Difference between revisions of "Sfp/2"
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− | + | * '''Description:''' 4'-phosphopantetheine transferases transferase, inactive pseudogene in strain 168<br/><br/> | |
− | * '''Description:''' | ||
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"|'''Gene name''' | |style="background:#ABCDEF;" align="center"|'''Gene name''' | ||
− | |''sfp/ | + | |''sfp/1'' |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' '' | + | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''sfp'' |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Essential''' || | + | |style="background:#ABCDEF;" align="center"| '''Essential''' || no |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Product''' || | + | |style="background:#ABCDEF;" align="center"| '''Product''' || 4'-phosphopantetheine transferase |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || | + | |style="background:#ABCDEF;" align="center"|'''Function''' || phosphopantetheinylates a serine residue in each<br/> of the seven peptidyl carrier protein domains of the <br/>first three subunits of surfactin synthetase ([[SrfAA]]-[[SrfAB]]-[[SrfAC]]) and [[AcpK]] |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || | + | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 19 kDa, 8.38 |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || | + | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 495 bp, 165 aa |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ycxD]]'', ''[[sfp/1]]'' |
|- | |- | ||
− | |style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/ | + | |style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/sfp_nucleotide.txt Gene sequence (+200bp) ]''' |
− | |style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/ | + | |style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/sfp_protein.txt Protein sequence]''' |
|- | |- | ||
− | |colspan="2" | '''Genetic context''' <br/> [[Image: | + | |colspan="2" style="background:#FAF8CC;color:#FF0000" align="center" | '''Caution: The sequence for this gene in SubtiList contains errors |
+ | |- | ||
+ | |colspan="2" | '''Genetic context''' <br/> [[Image:sfp_context.gif]] | ||
+ | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
|- | |- | ||
|} | |} | ||
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__TOC__ | __TOC__ | ||
− | <br/><br/> | + | <br/><br/><br/><br/><br/> |
= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
+ | {{SubtiWiki category|[[miscellaneous metabolic pathways]]}}, | ||
+ | {{SubtiWiki category|[[biofilm formation]]}}, | ||
+ | {{SubtiWiki category|[[biosynthesis of antibacterial compounds]]}}, | ||
{{SubtiWiki category|[[pseudogenes]]}} | {{SubtiWiki category|[[pseudogenes]]}} | ||
Line 42: | Line 47: | ||
=== Basic information === | === Basic information === | ||
− | * '''Locus tag:''' | + | * '''Locus tag:''' BSU03570 |
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
+ | |||
+ | No swarming motility on B medium. [http://www.ncbi.nlm.nih.gov/sites/entrez/19202088 PubMed] | ||
=== Database entries === | === Database entries === | ||
Line 50: | Line 57: | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
− | * '''SubtiList entry:''' | + | * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10176] |
=== Additional information=== | === 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]]''. | ||
+ | * Correction of ''[[sfp]]'', ''[[epsC]]'','' [[swrAA]]'', and ''[[degQ]]'' as well as introduction of ''rapP'' from a plasmid present in NCIB3610 results in biofilm formation in ''B. subtilis'' 168 {{PubMed|21278284}} | ||
Line 60: | Line 69: | ||
=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' | + | * '''Catalyzed reaction/ biological activity:''' CoA + apo-[peptidyl-carrier protein] = adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein] (according to Swiss-Prot) |
− | * '''Protein family:''' | + | * '''Protein family:''' Gsp/sfp/hetI/acpT family (according to Swiss-Prot) |
* '''Paralogous protein(s):''' | * '''Paralogous protein(s):''' | ||
Line 84: | Line 93: | ||
=== Database entries === | === Database entries === | ||
− | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1QR0 1QR0] (complex with CoA) |
* '''Swiss prot entry:''' | * '''Swiss prot entry:''' | ||
− | * '''KEGG entry:''' | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU03570] |
* '''E.C. number:''' | * '''E.C. number:''' | ||
Line 98: | Line 107: | ||
* '''Operon:''' | * '''Operon:''' | ||
− | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
* '''Regulation:''' | * '''Regulation:''' | ||
Line 111: | Line 120: | ||
* '''Expression vector:''' | * '''Expression vector:''' | ||
− | + | ||
* '''lacZ fusion:''' | * '''lacZ fusion:''' | ||
Line 121: | Line 130: | ||
=Labs working on this gene/protein= | =Labs working on this gene/protein= | ||
+ | |||
+ | [[Mohamed Marahiel]], Marburg University, Germany [http://www.uni-marburg.de/fb15/fachgebiete/bio/marahiel?language_sync=1 homepage] | ||
=Your additional remarks= | =Your additional remarks= | ||
=References= | =References= | ||
− | + | ==Reviews== | |
− | + | <pubmed>20735481 </pubmed> | |
+ | ==Original publications== | ||
+ | <pubmed>15955059,19202088,2848009,11489886,15065855,10581256,15066026,11867633,19202088, 19749039 20094656 9484229 20148996 21278284 21466506 </pubmed> | ||
[[Category:Pseudogenes]] | [[Category:Pseudogenes]] |
Revision as of 19:38, 19 April 2011
- 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, sfp/1 |
Gene sequence (+200bp) | Protein sequence |
Caution: The sequence for this gene in SubtiList contains errors | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
miscellaneous metabolic pathways, biofilm formation, biosynthesis of antibacterial compounds, pseudogenes
This gene is a member of the following regulons
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.
- Correction of sfp, epsC, swrAA, and degQ as well as introduction of rapP from a plasmid present in NCIB3610 results in biofilm formation in B. subtilis 168 PubMed
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
Massimiliano Marvasi, Pieter T Visscher, Lilliam Casillas Martinez
Exopolymeric substances (EPS) from Bacillus subtilis: polymers and genes encoding their synthesis.
FEMS Microbiol Lett: 2010, 313(1);1-9
[PubMed:20735481]
[WorldCat.org]
[DOI]
(I p)
Original publications
Jeremy G Owen, Janine N Copp, David F Ackerley
Rapid and flexible biochemical assays for evaluating 4'-phosphopantetheinyl transferase activity.
Biochem J: 2011, 436(3);709-17
[PubMed:21466506]
[WorldCat.org]
[DOI]
(I p)
Anna L McLoon, Sarah B Guttenplan, Daniel B Kearns, Roberto Kolter, Richard Losick
Tracing the domestication of a biofilm-forming bacterium.
J Bacteriol: 2011, 193(8);2027-34
[PubMed:21278284]
[WorldCat.org]
[DOI]
(I p)
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)