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| * '''Description:''' ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein) <br/><br/>
| | {{#bank: ClpP}} |
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| {| align="right" border="1" cellpadding="2"
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| |style="background:#ABCDEF;" align="center"|'''Gene name'''
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| |''clpP''
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| |-
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| |style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''yvdN ''
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| |-
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| |style="background:#ABCDEF;" align="center"| '''Essential''' || no
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| |-
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| |style="background:#ABCDEF;" align="center"| '''Product''' || ATP-dependent Clp protease proteolytic subunit
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| |-
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| |style="background:#ABCDEF;" align="center"|'''Function''' || protein degradation
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| |-
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| |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU34540 clpP]
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| |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=ClpP ClpP]
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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/subtipathways/search.php?enzyme=clpP clpP]'''
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| |-
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| |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 21 kDa, 5.008
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| |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 591 bp, 197 aa
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| |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[trnQ-Arg]]'', ''[[pgcM]]''
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| |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU34540 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU34540 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU34540 DNA_with_flanks]
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| |colspan="2" | '''Genetic context''' <br/> [[Image:clpP_context.gif]]
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| <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
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| |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=clpP_3546234_3546827_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:clpP_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU34540]]
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| |-
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| |}
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| __TOC__
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| <br/><br/><br/><br/>
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| <br/><br/><br/><br/>
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| <br/><br/><br/><br/>
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| <br/><br/>
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| = [[Categories]] containing this gene/protein =
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| {{SubtiWiki category|[[proteolysis]]}},
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| {{SubtiWiki category|[[general stress proteins (controlled by SigB)]]}},
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| {{SubtiWiki category|[[heat shock proteins]]}},
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| {{SubtiWiki category|[[phosphoproteins]]}},
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| [[most abundant proteins]]
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| = This gene is a member of the following [[regulons]] =
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| {{SubtiWiki regulon|[[CtsR regulon]]}},
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| {{SubtiWiki regulon|[[SigB regulon]]}}
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|
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| =The gene=
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| === Basic information ===
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| * '''Locus tag:''' BSU34540
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| ===Phenotypes of a mutant ===
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| * increased thermotolerance due to increased stabiliy of [[Spx]] and thus increased expression of ''[[trxA]]'' {{PubMed|24417481}}
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| === Database entries ===
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| * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU34540&redirect=T BSU34540]
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| * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/clpP.html]
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| * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG19016]
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| === Additional information===
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| =The protein=
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| === Basic information/ Evolution ===
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| * '''Catalyzed reaction/ biological activity:''' Hydrolysis of proteins to small peptides in the presence of ATP and magnesium (according to Swiss-Prot) endopeptidase/proteolysis
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| * '''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]
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| * '''Paralogous protein(s):'''
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| === Targets of [[ClpC]]-[[ClpP]]-dependent protein degradation ===
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| * [[DegU]]-P {{PubMed|20070525}}, [[MurAA]] {{PubMed|14763982}}, [[ComK]] {{PubMed|9890793}}, [[CtsR]] {{PubMed|17380125}}, [[Mdh]], [[MgsR]] {{PubMed|22812682}}
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| === Targets of [[ClpX]]-[[ClpP]]-dependent protein degradation ===
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| * [[MgsR]] {{PubMed|22812682}}
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| === Extended information on the protein ===
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| * '''Kinetic information:'''
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| * '''[[Domains]]:'''
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| * '''Modification:'''
