YciC

• Description: putative metallochaperone
  
  

Gene name	yciC
Synonyms
Essential	no
Product	putative metallochaperone
Function	zinc uptake
Gene expression levels in SubtiExpress: yciC
MW, pI	45 kDa, 4.399
Gene length, protein length	1191 bp, 397 aa
Immediate neighbours	yczL, yckA
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

trace metal homeostasis (Cu, Zn, Ni, Mn, Mo), membrane proteins, phosphoproteins

This gene is a member of the following regulons

Zur regulon

The gene

Basic information

• Locus tag: BSU03360

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: cobW C-terminal domain (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-58 PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: membrane associated PubMed

Database entries

• Structure:

• UniProt: P94400

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • yciA-yciB-yciC PubMed
  • yciC PubMed

• Expression browser: yciC PubMed

• Sigma factor:
  • yciA:SigA PubMed
  • yciC:SigA PubMed

• Regulation:
  • yciA: induced by zinc starvation (Zur) PubMed
  • yciC: induced by zinc starvation (Zur) PubMed

• Regulatory mechanism:
  • yciA: Zur: transcription repression in the presence of zinc PubMed
  • yciC: Zur: transcription repression in the presence of zinc PubMed

• 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

References

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [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)

Scott E Gabriel, Faith Miyagi, Ahmed Gaballa, John D Helmann
Regulation of the Bacillus subtilis yciC gene and insights into the DNA-binding specificity of the zinc-sensing metalloregulator Zur.
J Bacteriol: 2008, 190(10);3482-8
[PubMed:18344368] [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)

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)