Difference between revisions of "McsB"
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|style="background:#ABCDEF;" align="center"|'''Function''' || control of [[CtsR]] activity | |style="background:#ABCDEF;" align="center"|'''Function''' || control of [[CtsR]] activity | ||
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− | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU00850 mcsB] |
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/McsB McsB] | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/McsB McsB] | ||
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[mcsA]]'', ''[[clpC]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[mcsA]]'', ''[[clpC]]'' | ||
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− | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU00850 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU00850 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU00850 Advanced_DNA] |
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|colspan="2" | '''Genetic context''' <br/> [[Image:mcsB_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:mcsB_context.gif]] |
Revision as of 11:57, 13 May 2013
- Description: protein arginine kinase, adaptor protein, modulator of CtsR-dependent repression
Gene name | mcsB |
Synonyms | yacI |
Essential | no |
Product | protein arginine kinase |
Function | control of CtsR activity |
Gene expression levels in SubtiExpress: mcsB | |
Interactions involving this protein in SubtInteract: McsB | |
Metabolic function and regulation of this protein in SubtiPathways: Stress | |
MW, pI | 40 kDa, 5.068 |
Gene length, protein length | 1089 bp, 363 aa |
Immediate neighbours | mcsA, clpC |
Sequences | Protein DNA Advanced_DNA |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
protein modification, transcription factors and their control, sporulation proteins, general stress proteins (controlled by SigB), heat shock proteins
This gene is a member of the following regulons
CtsR regulon, SigB regulon, SigF regulon
The gene
Basic information
- Locus tag: BSU00850
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: targets non-functional CtsR for degradation by ClpP/ClpC PubMed
- Protein family: ATP:guanido phosphotransferase 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
- Structure:
- UniProt: P37570
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Mutant:
- mcsB::aphA3 availbale from the Gerth lab
- mcsBC167S::spec available from the Gerth lab
- GP1457 (mcsB::aphA3), available in Stülke lab
- BP69 (spc), available in Fabian Commichau's lab
- Expression vector: for expression, purification in E. coli with N-terminal His-tag, pRSETA available in Gerth lab
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody: available in Gerth lab
Labs working on this gene/protein
- Ulf Gerth, Greifswald, Germany
- Fabian Commichau Göttingen, Germany
Your additional remarks
References
Reviews
Additional reviews: PubMed
Aurelia Battesti, Susan Gottesman
Roles of adaptor proteins in regulation of bacterial proteolysis.
Curr Opin Microbiol: 2013, 16(2);140-7
[PubMed:23375660]
[WorldCat.org]
[DOI]
(I p)
Original Publications
Additional publications: PubMed