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| ** phosphorylated on Arg-13 {{PubMed|22517742}}
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| * '''[[Cofactors]]:'''
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| * '''Effectors of protein activity:'''
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| ** the novel antibiotic ADEP (acyldepsipeptides) dysregulates [[ClpP]] activity and allows [[FtsZ]] degradation in the absence of an ATPase subunit ([[ClpC]], [[ClpE]], or [[ClpX]]) {{PubMed|21969594}}
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| * '''[[SubtInteract|Interactions]]:'''
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| ** [[ClpE]]-[[ClpP]], [[ClpC]]-[[ClpP]], [[ClpX]]-[[ClpP]]
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| ** [[CtsR]]-[[ClpP]]/[[ClpC]] (degradation of [[CtsR]]) {{PubMed|11179229,16163393,17380125}}
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| ** [[McsB]]-[[ClpP]]/[[ClpC]] (rapid degradation of non-phosphorylated [[McsB]]) {{PubMed|20852588}}
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| ** [[Spx]]-[[ClpP]]/[[ClpX]] (degradation of [[Spx]]) {{PubMed|17827297}}
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| * '''[[Localization]]:'''
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| ** cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heat shock, colocalization with [[ClpX]], [[ClpC]] and [[ClpE]] {{PubMed|18786145,18689473}}
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| [[File:ClpP.jpg ]]
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| === Database entries ===
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| * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU34540&redirect=T BSU34540]
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| * '''Structure:''' [http://www.pdb.org/pdb/search/structidSearch.do?structureId=3KTG 3KTG] {{PubMed|20305655}}
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| * '''UniProt:''' [http://www.uniprot.org/uniprot/P80244 P80244]
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| * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU34540]
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| * '''E.C. number:''' [http://www.expasy.org/enzyme/3.4.21.92 3.4.21.92]
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| === Additional information===
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| =Expression and regulation=
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| * '''Operon:''' ''clpP'' {{PubMed|9643546}}
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| * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=clpP_3546234_3546827_1 clpP] {{PubMed|22383849}}
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| * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|9643546}}, [[SigB]] {{PubMed|9643546,11544224}}
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| * '''Regulation:'''
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| ** induced by stress ([[SigB]]) {{PubMed|9643546,11544224}}
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| ** induced by heat ([[CtsR]]) {{PubMed|9987115}}
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| * '''Regulatory mechanism:'''
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| ** [[CtsR]]: transcription repression {{PubMed|9987115,11179229,16163393,17380125}}
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| * '''Additional information:'''
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| ** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
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| ** number of protein molecules per cell (minimal medium with glucose and ammonium): 4011 {{PubMed|24696501}}
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| ** number of protein molecules per cell (complex medium with amino acids, without glucose): 11118 {{PubMed|24696501}}
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| ** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1536 {{PubMed|21395229}}
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| ** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 731 {{PubMed|21395229}}
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| ** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1056 {{PubMed|21395229}}
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| =Biological materials =
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| * '''Mutant:'''
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| ** ''clpP::spec'' and ''clpP::cat'', available in the [[Leendert Hamoen]] lab
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| ** BP99 (''clpP''::''tet''), available in [[Fabian Commichau]]'s lab {{PubMed|25610436}}
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| ** GP551 (spc), available in [[Jörg Stülke]]'s lab
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| ** 1S139 (''clpP''::''erm''), available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S139&Search=1S139 BGSC]
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| ** 1S140 ( ''clpP''::''spec''), available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S140&Search=1S140 BGSC]
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| ** BKE34540 (''[[clpP]]''::''erm'', available in the BGSC and in [[Jörg Stülke]]'s lab)
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| * '''Expression vector:'''
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| * '''lacZ fusion:'''
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| * '''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 [[Leendert Hamoen]] lab
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| * '''two-hybrid system:'''
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| * '''Antibody:''' available in [[Ulf Gerth]]'s and [[Jörg Stülke]]'s labs
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| =Labs working on this gene/protein=
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| * [[Leendert Hamoen]], Newcastle University, UK [http://www.ncl.ac.uk/camb/staff/profile/l.hamoen homepage]
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| =Your additional remarks=
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| =References=
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| ==Reviews==
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| <pubmed> 16211032 17302811 23375660 23479438,19609260,19781636</pubmed>
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| ==Original Publications==
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| <pubmed>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</pubmed>
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| [[Category:Protein-coding genes]]
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