ID   CLPP1_THEFY             Reviewed;         222 AA.
AC   Q47MU3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit 1;
DE            EC=3.4.21.92;
DE   AltName: Full=Endopeptidase Clp 1;
GN   Name=clpP1; OrderedLocusNames=Tfu_2193;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptosporangineae; Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(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 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in
CC       the presence of ATP and magnesium. Alpha-casein is the usual test
CC       substrate. In the absence of ATP, only oligopeptides shorter than
CC       five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec;
CC       and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu-
CC       and -Tyr-|-Trp bonds also occurs).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase S14 family.
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DR   EMBL; CP000088; AAZ56226.1; -; Genomic_DNA.
DR   RefSeq; YP_290249.1; -.
DR   MEROPS; S14.009; -.
DR   GeneID; 3581409; -.
DR   GenomeReviews; CP000088_GR; Tfu_2193.
DR   KEGG; tfu:Tfu_2193; -.
DR   NMPDR; fig|269800.4.peg.1309; -.
DR   HOGENOM; Q47MU3; -.
DR   OMA; Q47MU3; ANEILRM.
DR   BioCyc; TFUS269800:TFU_2193-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:HAMAP.
DR   GO; GO:0006508; P:proteolysis; IEA:HAMAP.
DR   HAMAP; MF_00444; -; 1.
DR   InterPro; IPR001907; Pept_S14_ClpP.
DR   InterPro; IPR018215; Pept_S14_ClpP_CS.
DR   PANTHER; PTHR10381; Pept_S14_ClpP; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR   PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Hydrolase;
KW   Nucleotide-binding; Protease; Serine protease.
FT   CHAIN         1    222       ATP-dependent Clp protease proteolytic
FT                                subunit 1.
FT                                /FTId=PRO_0000226476.
FT   ACT_SITE    121    121       By similarity.
FT   ACT_SITE    146    146       By similarity.
SQ   SEQUENCE   222 AA;  24792 MW;  BFED6C1550C3EFC4 CRC64;
     MSEFNFDPYR RYGGGMAPMA PQSRYVLPSY IERTAYGVKE MNPYNKLFEE RIIFVGVQID
     DTSANDIIAQ MMTLEHIDSD RDITLYINSP GGSFTSLMAI YDTMQFVRPD IQTVCVGQAA
     SAAAVLLAGG TKGKRTALPN SRILIHQPAT EGTHGQASDV EIMANEIMRI RHQLETILAK
     HTGRSVEEIS RDIERDKILT AEEAKEYGIV DDVLPYRKAS LK
//