ID   R9ZSL3_9FABA            Unreviewed;       196 AA.
AC   R9ZSL3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   22-FEB-2023, entry version 45.
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   ECO:0000313|EMBL:AGO44347.1};
OS   Glycine stenophita.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AGO44347.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Glycine.
OX   NCBI_TaxID=96944 {ECO:0000313|EMBL:AGO44347.1};
RN   [1] {ECO:0000313|EMBL:AGO44347.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Sherman-Broyles S., Bombarely A., Grimwood J., Schmutz J., Jackson S.,
RA   Doyle J.;
RT   "Comparative analysis of complete chloroplast sequences from seven
RT   perennial wild relatives of Glycine max.";
RL   Submitted (APR-2013) 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:0000256|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:0000256|ARBA:ARBA00034021,
CC         ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|PROSITE-
CC         ProRule:PRU10086};
CC   -!- SUBUNIT: Component of the chloroplastic Clp protease core complex.
CC       {ECO:0000256|HAMAP-Rule:MF_00444}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000256|HAMAP-
CC       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; KC893634; AGO44347.1; -; Genomic_DNA.
DR   RefSeq; YP_008145816.1; NC_021646.1.
DR   AlphaFoldDB; R9ZSL3; -.
DR   SMR; R9ZSL3; -.
DR   GeneID; 16793779; -.
DR   GO; GO:0009570; C:chloroplast stroma; 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; IPR033135; ClpP_His_AS.
DR   InterPro; IPR018215; ClpP_Ser_AS.
DR   PANTHER; PTHR10381; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10381:SF15; CHLOROPLASTIC ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1; 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   Chloroplast {ECO:0000313|EMBL:AGO44347.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00444};
KW   Plastid {ECO:0000313|EMBL:AGO44347.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00444};
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   196 AA;  22106 MW;  68A8F3B77F947AEC CRC64;
     MPIGVPRVPF RSPGEEDASW VDIYNRLYRE RLLFLGQEVD SEISNQLISL MVYLSIEEEN
     KDLYLFINSP GGWVIPGIAI YDTMQFVQPD VQTVCMGLAA SMGSFLLAGG EITKRLAFPH
     ARVMIHQPAS SFYEAQTGEF ILEAEELLKM RETITRVYVQ RTGKPLWVIS EDMERDVFMS
     AAEAQAHGIV DLVAVE
//