ID   A4XAI0_SALTO            Unreviewed;       220 AA.
AC   A4XAI0;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   02-SEP-2026, entry version 105.
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};
DE   AltName: Full=Endopeptidase Clp {ECO:0000256|HAMAP-Rule:MF_00444};
GN   Name=clpP {ECO:0000256|HAMAP-Rule:MF_00444};
GN   OrderedLocusNames=Strop_3498 {ECO:0000313|EMBL:ABP55929.1};
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC
OS   105044 / CNB-440).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Salinispora.
OX   NCBI_TaxID=369723 {ECO:0000313|EMBL:ABP55929.1, ECO:0000313|Proteomes:UP000000235};
RN   [1] {ECO:0000313|Proteomes:UP000000235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440
RC   {ECO:0000313|Proteomes:UP000000235};
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(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}.
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|HAMAP-Rule:MF_00444,
CC         ECO:0000256|PROSITE-ProRule:PRU10085};
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; CP000667; ABP55929.1; -; Genomic_DNA.
DR   RefSeq; WP_012014704.1; NC_009380.1.
DR   AlphaFoldDB; A4XAI0; -.
DR   STRING; 369723.Strop_3498; -.
DR   MEROPS; S14.009; -.
DR   KEGG; stp:Strop_3498; -.
DR   PATRIC; fig|369723.5.peg.3612; -.
DR   eggNOG; COG0740; Bacteria.
DR   HOGENOM; CLU_058707_3_2_11; -.
DR   Proteomes; UP000000235; 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:000002; 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; 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:SF26; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT-LIKE-RELATED; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {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:UP000000235};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW   Rule:MF_00444}.
FT   ACT_SITE        113
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10085"
FT   ACT_SITE        113
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00444"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00444"
SQ   SEQUENCE   220 AA;  24316 MW;  0FF17FE1C492551E CRC64;
     MTDLSLPPQF AAVHNRYVLP SFVERTSYGV KESNPYNKLF EDRIIFLGVQ VDDASANDVM
     AQLLTLEGTD PDRDIIMYIN SPGGSFTAMT AIYDTMQYVR PDIQTVCLGQ AASAAAMLLS
     AGTPGKRMAL PNSRIIIHQP ATEGGYGQGS DIEIQAREIL RMRTQLEEML SRHCNQPVEK
     VRKDIDRDKI MTAEESREYG LVDTILTSRK KGLLAANAAS
//