CLPP1_MYCLE
ID CLPP1_MYCLE Reviewed; 200 AA.
AC Q9CBY3;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit 1 {ECO:0000255|HAMAP-Rule:MF_00444};
DE EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE AltName: Full=Endopeptidase Clp 1 {ECO:0000255|HAMAP-Rule:MF_00444};
GN Name=clpP1 {ECO:0000255|HAMAP-Rule:MF_00444}; Synonyms=clpP;
GN OrderedLocusNames=ML1480;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC30430.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL583922; CAC30430.1; ALT_INIT; Genomic_DNA.
DR PIR; A87094; A87094.
DR AlphaFoldDB; Q9CBY3; -.
DR SMR; Q9CBY3; -.
DR STRING; 272631.ML1480; -.
DR MEROPS; S14.008; -.
DR EnsemblBacteria; CAC30430; CAC30430; CAC30430.
DR KEGG; mle:ML1480; -.
DR Leproma; ML1480; -.
DR eggNOG; COG0740; Bacteria.
DR HOGENOM; CLU_058707_3_2_11; -.
DR Proteomes; UP000000806; Chromosome.
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; IPR033135; ClpP_His_AS.
DR PANTHER; PTHR10381; PTHR10381; 1.
DR Pfam; PF00574; CLP_protease; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease.
FT CHAIN 1..200
FT /note="ATP-dependent Clp protease proteolytic subunit 1"
FT /id="PRO_0000179592"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 123
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ SEQUENCE 200 AA; 21847 MW; E1B0AE6C9AF83EE4 CRC64;
MGHVTDIRSN SQGFNLTDSV YERLLSERII FLGSEVNDNI ANRLCAQILL LAAEDAFKDI
SLYINSPGGS ISAGMAIYDT MVLAPCDIAT YAMGMAASMG EFLLAAGTRG KRYALPHARI
LMHQPLGGVT GSAADIAIQA EQFAVIKKEM FRLNAEFTGQ PIERIEADSD RDRWFTASEA
LEYGFVDHII TRAHVNGEVQ
