ID   CLPP4_STRCO             Reviewed;         200 AA.
AC   Q9X7S0;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Putative ATP-dependent Clp protease proteolytic subunit-like;
DE   AltName: Full=Endopeptidase Clp-like;
GN   Name=clpP4; OrderedLocusNames=SCO7280; ORFNames=SC5H1.12;
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 (His) proposed to be
CC       part of the active site. Therefore it could be inactive.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000305}.
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DR   EMBL; AL939131; CAB42937.1; -; Genomic_DNA.
DR   PIR; T35328; T35328.
DR   RefSeq; NP_631336.1; NC_003888.3.
DR   RefSeq; WP_003971863.1; NZ_VNID01000019.1.
DR   AlphaFoldDB; Q9X7S0; -.
DR   SMR; Q9X7S0; -.
DR   STRING; 100226.SCO7280; -.
DR   MEROPS; S14.009; -.
DR   GeneID; 1102718; -.
DR   KEGG; sco:SCO7280; -.
DR   PATRIC; fig|100226.15.peg.7382; -.
DR   eggNOG; COG0740; Bacteria.
DR   HOGENOM; CLU_058707_3_2_11; -.
DR   InParanoid; Q9X7S0; -.
DR   OMA; TFCVGQA; -.
DR   PhylomeDB; Q9X7S0; -.
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..200
FT                   /note="Putative ATP-dependent Clp protease proteolytic
FT                   subunit-like"
FT                   /id="PRO_0000179667"
FT   ACT_SITE        100
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   200 AA;  21659 MW;  8A8798480CF9DF99 CRC64;
     MGSYTIPNVV ERTPQGERSY DVFSRLLSER IIFLGTEIDD GVANVVIAQL LHLESSAPES
     EIAVYINSPG GSFTSLMAIY DTMTFVQAPI STFCVGQAAS TAAVLLAGGD PGRRFVLEHA
     RVLLGQPASG GRQGTVSDLA LQAKEMVRIR SQVEEVLARH THHDVATLRA DMDRDKVFTA
     QEAVAYGLAD EVLARRLTRV