Difference between revisions of "MreB"
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− | * '''Description:''' [[cell shape]]-determining protein, forms filaments, the polymers control/restrict the mobility of the cell wall elongation enzyme complex <br/><br/> | + | * '''Description:''' [[cell shape]]-determining protein, forms filaments, the polymers control/restrict the mobility of the cell wall elongation enzyme complex, required for [[LytE]] activity <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
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** polymerizes in the presence of millimolar divalent cations, binds and hydrolyzes GTP and ATP {{PubMed|19117023}} | ** polymerizes in the presence of millimolar divalent cations, binds and hydrolyzes GTP and ATP {{PubMed|19117023}} | ||
** involved in the organization of ϕ29 DNA replication machinery in peripheral helix-like structures {{PubMed|22420858}} | ** involved in the organization of ϕ29 DNA replication machinery in peripheral helix-like structures {{PubMed|22420858}} | ||
+ | ** required for [[LytE]] activity {{PubMed|23869552}} | ||
* '''Protein family:''' ftsA/mreB family (according to Swiss-Prot) | * '''Protein family:''' ftsA/mreB family (according to Swiss-Prot) | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
− | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
− | * ''' | + | * '''Cofactors:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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==Other original publications== | ==Other original publications== | ||
− | <pubmed>15752190,11290328,12809607,1400224,19192185,7836311, 16950129, 19192185, 19117023 19643765 19654094 19659933 8459776 11544518 20133608 21091501 21320184 18179421 21964069 22343529 22362028 22420858,21926231 23879732</pubmed> | + | <pubmed>15752190,11290328,12809607,1400224,19192185,7836311, 16950129, 19192185, 19117023 19643765 19654094 19659933 8459776 11544518 20133608 21091501 21320184 18179421 21964069 22343529 22362028 22420858,21926231 23879732 23869552</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 19:42, 14 December 2013
- Description: cell shape-determining protein, forms filaments, the polymers control/restrict the mobility of the cell wall elongation enzyme complex, required for LytE activity
Gene name | mreB |
Synonyms | divIVB |
Essential | yes PubMed |
Product | cell shape-determining protein |
Function | cell shape determination |
Gene expression levels in SubtiExpress: mreB | |
Interactions involving this protein in SubtInteract: MreB | |
MW, pI | 35 kDa, 4.901 |
Gene length, protein length | 1011 bp, 337 aa |
Immediate neighbours | mreC, radC |
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
cell shape, cell envelope stress proteins (controlled by SigM, V, W, X, Y), essential genes, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU28030
Phenotypes of a mutant
- essential PubMed
- the mutation can be suppressed by inactivation of ponA, ptsI, ccpA PubMed, by overexpression of YvcK PubMed, or by addition of 5 mM magnesium to the growth medium PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: ftsA/mreB family (according to Swiss-Prot)
Extended information on the protein
- Kinetic information:
- Modification:
- Cofactors:
- Effectors of protein activity:
- Localization:
- during logarithmic growth, MreB forms discrete patches thst move processively along peripheral tracks perpendicular to the cell axis PubMed
- forms transverse bands as cells enter the stationary phase PubMed
- close to the inner surface of the cytoplasmic membrane PubMed
- reports on helical structures formed by MreB PubMed seem to be misinterpretation of data PubMed
- normal localization depends on the presence of glucolipids, MreB forms irregular clusters in an ugtP mutant PubMed
Database entries
- UniProt: Q01465
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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 the labs of Jeff Errington and Boris Görke
- Antibody: available in the Jeff Errington and Peter Graumann labs
Labs working on this gene/protein
Jeff Errington, Newcastle University, UK homepage
Peter Graumann, Freiburg University, Germany homepage
Your additional remarks
References
Reviews
Localization
Other original publications