Difference between revisions of "CheW"
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:* subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed] | :* subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed] | ||
=Expression and regulation= | =Expression and regulation= | ||
| − | * '''Operon:''' | + | * '''Operon:''' part of the [[fla-che operon]] |
** ''[[flgB]]-[[flgC]]-[[fliE]]-[[fliF]]-[[fliG]]-[[fliH]]-[[fliI]]-[[fliJ]]-[[ylxF]]-[[fliK]]-[[flgD]]-[[flgE]]-[[fliL]]-[[fliM]]-[[fliY]]-[[cheY]]-[[fliZ]]-[[fliP]]-[[fliQ]]-[[fliR]]-[[flhB]]-[[flhA]]-[[flhF]]-[[flhG]]-[[cheB]]-[[cheA]]-[[cheW]]-[[cheC]]-[[cheD]]-[[sigD]]-[[swrB]]'' {{PubMed|9657996,8157612,15175317}} | ** ''[[flgB]]-[[flgC]]-[[fliE]]-[[fliF]]-[[fliG]]-[[fliH]]-[[fliI]]-[[fliJ]]-[[ylxF]]-[[fliK]]-[[flgD]]-[[flgE]]-[[fliL]]-[[fliM]]-[[fliY]]-[[cheY]]-[[fliZ]]-[[fliP]]-[[fliQ]]-[[fliR]]-[[flhB]]-[[flhA]]-[[flhF]]-[[flhG]]-[[cheB]]-[[cheA]]-[[cheW]]-[[cheC]]-[[cheD]]-[[sigD]]-[[swrB]]'' {{PubMed|9657996,8157612,15175317}} | ||
** ''[[ylxF]]-[[fliK]]-[[flgD]]-[[flgE]]-[[fliL]]-[[fliM]]-[[fliY]]-[[cheY]]-[[fliZ]]-[[fliP]]-[[fliQ]]-[[fliR]]-[[flhB]]-[[flhA]]-[[flhF]]-[[flhG]]-[[cheB]]-[[cheA]]-[[cheW]]-[[cheC]]-[[cheD]]-[[sigD]]-[[swrB]]'' {{PubMed|20233303}} | ** ''[[ylxF]]-[[fliK]]-[[flgD]]-[[flgE]]-[[fliL]]-[[fliM]]-[[fliY]]-[[cheY]]-[[fliZ]]-[[fliP]]-[[fliQ]]-[[fliR]]-[[flhB]]-[[flhA]]-[[flhF]]-[[flhG]]-[[cheB]]-[[cheA]]-[[cheW]]-[[cheC]]-[[cheD]]-[[sigD]]-[[swrB]]'' {{PubMed|20233303}} | ||
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** ''[[ylxF]]'': [[SigD]] {{PubMed|20233303}} | ** ''[[ylxF]]'': [[SigD]] {{PubMed|20233303}} | ||
| − | * '''Regulation:''' | + | * '''Regulation:''' see [[fla-che operon]] |
| − | |||
| − | * '''Regulatory mechanism:''' | + | * '''Regulatory mechanism:''' see [[fla-che operon]] |
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
* '''Additional information:''' | * '''Additional information:''' | ||
Revision as of 14:18, 12 February 2015
- Description: modulation of CheA activity in response to attractants, scaffold protein: facilitates coupling between CheA and receptors
| Gene name | cheW |
| Synonyms | |
| Essential | no |
| Product | CheA modulator |
| Function | control of CheA activity |
| Gene expression levels in SubtiExpress: cheW | |
| MW, pI | 17 kDa, 4.422 |
| Gene length, protein length | 468 bp, 156 aa |
| Immediate neighbours | cheA, cheC |
| 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
This gene is a member of the following regulons
CodY regulon, DegU regulon, SigD regulon, Spo0A regulon
The gene
Basic information
- Locus tag: BSU16440
Phenotypes of a mutant
Database entries
- BsubCyc: BSU16440
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s): CheV (N-terminal domain)
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- cytoplasm (according to Swiss-Prot)
- predominantly present at the cell poles PubMed
Database entries
- BsubCyc: BSU16440
- Structure:
- UniProt: P39802
- KEGG entry: [3]
- E.C. number:
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Operon: part of the fla-che operon
- Regulation: see fla-che operon
- Regulatory mechanism: see fla-che operon
- Additional information:
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
- in minimal medium, CheW is present with 2,100 +/- 430 molecules per cell PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium): 840 PubMed
- number of protein molecules per cell (complex medium with amino acids, without glucose): 1423 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1996 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1296 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 699 PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Gerald L Hazelbauer, Wing-Cheung Lai
Bacterial chemoreceptors: providing enhanced features to two-component signaling.
Curr Opin Microbiol: 2010, 13(2);124-32
[PubMed:20122866]
[WorldCat.org]
[DOI]
(I p)
Original publications
