YusV

• Description: ABC transporter for the siderophores Fe-enterobactin and Fe-bacillibactin, as well as for the siderophores schizokinen and arthrobactin (ATPase)
  
  

Gene name	yusV
Synonyms
Essential	no
Product	ABC transporter for the siderophores Fe-enterobactin, Fe-bacillibactin, schizokinen and arthrobactin (ATPase)
Function	acquisition of iron
Gene expression levels in SubtiExpress: yusV
Interactions involving this protein in SubtInteract: YusV
Metabolic function and regulation of this protein in SubtiPathways: YusV
MW, pI	30 kDa, 5.322
Gene length, protein length	825 bp, 275 aa
Immediate neighbours	yusU, yusW
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed 500px

Categories containing this gene/protein

ABC transporters, acquisition of iron, iron metabolism, membrane proteins

This gene is a member of the following regulons

Fur regulon

The gene

Basic information

• Locus tag: BSU32940

Database entries

• BsubCyc: BSU32940

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: ATPase for the FeuA-FeuB-FeuC siderophore ABC transporter and for the YfhA-YfiY-YfiZ siderophore ABC transporter

• Protein family: ABC transporter family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • YusV-(FeuB-FeuC)-FeuA PubMed
  • YusV-(YfhA-YfiZ)-YfiY PubMed

• Localization: associated to the membrane (via FeuB-FeuC and YfhA-YfiZ) PubMed

Database entries

• BsubCyc: BSU32940

• Structure:
  • 4R9U, the E. coli BtuC-BtuD complex, BtuD shares 32% identity, 57% similarity with YusV, PubMed

• UniProt: O32188

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: yusV PubMed

• Sigma factor:

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

• Regulatory mechanism:
  • Fur: transcription repression PubMed

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 400 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 970 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Vladimir M Korkhov, Samantha A Mireku, Dmitry B Veprintsev, Kaspar P Locher
Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F.
Nat Struct Mol Biol: 2014, 21(12);1097-9
[PubMed:25402482] [WorldCat.org] [DOI] (I p)

Florian Peuckert, Marcus Miethke, Alexander G Albrecht, Lars-Oliver Essen, Mohamed A Marahiel
Structural basis and stereochemistry of triscatecholate siderophore binding by FeuA.
Angew Chem Int Ed Engl: 2009, 48(42);7924-7
[PubMed:19746494] [WorldCat.org] [DOI] (I p)

Juliane Ollinger, Kyung-Bok Song, Haike Antelmann, Michael Hecker, John D Helmann
Role of the Fur regulon in iron transport in Bacillus subtilis.
J Bacteriol: 2006, 188(10);3664-73
[PubMed:16672620] [WorldCat.org] [DOI] (P 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)

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)