ID   A0A2M7B5X6_9BACT        Unreviewed;       194 AA.
AC   A0A2M7B5X6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   05-DEC-2018, entry version 4.
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   ECO:0000313|EMBL:PIU98472.1};
GN   ORFNames=COS61_01230 {ECO:0000313|EMBL:PIU98472.1};
OS   Candidatus Wolfebacteria bacterium CG03_land_8_20_14_0_80_40_12.
OC   Bacteria; Candidatus Wolfebacteria.
OX   NCBI_TaxID=1975069 {ECO:0000313|EMBL:PIU98472.1, ECO:0000313|Proteomes:UP000228949};
RN   [1] {ECO:0000313|EMBL:PIU98472.1, ECO:0000313|Proteomes:UP000228949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG03_land_8_20_14_0_80_40_12 {ECO:0000313|EMBL:PIU98472.1};
RA   Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.,
RA   Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R.,
RA   Stieglmeier M., Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT   "Depth-based differentiation of microbial function through sediment-
RT   hosted aquifers and enrichment of novel symbionts in the deep
RT   terrestrial subsurface.";
RL   Submitted (SEP-2017) 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
CC         of ATP and magnesium. Alpha-casein is the usual test substrate.
CC         In the absence of ATP, only oligopeptides shorter than five
CC         residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and
CC         Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and
CC         -Tyr-|-Trp bonds also occurs).; EC=3.4.21.92;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|PROSITE-
CC         ProRule:PRU10085, ECO:0000256|SAAS:SAAS01103923};
CC   -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings
CC       which stack back to back to give a disk-like structure with a
CC       central cavity, resembling the structure of eukaryotic
CC       proteasomes. {ECO:0000256|HAMAP-Rule:MF_00444}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00444}.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|RuleBase:RU003567,
CC       ECO:0000256|SAAS:SAAS00674837}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PIU98472.1}.
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DR   EMBL; PEVJ01000028; PIU98472.1; -; Genomic_DNA.
DR   Proteomes; UP000228949; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; 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   Complete proteome {ECO:0000313|Proteomes:UP000228949};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00444};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00444,
KW   ECO:0000256|SAAS:SAAS00674918};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00444,
KW   ECO:0000256|SAAS:SAAS00674844};
KW   Reference proteome {ECO:0000313|Proteomes:UP000228949};
KW   Serine protease {ECO:0000256|HAMAP-Rule:MF_00444,
KW   ECO:0000256|SAAS:SAAS00674861}.
FT   ACT_SITE     98     98       {ECO:0000256|PROSITE-ProRule:PRU10085}.
FT   ACT_SITE     98     98       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00444}.
FT   ACT_SITE    123    123       {ECO:0000256|HAMAP-Rule:MF_00444}.
SQ   SEQUENCE   194 AA;  21308 MW;  BA3401C03F011315 CRC64;
     MDFIPMVIEK NPSGERAYDI YSRLLKERII FIGGPINDAV ANSVIAQMLF LEHEDSKKDI
     TLYLNTPGGA VTAGLAIYDT IQYIKPDIST ICVGLAASMG AVLLAAGAKG KRFILPNSEV
     MLHQVMGEAG GQAVEIEITA RQILKIKDKI NELLAKHTGQ PLSRIEKDTD RDFYLSAQES
     KEYGLVDGII KNKR
//