Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | ATP-dependent Clp protease proteolytic subunit |
Protein Synonyms/Alias | |
Gene Name | clpP |
Gene Synonyms/Alias | yvdN; OrderedLocusNames=BSU34540 |
Created Date | 3-June-2014 |
Organism | Bacillus subtilis (strain 168) |
NCBI Taxa ID | 224308 |
Phosphorylation | Position | Peptide | Code | Type | References | 13 | TVIEQTNRGERAYDI | R | HTP | [1] | 11 | IPTVIEQTNRGERAY | T | HTP | [1] | 16 | EQTNRGERAYDIYSR | R | HTP | [1] | |
Reference | [1]Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis. Elsholz AK,Turgay K,Michalik S,Hessling B,Gronau K,Oertel D,Mäder U,Bernhardt J,Becher D,Hecker M,Gerth U Proc. Natl. Acad. Sci. U.S.A. 2012, May, 8;109(19):7451-6. [ PMID:22517742] |
Functional Description From UniProt | FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor |
| |
| 3D-structure; Completeproteome; Cytoplasm; Directproteinsequencing; Hydrolase; Protease; Referenceproteome; Serineprotease; Stressresponse |
Protein Sequence | MNLIPTVIEQ TNRGERAYDI YSRLLKDRII MLGSAIDDNV ANSIVSQLLF LAAEDPEKEI 60 SLYINSPGGS ITAGMAIYDT MQFIKPKVST ICIGMAASMG AFLLAAGEKG KRYALPNSEV 120 MIHQPLGGAQ GQATEIEIAA KRILLLRDKL NKVLAERTGQ PLEVIERDTD RDNFKSAEEA 180 LEYGLIDKIL THTEDKK 197 |
| GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell GO:0005524 F:ATP binding IEA:UniProtKB-KW GO:0004176 F:ATP-dependent peptidase activity IMP:CACAO GO:0004252 F:serine-type endopeptidase activity IEA:UniProtKB-HAMAP GO:0006200 P:ATP catabolic process IMP:GOC GO:0006950 P:response to stress IEA:UniProtKB-KW |
| |
| |
| |
| |
| |