ID   CLPP2_CHESB             Reviewed;         208 AA.
AC   Q11I48;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit 2 {ECO:0000255|HAMAP-Rule:MF_00444};
DE            EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE   AltName: Full=Endopeptidase Clp 2 {ECO:0000255|HAMAP-Rule:MF_00444};
GN   Name=clpP2 {ECO:0000255|HAMAP-Rule:MF_00444}; OrderedLocusNames=Meso_1531;
OS   Chelativorans sp. (strain BNC1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Chelativorans; unclassified Chelativorans.
OX   NCBI_TaxID=266779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BNC1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL   Submitted (JUN-2006) 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; CP000390; ABG62927.1; -; Genomic_DNA.
DR   RefSeq; WP_011580870.1; NC_008254.1.
DR   AlphaFoldDB; Q11I48; -.
DR   SMR; Q11I48; -.
DR   STRING; 266779.Meso_1531; -.
DR   MEROPS; S14.001; -.
DR   EnsemblBacteria; ABG62927; ABG62927; Meso_1531.
DR   KEGG; mes:Meso_1531; -.
DR   eggNOG; COG0740; Bacteria.
DR   HOGENOM; CLU_058707_3_2_5; -.
DR   OMA; GFKRQDP; -.
DR   OrthoDB; 1728970at2; -.
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   PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Protease; Serine protease.
FT   CHAIN           1..208
FT                   /note="ATP-dependent Clp protease proteolytic subunit 2"
FT                   /id="PRO_0000252826"
FT   ACT_SITE        102
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ   SEQUENCE   208 AA;  23331 MW;  5CB65452E7FAF537 CRC64;
     MRDTMNLIPM VVEQSARGER SFDIFSRLLR ERIIFLNGQV DDNSAALVCA QMLHLEAENP
     KKEIAFYINS PGGVVSSGFA IYDTMQFIKC PVATLCLGTA ASMGSFLLMA GERGMRVALP
     NASIILHQPL GGFQGQASDI ERHAQNVMRH KRRMIRLYAE HCGRAEEDVE RTLDRDFFMT
     AEDAREWGLV DHVYRRRAGD LPLIAPSS