Difference between revisions of "FusA"
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− | * '''Description:''' elongation factor G <br/><br/> | + | * '''Description:''' elongation factor G, facilitates movement of tRNA–mRNA by one codon <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
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|style="background:#ABCDEF;" align="center"| '''Product''' || elongation factor G | |style="background:#ABCDEF;" align="center"| '''Product''' || elongation factor G | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || translation | + | |style="background:#ABCDEF;" align="center"|'''Function''' || [[translation]] |
|- | |- | ||
|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=BSU01120 fusA] | |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=BSU01120 fusA] | ||
+ | |- | ||
+ | |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/FusA FusA] | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 76 kDa, 4.615 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 76 kDa, 4.615 | ||
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<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
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<br/><br/> | <br/><br/> | ||
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* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
+ | ** FusA-RplL {{PubMed|23912278}} | ||
+ | ** FusA-RpsL {{PubMed|23912278}} | ||
* '''[[Localization]]:''' cytoplasm (according to Swiss-Prot) | * '''[[Localization]]:''' cytoplasm (according to Swiss-Prot) | ||
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=== Database entries === | === Database entries === | ||
− | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?pdbId=1ELO 1ELO] (from ''Thermus thermophilus'') {{PubMed|8070397}} | + | * '''Structure:''' |
+ | ** [http://www.rcsb.org/pdb/explore/explore.do?pdbId=1ELO 1ELO] (from ''Thermus thermophilus'') {{PubMed|8070397}} | ||
+ | ** [http://www.pdb.org/pdb/explore/explore.do?structureId=4BTC 4BTC], [http://www.pdb.org/pdb/explore/explore.do?structureId=4BTD 4BTD], the ''Thermus thermophilus'' EF-G–[[ribosome]] complex in a pretranslocation state {{PubMed|23912278}} | ||
* '''UniProt:''' [http://www.uniprot.org/uniprot/P80868 P80868] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P80868 P80868] | ||
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* '''Expression vector:''' | * '''Expression vector:''' | ||
− | ** for expression/ purification from ''B. subtilis'' with N-terminal Strep-tag, for [[SPINE]], in [[pGP380]]: pGP840, available in [[Stülke]] lab | + | ** for expression/ purification from ''B. subtilis'' with N-terminal Strep-tag, for [[SPINE]], in [[pGP380]]: pGP840, available in [[Jörg Stülke]]'s lab |
− | ** for expression/ purification from ''E. coli'' with N-terminal His-tag, in [[pWH844]]: pGP848, available in [[Stülke]] lab | + | ** for expression/ purification from ''E. coli'' with N-terminal His-tag, in [[pWH844]]: pGP848, available in [[Jörg Stülke]]'s lab |
* '''lacZ fusion:''' | * '''lacZ fusion:''' | ||
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=References= | =References= | ||
− | <pubmed> 17726680, 17218307 20348921 8070397 </pubmed> | + | <pubmed> 17726680, 17218307 20348921 8070397 23912278</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 11:28, 20 August 2013
- Description: elongation factor G, facilitates movement of tRNA–mRNA by one codon
Gene name | fusA |
Synonyms | fus |
Essential | yes PubMed |
Product | elongation factor G |
Function | translation |
Gene expression levels in SubtiExpress: fusA | |
Interactions involving this protein in SubtInteract: FusA | |
MW, pI | 76 kDa, 4.615 |
Gene length, protein length | 2076 bp, 692 aa |
Immediate neighbours | rpsG, tufA |
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, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU01120
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: hydrolyses GTP
- Protein family: EF-G/EF-2 subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylation on Ser-213 AND Ser-302 AND Ser-569 AND Ser-680 AND (Thr-24 OR Thr-25) AND (Thr-43 OR Ser 48) PubMed, PubMed
- Cofactor(s):
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P80868
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- for expression/ purification from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP840, available in Jörg Stülke's lab
- for expression/ purification from E. coli with N-terminal His-tag, in pWH844: pGP848, available in Jörg Stülke's lab
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Yun Chen, Shu Feng, Veerendra Kumar, Rya Ero, Yong-Gui Gao
Structure of EF-G-ribosome complex in a pretranslocation state.
Nat Struct Mol Biol: 2013, 20(9);1077-84
[PubMed:23912278]
[WorldCat.org]
[DOI]
(I p)
Nina Clementi, Anna Chirkova, Barbara Puffer, Ronald Micura, Norbert Polacek
Atomic mutagenesis reveals A2660 of 23S ribosomal RNA as key to EF-G GTPase activation.
Nat Chem Biol: 2010, 6(5);344-51
[PubMed:20348921]
[WorldCat.org]
[DOI]
(I p)
Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680]
[WorldCat.org]
[DOI]
(P p)
Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307]
[WorldCat.org]
[DOI]
(P p)
A AEvarsson, E Brazhnikov, M Garber, J Zheltonosova, Y Chirgadze, S al-Karadaghi, L A Svensson, A Liljas
Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.
EMBO J: 1994, 13(16);3669-77
[PubMed:8070397]
[WorldCat.org]
[DOI]
(P p)