Difference between revisions of "Cca"
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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1191 bp, 397 aa | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1191 bp, 397 aa | ||
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| − | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[birA]]'', ''[[ | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[birA]]'', ''[[bshA]]'' |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB14161]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' | |colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB14161]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' | ||
Revision as of 10:16, 7 April 2010
- Description: tRNA nucleotidyltransferase, maturation of the single-copy tRNACys, which lacks an encoded CCA 3' end
| Gene name | cca |
| Synonyms | papS, ypjI |
| Essential | yes PubMed |
| Product | tRNA nucleotidyltransferase |
| Function | tRNA modification |
| MW, pI | 45 kDa, 8.041 |
| Gene length, protein length | 1191 bp, 397 aa |
| Immediate neighbours | birA, bshA |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Locus tag: BSU22450
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: ATP + tRNA(n) = diphosphate + tRNA(n+1) (according to Swiss-Prot)
- Protein family: the protein is similar to the E. coli poly(A) polymerase
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 1MIV (Geobacillus stearothermophilus 44% identity)
- UniProt: P42977
- KEGG entry: [2]
- E.C. number: 2.7.7.25
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Juan Campos-Guillén, Jackeline Lizzeta Arvizu-Gómez, George H Jones, Gabriela Olmedo-Alvarez
Characterization of tRNA(Cys) processing in a conditional Bacillus subtilis CCase mutant reveals the participation of RNase R in its quality control.
Microbiology (Reading): 2010, 156(Pt 7);2102-2111
[PubMed:20360175]
[WorldCat.org]
[DOI]
(I p)
Hyundae D Cho, Christophe L M J Verlinde, Alan M Weiner
Reengineering CCA-adding enzymes to function as (U,G)- or dCdCdA-adding enzymes or poly(C,A) and poly(U,G) polymerases.
Proc Natl Acad Sci U S A: 2007, 104(1);54-9
[PubMed:17179213]
[WorldCat.org]
[DOI]
(P p)
Fang Li, Yong Xiong, Jimin Wang, HyunDae D Cho, Kozo Tomita, Alan M Weiner, Thomas A Steitz
Crystal structures of the Bacillus stearothermophilus CCA-adding enzyme and its complexes with ATP or CTP.
Cell: 2002, 111(6);815-24
[PubMed:12526808]
[WorldCat.org]
[DOI]
(P p)
L C Raynal, H M Krisch, A J Carpousis
The Bacillus subtilis nucleotidyltransferase is a tRNA CCA-adding enzyme.
J Bacteriol: 1998, 180(23);6276-82
[PubMed:9829937]
[WorldCat.org]
[DOI]
(P p)
