ID   CLPP5_STRCO             Reviewed;         211 AA.
AC   Q9FCC9;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Putative ATP-dependent Clp protease proteolytic subunit-like;
DE   AltName: Full=Endopeptidase Clp-like {ECO:0000255|HAMAP-Rule:MF_00444};
GN   Name=clpP5 {ECO:0000255|HAMAP-Rule:MF_00444}; OrderedLocusNames=SCO1238;
GN   ORFNames=2SCG1.13;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Has lost one of the conserved residue (Ser) proposed to be
CC       part of the active site. Therefore it could be inactive.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00444}.
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DR   EMBL; AL939108; CAC01462.1; -; Genomic_DNA.
DR   RefSeq; NP_625526.1; NC_003888.3.
DR   RefSeq; WP_003977593.1; NZ_VNID01000006.1.
DR   AlphaFoldDB; Q9FCC9; -.
DR   SMR; Q9FCC9; -.
DR   STRING; 100226.SCO1238; -.
DR   MEROPS; S14.009; -.
DR   GeneID; 1096661; -.
DR   KEGG; sco:SCO1238; -.
DR   PATRIC; fig|100226.15.peg.1237; -.
DR   eggNOG; COG0740; Bacteria.
DR   HOGENOM; CLU_058707_3_2_11; -.
DR   InParanoid; Q9FCC9; -.
DR   OMA; QLMYLEH; -.
DR   PhylomeDB; Q9FCC9; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0009368; C:endopeptidase Clp complex; IBA:GO_Central.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
DR   GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
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   PANTHER; PTHR10381; PTHR10381; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   SUPFAM; SSF52096; SSF52096; 1.
PE   3: Inferred from homology;
KW   Reference proteome.
FT   CHAIN           1..211
FT                   /note="Putative ATP-dependent Clp protease proteolytic
FT                   subunit-like"
FT                   /id="PRO_0000179668"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ   SEQUENCE   211 AA;  22667 MW;  03F4C0C914053F21 CRC64;
     MTRPSARHVL PEFTERTSAG TRTSDPYSKL LQERIVFLGT PVDETSANDV TAQLMYLEHQ
     APDRDIELYV NSPGGSFTAM TAIYDTMRYV ACDVATTCLG QAGPSAAVLL AAGTPGKRAA
     LPGARVVLHQ PALTEPVRGQ AGDLAVHAAE LVRVRARLEE ILVRHTGRTP GQVAADLERD
     TVLDARQARE YGLVDRIVPG RRTPPASSGA R