Difference between revisions of "Era"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
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=== Additional information=== | === Additional information=== | ||
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=The protein= | =The protein= | ||
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* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
+ | ** [[Era]]-[[16S rRNA]] {{PubMed|19706445}} | ||
* '''[[Localization]]:''' | * '''[[Localization]]:''' | ||
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* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU25290&redirect=T BSU25290] | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU25290&redirect=T BSU25290] | ||
− | * '''Structure:''' | + | * '''Structure:''' [http://pdb.org/pdb/explore/explore.do?structureId=3IEV 3IEV] ([[Era]] from ''Aquifex aeolicus'', 50% identity/ 77% similarity, complex with the 3' end of [[16S rRNA]]) {{PubMed|19706445}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P42182 P42182] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P42182 P42182] | ||
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==Original publications== | ==Original publications== | ||
− | <pubmed>12427945, 6330116 </pubmed> | + | <pubmed>12427945, 6330116 19706445</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 11:47, 25 February 2015
- Description: GTP-binding protein, involved in the assembly of the 30S ribosomal subunit
Gene name | era |
Synonyms | bex, yqfH |
Essential | yes PubMed |
Product | GTP-binding protein |
Function | ribosome assembly |
Gene expression levels in SubtiExpress: era | |
MW, pI | 33 kDa, 8.376 |
Gene length, protein length | 903 bp, 301 aa |
Immediate neighbours | yqzL, cdd |
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
translation, essential genes, GTP-binding proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU25290
Phenotypes of a mutant
essential PubMed
Database entries
- BsubCyc: BSU25290
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Binds and hydrolyzes GTP and readily exchanges GDP for GTP
- Protein family: Era subfamily (according to Swiss-Prot) Era/Obg family
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- BsubCyc: BSU25290
- Structure: 3IEV (Era from Aquifex aeolicus, 50% identity/ 77% similarity, complex with the 3' end of 16S rRNA) PubMed
- UniProt: P42182
- 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:
- Antibody:
Labs working on this gene/protein
Naotake Ogasawara, Nara, Japan
Your additional remarks
References
Reviews
Natalie Verstraeten, Maarten Fauvart, Wim Versées, Jan Michiels
The universally conserved prokaryotic GTPases.
Microbiol Mol Biol Rev: 2011, 75(3);507-42, second and third pages of table of contents
[PubMed:21885683]
[WorldCat.org]
[DOI]
(I p)
Robert A Britton
Role of GTPases in bacterial ribosome assembly.
Annu Rev Microbiol: 2009, 63;155-76
[PubMed:19575570]
[WorldCat.org]
[DOI]
(I p)
Original publications
Chao Tu, Xiaomei Zhou, Joseph E Tropea, Brian P Austin, David S Waugh, Donald L Court, Xinhua Ji
Structure of ERA in complex with the 3' end of 16S rRNA: implications for ribosome biogenesis.
Proc Natl Acad Sci U S A: 2009, 106(35);14843-8
[PubMed:19706445]
[WorldCat.org]
[DOI]
(I p)
Takuya Morimoto, Pek Chin Loh, Tomohiro Hirai, Kei Asai, Kazuo Kobayashi, Shigeki Moriya, Naotake Ogasawara
Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis.
Microbiology (Reading): 2002, 148(Pt 11);3539-3552
[PubMed:12427945]
[WorldCat.org]
[DOI]
(P p)
P Z Wang, R H Doi
Overlapping promoters transcribed by bacillus subtilis sigma 55 and sigma 37 RNA polymerase holoenzymes during growth and stationary phases.
J Biol Chem: 1984, 259(13);8619-25
[PubMed:6330116]
[WorldCat.org]
(P p)