SubtiBank SubtiBank
clpP [Wed Mar 30 2016 16:59:26 GMT+0200 (CEST)]
You are currently viewing an outdated version of SubtiWiki. Please use the newest version!

clpP [Wed Mar 30 2016 16:59:26 GMT+0200 (CEST)]

ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein)
locus
BSU34540
pI
5.00
mw
21.00 kDa
function
protein degradation
product
ATP-dependent Clp protease proteolytic subunit
essential
no
ec
3.4.21.92
synonyms
yvdN
Outlinks
KEGGBsubCycSubtiListUniProtExpression Browser

Genomic Context

      

categories

  • [category|SW 3|Information processing] → [category|SW 3.3|Protein synthesis, modification and degradation] → [category|SW 3.3.7|Proteolysis] → [category|SW 3.3.7.4|Additional proteins involved in proteolysis]
  • [category|SW 4|Lifestyles] → [category|SW 4.3|Coping with stress] → [category|SW 4.3.1|General stress proteins (controlled by SigB)]
  • [category|SW 4|Lifestyles] → [category|SW 4.3|Coping with stress] → [category|SW 4.3.4|Heat shock proteins]
  • [category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.1|Phosphorylation on an Arg residue]

    • [SW|Categories] containing this gene/protein

  • [SW|proteolysis], [SW|general stress proteins (controlled by SigB)], [SW|heat shock proteins], [SW|phosphoproteins], [SW|most abundant proteins]

    • This gene is a member of the following [SW|regulons]

  • [SW|CtsR regulon], [SW|SigB regulon]

    • Gene

    Coordinates on the chromosome (coding sequence)
    3,546,234 -> 3,546,827

    Phenotypes of a mutant

  • increased thermotolerance due to increased stabiliy of [protein|search|Spx] and thus increased expression of ''[protein|search|trxA]'' [Pubmed|24417481]
  • the mutation suppresses the heat sensitivity of spores overexpressing ''[SW|cmpA]'' [Pubmed|26387458]
  • non-motile [Pubmed|27014237]

    • The protein

    Catalyzed reaction/ biological activity

  • Hydrolysis of proteins to small peptides in the presence of ATP and magnesium (according to Swiss-Prot) endopeptidase/proteolysis

    • Protein family

  • peptidase S14 family (according to Swiss-Prot) ClpP (IPR001907) [http://www.ebi.ac.uk/interpro/DisplayIproEntry?ac=IPR001907 InterPro], (PF00574) [http://pfam.sanger.ac.uk/family?acc=PF00574 PFAM]

    • Modification

  • phosphorylated on Arg-13 [Pubmed|22517742]

    • Effectors of protein activity

  • the novel antibiotic ADEP (acyldepsipeptides) dysregulates [protein|search|ClpP] activity and allows [protein|search|FtsZ] degradation in the absence of an ATPase subunit ([protein|search|ClpC], [protein|search|ClpE], or [protein|search|ClpX]) [Pubmed|21969594]

    • Structure

  • [PDB|3KTG] [Pubmed|20305655]

    • [SW|Localization]

  • cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heat shock, colocalization with [protein|search|ClpX], [protein|search|ClpC] and [protein|search|ClpE] [Pubmed|18786145,18689473]

    • [SW|Interactions]

  • forms a complex structure of two heptameric rings [Pubmed|26639779]
  • [protein|search|ClpE]-[protein|search|ClpP], [protein|search|ClpC]-[protein|search|ClpP], [protein|search|ClpX]-[protein|search|ClpP]
  • [protein|search|CtsR]-[protein|search|ClpP]/[protein|search|ClpC] (degradation of [protein|search|CtsR]) [Pubmed|11179229,16163393,17380125]
  • [protein|search|McsB]-[protein|search|ClpP]/[protein|search|ClpC] (rapid degradation of non-phosphorylated [protein|search|McsB]) [Pubmed|20852588]
  • [protein|search|Spx]-[protein|search|ClpP]/[protein|search|ClpX] (degradation of [protein|search|Spx]) [Pubmed|17827297]

    • Expression and Regulation

    Operon

  • ''clpP'' [Pubmed|9643546]

    • [SW|Sigma factor]

  • [protein|search|SigA] [Pubmed|9643546], [protein|search|SigB] [Pubmed|9643546,11544224]

    • Regulation

  • induced by stress ([protein|search|SigB]) [Pubmed|9643546,11544224]
  • induced by heat ([protein|search|CtsR]) [Pubmed|9987115]

    • Regulatory mechanism

  • [protein|search|CtsR]: transcription repression [Pubmed|9987115,11179229,16163393,17380125]

    • Additional information

  • belongs to the 100 [SW|most abundant proteins] [PubMed|15378759]

    • Biological materials

    Mutant

  • ''clpP::spec'' and ''clpP::cat'', available in the [SW|Leendert Hamoen] lab
  • BP99 (''clpP''::''tet''), available in [SW|Fabian Commichau]'s lab [Pubmed|25610436]
  • GP551 (spc), available in [SW|Jörg Stülke]'s lab
  • QB4916 (spc), available in [SW|Ulf Gerths]'s and [SW|Jörg Stülke]'s labs
  • 1S139 (''clpP''::''erm''), available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S139&Search=1S139 BGSC]
  • 1S140 ( ''clpP''::''spec''), available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S140&Search=1S140 BGSC]
  • BKE34540 (''[protein|search|clpP]''::''erm'', available in the BGSC and in [SW|Jörg Stülke]'s lab)
  • GP1822 (''[protein|search|clpP]''::''erm'', available in [SW|Jörg Stülke]'s lab)
  • GPUG1 (erm), available in [SW|Ulf Gerth]'s and [SW|Jörg Stülke]'s labs

    • GFP fusion

  • C-terminal GFP fusions (both single copy and as 2th copy in ''amyE'' locus, also as CFP and YFP variants) available in the [SW|Leendert Hamoen] lab

    • Antibody

  • available in [SW|Ulf Gerth]'s and [SW|Jörg Stülke]'s labs

    • Labs working on this gene/protein

  • [SW|Leendert Hamoen], Newcastle University, UK [http://www.ncl.ac.uk/camb/staff/profile/l.hamoen homepage]

    • References

    Reviews

  • 16211032,17302811,23375660,23479438,19609260,19781636,26639779

    • Original Publications

  • 9643546,10809708,11807061,9987115,14679237,18689476,15317791,17586624,11684022,12923101,17560370,16899079,19226326,20070525,9987115,11544224,14763982,9643546,19767395,11112444,9535081,18689473,20305655,20852588,16200071,21969594,22080375,22517742,17380125,12598648,9890793,20049702,20049702,23927726,24263382,24226776,24417481,15378759,23361916,24942655,25212124,25433860,25610436,26387458,27014237