CLPP1_STRCO
ID CLPP1_STRCO Reviewed; 219 AA.
AC Q9F315; Q9ZH59;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit 1 {ECO:0000255|HAMAP-Rule:MF_00444};
DE EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE AltName: Full=Endopeptidase Clp 1 {ECO:0000255|HAMAP-Rule:MF_00444};
GN Name=clpP1 {ECO:0000255|HAMAP-Rule:MF_00444}; OrderedLocusNames=SCO2619;
GN ORFNames=SCC80.04c;
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}.
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DR EMBL; AF071885; AAC70947.1; -; Genomic_DNA.
DR EMBL; AL939113; CAC09995.1; -; Genomic_DNA.
DR RefSeq; NP_626855.1; NC_003888.3.
DR RefSeq; WP_003976180.1; NC_003888.3.
DR AlphaFoldDB; Q9F315; -.
DR SMR; Q9F315; -.
DR STRING; 100226.SCO2619; -.
DR MEROPS; S14.008; -.
DR GeneID; 1098053; -.
DR KEGG; sco:SCO2619; -.
DR PATRIC; fig|100226.15.peg.2665; -.
DR eggNOG; COG0740; Bacteria.
DR HOGENOM; CLU_058707_4_1_11; -.
DR InParanoid; Q9F315; -.
DR OMA; TIQAENM; -.
DR PhylomeDB; Q9F315; -.
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 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.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease.
FT CHAIN 1..219
FT /note="ATP-dependent Clp protease proteolytic subunit 1"
FT /id="PRO_0000179664"
FT ACT_SITE 113
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT CONFLICT 125..127
FT /note="GKR -> RQ (in Ref. 1; AAC70947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 219 AA; 23229 MW; 235A828E5B1E0BDD CRC64;
MRRPGAVVRR AGGYVTNLMP SAAGEPSIGG GLGDQVYNRL LGERIIFLGQ PVDDDIANKI
TAQLLLLASD PDKDIFLYIN SPGGSITAGM AIYDTMQYIK NDVVTIAMGL AASMGQFLLS
AGTPGKRFAL PNAEILIHQP SAGLAGSASD IKIHAERLLH TKRRMAELTS QHTGQTIEQI
TRDSDRDRWF DAFEAKEYGL IDDVIATAAG MPGGGGTGA
