Hmp

• Description: flavohemoglobin, involved in resistance to nitric oxide (NO), essential for long-term survival under anaerobic conditions
  
  

Gene name	hmp
Synonyms	ykiA
Essential	no
Product	flavohemoglobin
Function	resistance to NO
Metabolic function and regulation of this protein in SubtiPathways: Stress
MW, pI	44 kDa, 5.705
Gene length, protein length	1197 bp, 399 aa
Immediate neighbours	ykhA, ykzH
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

electron transport/ other, resistance against other toxic compounds (nitric oxide, phenolic acids, flavonoids, oxalate)

This gene is a member of the following regulons

NsrR regulon, ResD regulon

The gene

Basic information

• Locus tag: BSU13040

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: 2 NO + 2 O₂ + NAD(P)H = 2 NO₃^- + NAD(P)⁺ (according to Swiss-Prot)

• Protein family: FAD-binding FR-type domain (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: P49852

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: hmp PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • expressed under anaerobic conditions (ResD) PubMed
  • induced by nitric oxide under anaerobic conditions (NsrR) PubMed

• Regulatory mechanism:
  • ResD: transcription activation PubMed
  • NsrR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Falko Hochgräfe, Carmen Wolf, Stephan Fuchs, Manuel Liebeke, Michael Lalk, Susanne Engelmann, Michael Hecker
Nitric oxide stress induces different responses but mediates comparable protein thiol protection in Bacillus subtilis and Staphylococcus aureus.
J Bacteriol: 2008, 190(14);4997-5008
[PubMed:18487332] [WorldCat.org] [DOI] (I p)

Michiko M Nakano
Essential role of flavohemoglobin in long-term anaerobic survival of Bacillus subtilis.
J Bacteriol: 2006, 188(17);6415-8
[PubMed:16923910] [WorldCat.org] [DOI] (P p)

Michiko M Nakano, Hao Geng, Shunji Nakano, Kazuo Kobayashi
The nitric oxide-responsive regulator NsrR controls ResDE-dependent gene expression.
J Bacteriol: 2006, 188(16);5878-87
[PubMed:16885456] [WorldCat.org] [DOI] (P p)

Charles M Moore, Michiko M Nakano, Tao Wang, Rick W Ye, John D Helmann
Response of Bacillus subtilis to nitric oxide and the nitrosating agent sodium nitroprusside.
J Bacteriol: 2004, 186(14);4655-64
[PubMed:15231799] [WorldCat.org] [DOI] (P p)

M M Nakano, Y Zhu, M Lacelle, X Zhang, F M Hulett
Interaction of ResD with regulatory regions of anaerobically induced genes in Bacillus subtilis.
Mol Microbiol: 2000, 37(5);1198-207
[PubMed:10972836] [WorldCat.org] [DOI] (P p)

M LaCelle, M Kumano, K Kurita, K Yamane, P Zuber, M M Nakano
Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis.
J Bacteriol: 1996, 178(13);3803-8
[PubMed:8682784] [WorldCat.org] [DOI] (P p)