AAA unfoldase, ATPase subunit of the ClpC-ClpP protease, directs proteins phosphorylated on arginine residues to ClpP
function
protein degradationpositive regulator of autolysin (LytC and LytD) synthesis
product
AAA unfoldase, ATPase subunit of the ClpC-ClpP protease
Genomic Context
categories
[category|SW 1|Cellular processes] → [category|SW 1.1|Cell envelope and cell division] → [category|SW 1.1.5|Cell wall/ other][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 4.2|Sporulation] → [category|SW 4.2.1|Sporulation proteins] → [category|SW 4.2.1.4|Sporulation proteins/ other][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]This gene is a member of the following [SW|regulons]
[SW|CtsR regulon], [SW|SigB regulon], [SW|SigF regulon]Gene
Coordinates
103,572 → 106,004
Phenotypes of a mutant
inactivation of ''[gene|86A2F2F65290F4471D6FD03B694821C66C180D8A|clpC]'' reduces sporulation efficiency to 0.4% that of wild type cells; delayed entry into sporulation, defect in engulfment with reduced SigG activity, and production of small spores [Pubmed|26735940]The protein
Catalyzed reaction/ biological activity
ATPase/chaperoneProtein family
[gene|331993A875907C10C77105FD8DDD86D4412CE405|mecA] family (according to Swiss-Prot) clpA/clpB family. [protein|86A2F2F65290F4471D6FD03B694821C66C180D8A|ClpC] subfamily (according to Swiss-Prot), AAA -type ATPase (IPR013093) [http://www.ebi.ac.uk/interpro/IEntry?ac=IPR013093 InterPro] (PF07724) [http://pfam.sanger.ac.uk/family?acc=PF07724 PFAM]Paralogous protein(s)
[protein|8C5B14FE5E03427F9A598C75D4081FA0D6696299|ClpE], [protein|297F53DAD3351E0C55108DD2C93B78FFB174438C|ClpX][SW|Domains]
AAA-ATPase [http://pfam.sanger.ac.uk/family?acc=PF07724 PFAM]Modification
phosphorylated on Arg-5 and Arg-254 [Pubmed|22517742]Structure
[PDB|2K77] (N-terminal domain)[PDB|3PXG], [PDB|3J3U 3J3U] (the [protein|331993A875907C10C77105FD8DDD86D4412CE405|MecA]-[protein|86A2F2F65290F4471D6FD03B694821C66C180D8A|ClpC] complex) [Pubmed|23595989][SW|Localization]
cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heatshock, colocalization with [protein|CB06A70DE7462CEB7AF5D8C28943C878DD56DE1A|ClpP] [http://www.ncbi.nlm.nih.gov/pubmed/18786145 Pubmed]forms foci coincident with nucleoid edges, usually near cell poles [Pubmed|18689473][[File:ClpC.jpg ]]Additional information
subject to Clp-dependent proteolysis upon glucose starvation [Pubmed|17981983]Expression and Regulation
Operons
genes
[gene|908DB17A39D518E84977250C55825E77FA02E391|ctsR]-[gene|CA0939064E70A97434FA450A69E779FD89880613|mcsA]-[gene|7B1B664A1AE1F641E8E7D9E2894D5C8FFFA92948|mcsB]-[gene|86A2F2F65290F4471D6FD03B694821C66C180D8A|clpC]-[gene|151F226370D225776F3FE7EA4901485095F1AC45|radA]-[gene|2B091CCEE9E34D659771E39B1FC9050A145048AB|disA]
description
[Pubmed|8793870]
sigma factors
[protein|081DF3EE9FA56209D648C7677188C61CE3AA8E41|SigM]: sigma factor, [Pubmed|17434969], in [regulon|081DF3EE9FA56209D648C7677188C61CE3AA8E41|SigM regulon][protein|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA]: sigma factor, [Pubmed|8793870], in [regulon|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA regulon][protein|580011DE5DC40EC9E7E0512791D328FAA010DCB8|SigB]: sigma factor, [pubmed|8793870] [pubmed|11544224], in [regulon|580011DE5DC40EC9E7E0512791D328FAA010DCB8|SigB regulon][protein|CFF318EE6CACDEE763FBF96A2ABB46E944679AAA|SigF]: sigma factor, [Pubmed|16497325], in [regulon|CFF318EE6CACDEE763FBF96A2ABB46E944679AAA|SigF regulon]regulatory mechanism
[protein|908DB17A39D518E84977250C55825E77FA02E391|CtsR]: repression, [pubmed|9987115,11179229,16163393,17380125], in [regulon|908DB17A39D518E84977250C55825E77FA02E391|CtsR regulon][protein|2C6386E9A63F410558D168798D077DF91590F454|Spx]: activation, [pubmed|30962353], in [regulon|2C6386E9A63F410558D168798D077DF91590F454|Spx regulon]regulation
expressed during germination and spore outgrowth [Pubmed|24244006]induction during diamide stress ([protein|2C6386E9A63F410558D168798D077DF91590F454|Spx]) [pubmed|30962353]view in new tabBiological materials
Mutant
''[gene|86A2F2F65290F4471D6FD03B694821C66C180D8A|clpC]::tet'' available from the [http://subtiwiki.uni-goettingen.de/wiki/index.php/Leendert_Hamoen Hamoen] LabBP98 (''clpC''::''spc''), available in [SW|Fabian Commichau]'s lab [Pubmed|25610436]BKE00860 (''clpC''::''erm trpC2'') is available from the [http://bgsc.org Bacillus Genetic Stock Center]GFP fusion
C-terminal GFP fusions (single copy, also as CFP and YFP variants) available from the [http://subtiwiki.uni-goettingen.de/wiki/index.php/Leendert_Hamoen Hamoen] LabAntibody
available in [SW|Ulf Gerth]'s and [SW|Jörg Stülke]'s labsLabs working on this gene/protein
[SW|Leendert Hamoen], Newcastle University, UK [http://www.ncl.ac.uk/camb/staff/profile/l.hamoen homepage][SW|Kürsad Turgay], Freie Universität Berlin, Germany [http://www.biologie.fu-berlin.de/en/microbio/mibi-turg/index.html homepage]References
Reviews
17302811,23375660,23479438,19609260,19781636,26639779 Original Publications
9987115,8016067,9000055,12923101,10447896,9141693,2113920,16497325,19226326,8793870,10809708,14679237,17560370,11684022,8195092,11722737,11914365,12028382,18689476,19361434,9890793,19767395,9987115,11544224,17981983,14763982,8016066,19361434,18689473,20070525,20923420,20852588,22517742,21622759,21368759,21821766,23595989,18786145,16525504,17380125,16163393,12598648,24263382,25610436,26458230,26735940,27014237,27749819