ID   CLPP1_PROM9             Reviewed;         195 AA.
AC   Q31BD5;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
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};
GN   OrderedLocusNames=PMT9312_0750;
OS   Prochlorococcus marinus (strain MIT 9312).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9312;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00444}.
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   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00444}.
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DR   EMBL; CP000111; ABB49810.1; -; Genomic_DNA.
DR   RefSeq; WP_011376305.1; NC_007577.1.
DR   AlphaFoldDB; Q31BD5; -.
DR   SMR; Q31BD5; -.
DR   STRING; 74546.PMT9312_0750; -.
DR   MEROPS; S14.001; -.
DR   EnsemblBacteria; ABB49810; ABB49810; PMT9312_0750.
DR   KEGG; pmi:PMT9312_0750; -.
DR   eggNOG; COG0740; Bacteria.
DR   HOGENOM; CLU_058707_3_2_3; -.
DR   OMA; GIFDTMQ; -.
DR   OrthoDB; 1728970at2; -.
DR   Proteomes; UP000002715; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
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; 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   TIGRFAMs; TIGR00493; clpP; 1.
DR   PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Protease; Serine protease.
FT   CHAIN           1..195
FT                   /note="ATP-dependent Clp protease proteolytic subunit 1"
FT                   /id="PRO_0000236398"
FT   ACT_SITE        96
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT   ACT_SITE        121
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ   SEQUENCE   195 AA;  21796 MW;  C6E24A86703359A4 CRC64;
     MIPLVLEESG GSERVFDIYS RLLRERIIFL GEQVTSETAN RIVAQLLFLE AEDPDKDIYM
     YINSPGGSVY DGLGIFDTMQ HVKPDIHTVC VGLAASMGAF LLAAGTKGKR SSLRHSRIMI
     HQPLGGARGQ ASDIRIQADE ILFLKERLNT ELSERTGKDY ETIKEDTDRD FYMSPSEAVE
     YGLIDLVLDK KPVKV