Difference between revisions of "CopA"
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=== Additional information=== | === Additional information=== | ||
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=The protein= | =The protein= | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
** two N-terminal soluble domains, CopAa and CopAb, connected by a short linker | ** two N-terminal soluble domains, CopAa and CopAb, connected by a short linker | ||
* '''Modification:''' | * '''Modification:''' | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2RML 2RML] ( N-terminal soluble domain) | + | * '''Structure:''' |
| + | ** [http://www.rcsb.org/pdb/explore.do?structureId=2RML 2RML] ( N-terminal soluble domain) | ||
| + | ** [http://www.pdb.org/pdb/explore/explore.do?structureId=4BBJ 4BBJ] (the protein from Legionella pneumophila, 45% identity, 79% similarity) {{PubMed|24317491}} | ||
* '''UniProt:''' [http://www.uniprot.org/uniprot/O32220 O32220] | * '''UniProt:''' [http://www.uniprot.org/uniprot/O32220 O32220] | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=copA_3441121_3443529_-1 copA] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=copA_3441121_3443529_-1 copA] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' [[SigA]] {{PubMed|12779235}} | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|12779235}} |
| + | |||
* '''Regulation:''' | * '''Regulation:''' | ||
** induced by copper ([[CsoR]]) {{PubMed|18048925,12779235}} | ** induced by copper ([[CsoR]]) {{PubMed|18048925,12779235}} | ||
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==Original publications== | ==Original publications== | ||
| − | + | <pubmed>19751213 11922674,12590580,14663075,12779235,12644235,18048925,14514665,14711369, 19378562 15212800 20233928 24317491 22531974,22077885</pubmed> | |
| − | <pubmed>19751213 11922674,12590580,14663075,12779235,12644235,18048925,14514665,14711369, 19378562 15212800 20233928 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 13:33, 8 January 2014
- Description: copper-transporting ATPase, resistance to copper
| Gene name | copA |
| Synonyms | yvgX |
| Essential | no |
| Product | copper transporting ATPase |
| Function | copper export, detoxification |
| Gene expression levels in SubtiExpress: copA | |
| Interactions involving this protein in SubtInteract: CopA | |
| Metabolic function and regulation of this protein in SubtiPathways: metal ion homeostasis | |
| MW, pI | 85 kDa, 5.484 |
| Gene length, protein length | 2409 bp, 803 aa |
| Immediate neighbours | cadA, copZ |
| 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
transporters/ other, trace metal homeostasis (Cu, Zn, Ni, Mn, Mo), resistance against toxic metals, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU33500
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + H2O + Cu1+(In) = ADP + phosphate + Cu1+(Out) (according to Swiss-Prot)
- Protein family: Type IB subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- two N-terminal soluble domains, CopAa and CopAb, connected by a short linker
- Modification:
- Effectors of protein activity:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: O32220
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
John Helmann, Cornell University, USA Homepage
Your additional remarks
References
Reviews
Original publications
Magnus Andersson, Daniel Mattle, Oleg Sitsel, Tetyana Klymchuk, Anna Marie Nielsen, Lisbeth Birk Møller, Stephen H White, Poul Nissen, Pontus Gourdon
Copper-transporting P-type ATPases use a unique ion-release pathway.
Nat Struct Mol Biol: 2014, 21(1);43-8
[PubMed:24317491]
[WorldCat.org]
[DOI]
(I p)
Liang Zhou, Chloe Singleton, Nick E Le Brun
CopAb, the second N-terminal soluble domain of Bacillus subtilis CopA, dominates the Cu(I)-binding properties of CopAab.
Dalton Trans: 2012, 41(19);5939-48
[PubMed:22531974]
[WorldCat.org]
[DOI]
(I p)
Liang Zhou, Chloe Singleton, Oliver Hecht, Geoffrey R Moore, Nick E Le Brun
Cu(I)- and proton-binding properties of the first N-terminal soluble domain of Bacillus subtilis CopA.
