CLPP2_STRCO
ID CLPP2_STRCO Reviewed; 218 AA.
AC Q9ZH58;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit 2 {ECO:0000255|HAMAP-Rule:MF_00444};
DE EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE AltName: Full=Endopeptidase Clp 2 {ECO:0000255|HAMAP-Rule:MF_00444};
GN Name=clpP2 {ECO:0000255|HAMAP-Rule:MF_00444}; OrderedLocusNames=SCO2618;
GN ORFNames=SCC80.03c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=10320574; DOI=10.1046/j.1365-2958.1999.01364.x;
RA de Crecy-Lagard V., Servant-Moisson P., Viala J., Grandvalet C.,
RA Mazodier P.;
RT "Alteration of the synthesis of the Clp ATP-dependent protease affects
RT morphological and physiological differentiation in Streptomyces.";
RL Mol. Microbiol. 32:505-517(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=19682253; DOI=10.1111/j.1365-2958.2009.06824.x;
RA Kim M.S., Hahn M.Y., Cho Y., Cho S.N., Roe J.H.;
RT "Positive and negative feedback regulatory loops of thiol-oxidative stress
RT response mediated by an unstable isoform of sigmaR in actinomycetes.";
RL Mol. Microbiol. 73:815-825(2009).
CC -!- FUNCTION: Cleaves peptides in various proteins in a process that
CC requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a
CC major role in the degradation of misfolded proteins (By similarity).
CC Probably partially responsible for degradation of ECF sigma factor SigR
CC prime. {ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000269|PubMed:19682253}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins to small peptides in the presence of
CC ATP and magnesium. alpha-casein is the usual test substrate. In the
CC absence of ATP, only oligopeptides shorter than five residues are
CC hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-
CC Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also
CC occurs).; EC=3.4.21.92; Evidence={ECO:0000255|HAMAP-Rule:MF_00444};
CC -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings which
CC stack back to back to give a disk-like structure with a central cavity,
CC resembling the structure of eukaryotic proteasomes. {ECO:0000255|HAMAP-
CC Rule:MF_00444}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}.
CC -!- INDUCTION: Expressed from 2 promoters, 1 of which (clpP2) is positively
CC regulated by the thio-oxidizing agent diamide, probably via SigR.
CC Probably a clpP1-clpP2 operon. {ECO:0000269|PubMed:19682253}.
CC -!- DISRUPTION PHENOTYPE: A double clpP1-clpP2 deletion increases the
CC stability of ECF sigma factor SigR prime from 10 to 23 minutes.
CC {ECO:0000269|PubMed:19682253}.
CC -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP-
CC Rule:MF_00444}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC70948.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAC09994.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF071885; AAC70948.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL939113; CAC09994.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_626854.1; NC_003888.3.
DR AlphaFoldDB; Q9ZH58; -.
DR SMR; Q9ZH58; -.
DR STRING; 100226.SCO2618; -.
DR MEROPS; S14.009; -.
DR GeneID; 1098052; -.
DR KEGG; sco:SCO2618; -.
DR PATRIC; fig|100226.15.peg.2664; -.
DR eggNOG; COG0740; Bacteria.
DR HOGENOM; CLU_058707_3_2_11; -.
DR InParanoid; Q9ZH58; -.
DR PhylomeDB; Q9ZH58; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009368; C:endopeptidase Clp complex; IBA:GO_Central.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR CDD; cd07017; S14_ClpP_2; 1.
DR HAMAP; MF_00444; ClpP; 1.
DR InterPro; IPR001907; ClpP.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR023562; ClpP/TepA.
DR InterPro; IPR033135; ClpP_His_AS.
DR InterPro; IPR018215; ClpP_Ser_AS.
DR PANTHER; PTHR10381; PTHR10381; 1.
DR Pfam; PF00574; CLP_protease; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease.
FT CHAIN 1..218
FT /note="ATP-dependent Clp protease proteolytic subunit 2"
FT /id="PRO_0000179665"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 139
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ SEQUENCE 218 AA; 24180 MW; 67082B89EAC49F2E CRC64;
MRAASQGRYT GPQAESRYVI PRFVERTSQG VREYDPYAKL FEERVIFLGV QIDDASANDV
MAQLLCLESM DPDRDISVYI NSPGGSFTAL TAIYDTMQYV KPDVQTVCMG QAASAAAVLL
AAGTPGKRMA LPNARVLIHQ PYSETGRGQV SDLEIAANEI LRMRSQLEEM LAKHSTTPVE
KIREDIERDK ILTAEDALSY GLIDQIITTR KMDNSSLR
