FbpB

• Description: Fur-regulated basic protein, acts as RNA chaperone for fsrA, response to iron limitation
  
  

Gene name	fbpB
Synonyms	ydbN
Essential	no
Product	Fur-regulated basic protein, acts as RNA chaperone for fsrA, response to iron limitation
Function	RNA chaperone
Gene expression levels in SubtiExpress: fbpB
MW, pI	6 kDa, 9.9
Gene length, protein length	177 bp, 59 aa
Immediate neighbours	ydbM, fbpA
Sequences	Protein DNA DNA_with_flanks
Genetic context
Expression at a glance   PubMed

Categories containing this gene/protein

acquisition of iron, iron metabolism, RNA chaperones, short peptides

This gene is a member of the following regulons

Fur regulon

The gene

Basic information

• Locus tag: BSU04530

Phenotypes of a mutant

• transcription profile of a fbpA fbpB double mutant strain: GEO PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

• GEO entry: GEO PubMed

Additional information

The sequence of the former ydbN gene was corrected, and does now contain two genes, fbpA and fbpB. PubMed

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: P96609

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: fbpA-fbpB PubMed

• Expression browser: fbpB PubMed

• Sigma factor:

• Regulation:
  • induced upon iron starvation (Fur) PubMed

• Regulatory mechanism:
  • Fur: transcription repression PubMed

• Additional information:
  • The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Gregory T Smaldone, Haike Antelmann, Ahmed Gaballa, John D Helmann
The FsrA sRNA and FbpB protein mediate the iron-dependent induction of the Bacillus subtilis lutABC iron-sulfur-containing oxidases.
J Bacteriol: 2012, 194(10);2586-93
[PubMed:22427629] [WorldCat.org] [DOI] (I p)

Gregory T Smaldone, Olga Revelles, Ahmed Gaballa, Uwe Sauer, Haike Antelmann, John D Helmann
A global investigation of the Bacillus subtilis iron-sparing response identifies major changes in metabolism.
J Bacteriol: 2012, 194(10);2594-605
[PubMed:22389480] [WorldCat.org] [DOI] (I p)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Ahmed Gaballa, Haike Antelmann, Claudio Aguilar, Sukhjit K Khakh, Kyung-Bok Song, Gregory T Smaldone, John D Helmann
The Bacillus subtilis iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins.
Proc Natl Acad Sci U S A: 2008, 105(33);11927-32
[PubMed:18697947] [WorldCat.org] [DOI] (I p)

Noel Baichoo, Tao Wang, Rick Ye, John D Helmann
Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon.
Mol Microbiol: 2002, 45(6);1613-29
[PubMed:12354229] [WorldCat.org] [DOI] (P p)