Difference between revisions of "ZnuA"
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|style="background:#ABCDEF;" align="center"|'''Function''' || zinc uptake | |style="background:#ABCDEF;" align="center"|'''Function''' || zinc uptake | ||
|- | |- | ||
− | |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/ | + | |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/ZnuA ZnuA] |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/stress_response.html Stress]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/stress_response.html Stress]''' | ||
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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 957 bp, 319 aa | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 957 bp, 319 aa | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ycdG]]'', ''[[ | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ycdG]]'', ''[[znuC]]'' |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB12079]+-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:CAB12079]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' | ||
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===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
− | + | ** reduced genetic competence, can be rescued by the addition of excess zinc {{PubMed|21813502}} | |
+ | ** reduced expression of the ''[[comFA]]-[[comFB]]-[[comFC]]-[[yvyF]]-[[flgM]]-[[yvyG]]-[[flgK]]-[[flgL]]'' operon {{PubMed|21813502}} | ||
=== Database entries === | === Database entries === | ||
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=== Additional information=== | === Additional information=== | ||
− | |||
− | |||
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' [[ | + | * '''Interactions:''' [[ZnuA]]-[[ZnuB]]-[[ZnuC]] {{PubMed|10092453}} |
* '''Localization:''' | * '''Localization:''' | ||
− | ** associated to the membrane (via [[ | + | ** associated to the membrane (via [[ZnuB]]) {{PubMed|10092453,18763711}} |
** extracellular (signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed] | ** extracellular (signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed] | ||
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=Expression and regulation= | =Expression and regulation= | ||
− | * '''Operon:''' ''[[ | + | * '''Operon:''' ''[[znuA]]-[[znuC]]-[[znuB]]'' {{PubMed|9811636}} |
* '''[[Sigma factor]]:''' [[SigA]] {{PubMed|12426338}} | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|12426338}} | ||
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=References= | =References= | ||
− | <pubmed>12426338,9811636,10092453,,12426338,18957862 18763711, </pubmed> | + | <pubmed>12426338,9811636,10092453, 21813502,12426338,18957862 18763711, </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 11:20, 5 August 2011
- Description: ABC transporter for zinc (binding protein)
Gene name | ycdH |
Synonyms | |
Essential | no |
Product | ABC transporter for zinc (binding protein) |
Function | zinc uptake |
Interactions involving this protein in SubtInteract: ZnuA | |
Metabolic function and regulation of this protein in SubtiPathways: Stress | |
MW, pI | 35 kDa, 5.146 |
Gene length, protein length | 957 bp, 319 aa |
Immediate neighbours | ycdG, znuC |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
ABC transporters, trace metal homeostasis (Cu, Zn, Ni, Mn, Mo), membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU02850
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: bacterial solute-binding protein 9 family (according to Swiss-Prot)
- Paralogous protein(s): MntA
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure: 2O1E
- UniProt: O34966
- KEGG entry: [3]
- 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
Your additional remarks
References
Mitsuo Ogura
ZnuABC and ZosA zinc transporters are differently involved in competence development in Bacillus subtilis.
J Biochem: 2011, 150(6);615-25
[PubMed:21813502]
[WorldCat.org]
[DOI]
(I p)
Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862]
[WorldCat.org]
[DOI]
(I p)
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[WorldCat.org]
[DOI]
(I p)
Ahmed Gaballa, Tao Wang, Rick W Ye, John D Helmann
Functional analysis of the Bacillus subtilis Zur regulon.
J Bacteriol: 2002, 184(23);6508-14
[PubMed:12426338]
[WorldCat.org]
[DOI]
(P p)
Y Quentin, G Fichant, F Denizot
Inventory, assembly and analysis of Bacillus subtilis ABC transport systems.
J Mol Biol: 1999, 287(3);467-84
[PubMed:10092453]
[WorldCat.org]
[DOI]
(P p)
A Gaballa, J D Helmann
Identification of a zinc-specific metalloregulatory protein, Zur, controlling zinc transport operons in Bacillus subtilis.
J Bacteriol: 1998, 180(22);5815-21
[PubMed:9811636]
[WorldCat.org]
[DOI]
(P p)