT |
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 of cofactors, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU12080
Phenotypes of a mutant
Database entries
- BsubCyc: BSU12080
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: Protoheme IX farnesyltransferase subfamily (according to Swiss-Prot)
- Paralogous protein(s): CtaB
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- cell membrane (according to Swiss-Prot)
Database entries
- BsubCyc: BSU12080
- Structure:
- UniProt: O31652
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- 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
Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947]
[WorldCat.org]
[DOI]
(I p)
Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675]
[WorldCat.org]
[DOI]
(I p)
M Throne-Holst, L Hederstedt
The Bacillus subtilis ctaB paralogue, yjdK, can complement the heme A synthesis deficiency of a CtaB-deficient mutant.
FEMS Microbiol Lett: 2000, 183(2);247-51
[PubMed:10675592]
[WorldCat.org]
[DOI]
(P p)