ID   A2CB85_PROM3            Unreviewed;       200 AA.
AC   A2CB85;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   02-SEP-2026, entry version 118.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|RuleBase:RU003567};
DE            EC=3.4.21.92 {ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|RuleBase:RU000549};
DE   AltName: Full=Endopeptidase Clp {ECO:0000256|HAMAP-Rule:MF_00444};
GN   Name=clpP {ECO:0000256|HAMAP-Rule:MF_00444};
GN   OrderedLocusNames=P9303_20031 {ECO:0000313|EMBL:ABM78745.1};
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=59922 {ECO:0000313|EMBL:ABM78745.1, ECO:0000313|Proteomes:UP000002274};
RN   [1] {ECO:0000313|EMBL:ABM78745.1, ECO:0000313|Proteomes:UP000002274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303 {ECO:0000313|EMBL:ABM78745.1,
RC   ECO:0000313|Proteomes:UP000002274};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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:0000256|HAMAP-Rule:MF_00444, ECO:0000256|RuleBase:RU000550}.
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:0000256|ARBA:ARBA00034021,
CC         ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|PROSITE-
CC         ProRule:PRU10086};
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:0000256|HAMAP-
CC       Rule:MF_00444}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00444}.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family.
CC       {ECO:0000256|ARBA:ARBA00007039, ECO:0000256|HAMAP-Rule:MF_00444,
CC       ECO:0000256|RuleBase:RU003567}.
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DR   EMBL; CP000554; ABM78745.1; -; Genomic_DNA.
DR   RefSeq; WP_011826624.1; NC_008820.1.
DR   AlphaFoldDB; A2CB85; -.
DR   STRING; 59922.P9303_20031; -.
DR   MEROPS; S14.001; -.
DR   KEGG; pmf:P9303_20031; -.
DR   HOGENOM; CLU_058707_3_2_3; -.
DR   BioCyc; PMAR59922:G1G80-1743-MONOMER; -.
DR   Proteomes; UP000002274; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009368; C:endopeptidase Clp complex; IEA:TreeGrafter.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0051117; F:ATPase binding; IEA:TreeGrafter.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:TreeGrafter.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   CDD; cd07017; S14_ClpP_2; 1.
DR   FunFam; 3.90.226.10:FF:000001; ATP-dependent Clp protease proteolytic subunit; 1.
DR   Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 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   NCBIfam; NF001368; PRK00277.1; 1.
DR   NCBIfam; NF009205; PRK12553.1; 1.
DR   PANTHER; PTHR10381; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10381:SF70; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR   PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00444};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00444};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00444};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002274};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW   Rule:MF_00444}.
FT   ACT_SITE        101
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10085"
FT   ACT_SITE        101
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00444"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00444,
FT                   ECO:0000256|PROSITE-ProRule:PRU10086"
SQ   SEQUENCE   200 AA;  22038 MW;  46A5CE4A14B16BD2 CRC64;
     MPIGTPSVPY RLPGSQMERW VDIYTRLGVE RILFLGQEVS DGVANSLVAQ MLYLDSEDST
     KPIYLYINSP GGSVTAGLAI YDTMKYVKSD VVTICVGLAA SMGAFLLTAG TKGKRLALPH
     SRIMIHQPLG GTNQRQASDI EIEAREILRI KDMLNHSMAE LTGQTFEKIE KDTDRDYFLS
     AAEAKDYGLI DRVIAHPNEA
//