FEBS J: 2012, 279(2);285-98
[PubMed:22077885]
[WorldCat.org]
[DOI]
(I p)
Shashi Chillappagari, Andreas Seubert, Hein Trip, Oscar P Kuipers, Mohamed A Marahiel, Marcus Miethke
Copper stress affects iron homeostasis by destabilizing iron-sulfur cluster formation in Bacillus subtilis.
J Bacteriol: 2010, 192(10);2512-24
[PubMed:20233928]
[WorldCat.org]
[DOI]
(I p)
Chloe Singleton, Stephen Hearnshaw, Liang Zhou, Nick E Le Brun, Andrew M Hemmings
Mechanistic insights into Cu(I) cluster transfer between the chaperone CopZ and its cognate Cu(I)-transporting P-type ATPase, CopA.
Biochem J: 2009, 424(3);347-56
[PubMed:19751213]
[WorldCat.org]
[DOI]
(I e)
Chloe Singleton, Nick E Le Brun
The N-terminal soluble domains of Bacillus subtilis CopA exhibit a high affinity and capacity for Cu(I) ions.
Dalton Trans: 2009, (4);688-96
[PubMed:19378562]
[WorldCat.org]
[DOI]
(P p)
Gregory T Smaldone, John D Helmann
CsoR regulates the copper efflux operon copZA in Bacillus subtilis.
Microbiology (Reading): 2007, 153(Pt 12);4123-4128
[PubMed:18048925]
[WorldCat.org]
[DOI]
(P p)
Irina M Solovieva, Karl-Dieter Entian
Metalloregulation in Bacillus subtilis: the copZ chromosomal gene is involved in cadmium resistance.
FEMS Microbiol Lett: 2004, 236(1);115-22
[PubMed:15212800]
[WorldCat.org]
[DOI]
(P p)
Gilles P M Borrelly, Claudia A Blindauer, Ralf Schmid, Clive S Butler, Chris E Cooper, Ian Harvey, Peter J Sadler, Nigel J Robinson
A novel copper site in a cyanobacterial metallochaperone.
Biochem J: 2004, 378(Pt 2);293-7
[PubMed:14711369]
[WorldCat.org]
[DOI]
(I p)
Ahmed Gaballa, Min Cao, John D Helmann
Two MerR homologues that affect copper induction of the Bacillus subtilis copZA operon.
Microbiology (Reading): 2003, 149(Pt 12);3413-3421
[PubMed:14663075]
[WorldCat.org]
[DOI]
(P p)
Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Leonardo Gonnelli, Xun-Cheng Su
Structural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilis.
J Biol Chem: 2003, 278(50);50506-13
[PubMed:14514665]
[WorldCat.org]
[DOI]
(P p)
Ahmed Gaballa, John D Helmann
Bacillus subtilis CPx-type ATPases: characterization of Cd, Zn, Co and Cu efflux systems.
Biometals: 2003, 16(4);497-505
[PubMed:12779235]
[WorldCat.org]
[DOI]
(P p)
David S Radford, Margaret A Kihlken, Gilles P M Borrelly, Colin R Harwood, Nick E Le Brun, Jennifer S Cavet
CopZ from Bacillus subtilis interacts in vivo with a copper exporting CPx-type ATPase CopA.
FEMS Microbiol Lett: 2003, 220(1);105-12
[PubMed:12644235]
[WorldCat.org]
[DOI]
(P p)
Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Rebecca Del Conte, Leonardo Gonnelli
Understanding copper trafficking in bacteria: interaction between the copper transport protein CopZ and the N-terminal domain of the copper ATPase CopA from Bacillus subtilis.
Biochemistry: 2003, 42(7);1939-49
[PubMed:12590580]
[WorldCat.org]
[DOI]
(P p)
Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Mariapina D'Onofrio, Leonardo Gonnelli, Frutos Carlos Marhuenda-Egea, Francisco Javier Ruiz-Dueñas
Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded states.
J Mol Biol: 2002, 317(3);415-29
[PubMed:11922674]
[WorldCat.org]
[DOI]
(P p)
