Difference between revisions of "Sfp/1"

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This gene is a pseudogene in ''B. subtilis'' 168 due to a mutation that resulted in an internal frameshift. The second part of the pseudogene is ''[[sfp/2]]''.
 
This gene is a pseudogene in ''B. subtilis'' 168 due to a mutation that resulted in an internal frameshift. The second part of the pseudogene is ''[[sfp/2]]''.
  
 +
 +
= Categories containing this gene/protein =
 +
{{SubtiWiki category|[[miscellaneous metabolic pathways]]}},
 +
{{SubtiWiki category|[[biosynthesis of antibacterial compounds]]}},
 +
{{SubtiWiki category|[[pseudogenes]]}}
 
=The protein=
 
=The protein=
  

Revision as of 19:51, 30 November 2010

  • Description: 4'-phosphopantetheine transferases transferase, inactive pseudogene in strain 168

Gene name sfp/1
Synonyms sfp
Essential no
Product 4'-phosphopantetheine transferase
Function phosphopantetheinylates a serine residue in each
of the seven peptidyl carrier protein domains of the
first three subunits of surfactin synthetase (SrfAA-SrfAB-SrfAC) and AcpK
MW, pI 19 kDa, 8.38
Gene length, protein length 495 bp, 165 aa
Immediate neighbours ycxD, yczE
Gene sequence (+200bp) Protein sequence
Caution: The sequence for this gene in SubtiList contains errors
Genetic context
Sfp context.gif
This image was kindly provided by SubtiList






The gene

Basic information

  • Locus tag: BSU03570

Phenotypes of a mutant

No swarming motility on B medium. PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

This gene is a pseudogene in B. subtilis 168 due to a mutation that resulted in an internal frameshift. The second part of the pseudogene is sfp/2.


Categories containing this gene/protein

miscellaneous metabolic pathways, biosynthesis of antibacterial compounds, pseudogenes

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: CoA + apo-[peptidyl-carrier protein] = adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein] (according to Swiss-Prot)
  • Protein family: Gsp/sfp/hetI/acpT family (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: 1QR0 (complex with CoA)
  • Swiss prot entry:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Mohamed Marahiel, Marburg University, Germany homepage

Your additional remarks

References

Reviews

Original publications

F Coutte, V Leclère, M Béchet, J-S Guez, D Lecouturier, M Chollet-Imbert, P Dhulster, P Jacques
Effect of pps disruption and constitutive expression of srfA on surfactin productivity, spreading and antagonistic properties of Bacillus subtilis 168 derivatives.
J Appl Microbiol: 2010, 109(2);480-491
[PubMed:20148996] [WorldCat.org] [DOI] (I p)

Adam Yasgar, Timothy L Foley, Ajit Jadhav, James Inglese, Michael D Burkart, Anton Simeonov
A strategy to discover inhibitors of Bacillus subtilis surfactin-type phosphopantetheinyl transferase.
Mol Biosyst: 2010, 6(2);365-75
[PubMed:20094656] [WorldCat.org] [DOI] (I p)

Joyce E Patrick, Daniel B Kearns
Laboratory strains of Bacillus subtilis do not exhibit swarming motility.
J Bacteriol: 2009, 191(22);7129-33
[PubMed:19749039] [WorldCat.org] [DOI] (I p)

Kassem Hamze, Daria Julkowska, Sabine Autret, Krzysztof Hinc, Krzysztofa Nagorska, Agnieszka Sekowska, I Barry Holland, Simone J Séror
Identification of genes required for different stages of dendritic swarming in Bacillus subtilis, with a novel role for phrC.
Microbiology (Reading): 2009, 155(Pt 2);398-412
[PubMed:19202088] [WorldCat.org] [DOI] (P p)

Juergen J May, Robert Finking, Frank Wiegeshoff, Thomas T Weber, Nina Bandur, Ulrich Koert, Mohamed A Marahiel
Inhibition of the D-alanine:D-alanyl carrier protein ligase from Bacillus subtilis increases the bacterium's susceptibility to antibiotics that target the cell wall.
FEBS J: 2005, 272(12);2993-3003
[PubMed:15955059] [WorldCat.org] [DOI] (P p)

Daniel B Kearns, Frances Chu, Rivka Rudner, Richard Losick
Genes governing swarming in Bacillus subtilis and evidence for a phase variation mechanism controlling surface motility.
Mol Microbiol: 2004, 52(2);357-69
[PubMed:15066026] [WorldCat.org] [DOI] (P p)

Mohammad Reza Mofid, Robert Finking, Lars Oliver Essen, Mohamed A Marahiel
Structure-based mutational analysis of the 4'-phosphopantetheinyl transferases Sfp from Bacillus subtilis: carrier protein recognition and reaction mechanism.
Biochemistry: 2004, 43(14);4128-36
[PubMed:15065855] [WorldCat.org] [DOI] (P p)

Mohammad Reza Mofid, Robert Finking, Mohamed A Marahiel
Recognition of hybrid peptidyl carrier proteins/acyl carrier proteins in nonribosomal peptide synthetase modules by the 4'-phosphopantetheinyl transferases AcpS and Sfp.
J Biol Chem: 2002, 277(19);17023-31
[PubMed:11867633] [WorldCat.org] [DOI] (P p)

H D Mootz, R Finking, M A Marahiel
4'-phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis.
J Biol Chem: 2001, 276(40);37289-98
[PubMed:11489886] [WorldCat.org] [DOI] (P p)

K Reuter, M R Mofid, M A Marahiel, R Ficner
Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4'-phosphopantetheinyl transferase superfamily.
EMBO J: 1999, 18(23);6823-31
[PubMed:10581256] [WorldCat.org] [DOI] (P p)

L E Quadri, P H Weinreb, M Lei, M M Nakano, P Zuber, C T Walsh
Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases.
Biochemistry: 1998, 37(6);1585-95
[PubMed:9484229] [WorldCat.org] [DOI] (P p)

M M Nakano, M A Marahiel, P Zuber
Identification of a genetic locus required for biosynthesis of the lipopeptide antibiotic surfactin in Bacillus subtilis.
J Bacteriol: 1988, 170(12);5662-8
[PubMed:2848009] [WorldCat.org] [DOI] (P p)