Difference between revisions of "AcpS"

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|style="background:#ABCDEF;" align="center"|'''Function''' || fatty acid biosynthesis  
 
|style="background:#ABCDEF;" align="center"|'''Function''' || fatty acid biosynthesis  
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/AcpS AcpS]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_synthesis.html Lipid synthesis]'''
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_synthesis.html Lipid synthesis]'''

Revision as of 14:36, 29 July 2011

  • Description: acyl-carrier protein synthase, 4'-phosphopantetheine transferase

Gene name acpS
Synonyms ydcB
Essential yes PubMed
Product acyl-carrier protein synthase
Function fatty acid biosynthesis
Interactions involving this protein in SubtInteract: AcpS
Metabolic function and regulation of this protein in SubtiPathways:
Lipid synthesis
MW, pI 13 kDa, 9.915
Gene length, protein length 363 bp, 121 aa
Immediate neighbours ydcA, ydcC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
AcpS context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

biosynthesis of lipids, essential genes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU04620

Phenotypes of a mutant

essential PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein] (according to Swiss-Prot)
  • Protein family: AcpS family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s): magnesium PubMed
  • Effectors of protein activity:

Database entries

  • KEGG entry: [2]

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

Your additional remarks

References

Reviews

Stephen W White, Jie Zheng, Yong-Mei Zhang, Rock
The structural biology of type II fatty acid biosynthesis.
Annu Rev Biochem: 2005, 74;791-831
[PubMed:15952903] [WorldCat.org] [DOI] (P p)

Original Publications

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)

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 D Parris, L Lin, A Tam, R Mathew, J Hixon, M Stahl, C C Fritz, J Seehra, W S Somers
Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites.
Structure: 2000, 8(8);883-95
[PubMed:10997907] [WorldCat.org] [DOI] (P p)