ID   CLPP1_CORGL             Reviewed;         208 AA.
AC   Q8NN02;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 40.
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=Cgl2411, cg2644;
OS   Corynebacterium glutamicum (Brevibacterium flavum).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1718;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RA   Nakagawa S.;
RT   "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX   MEDLINE=22830012; PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
RA   Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
RA   Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
RA   McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
RA   Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
RA   Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence
RT   and its impact on the production of L-aspartate-derived amino acids
RT   and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
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; BA000036; BAB99804.1; -; Genomic_DNA.
DR   EMBL; BX927155; CAF21075.1; -; Genomic_DNA.
DR   RefSeq; NP_601611.1; -.
DR   RefSeq; YP_226655.1; -.
DR   HSSP; P19245; 1TYF.
DR   MEROPS; S14.009; -.
DR   World-2DPAGE; 0001:Q8NN02; -.
DR   PRIDE; Q8NN02; -.
DR   GeneID; 1020360; -.
DR   GeneID; 3345289; -.
DR   GenomeReviews; BA000036_GR; Cgl2411.
DR   GenomeReviews; BX927147_GR; cg2644.
DR   KEGG; cgb:cg2644; -.
DR   KEGG; cgl:NCgl2327; -.
DR   HOGENOM; Q8NN02; -.
DR   OMA; Q8NN02; ANEILRM.
DR   BioCyc; CGLU196627-1:CG2644-MON; -.
DR   BRENDA; 3.4.21.92; 812.
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   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; Hydrolase;
KW   Nucleotide-binding; Protease; Serine protease.
FT   CHAIN         1    208       ATP-dependent Clp protease proteolytic
FT                                subunit 1.
FT                                /FTId=PRO_0000179545.
FT   ACT_SITE    108    108       By similarity.
FT   ACT_SITE    133    133       By similarity.
SQ   SEQUENCE   208 AA;  23037 MW;  4972B7CBF0344AA7 CRC64;
     MSNGFQMPTS RYVLPSFIEQ SAYGTKETNP YAKLFEERII FLGTQVDDTS ANDIMAQLLV
     LEGMDPDRDI TLYINSPGGS FTALMAIYDT MQYVRPDVQT VCLGQAASAA AVLLAAGAPG
     KRAVLPNSRV LIHQPATQGT QGQVSDLEIQ AAEIERMRRL METTLAEHTG KTAEQIRIDT
     DRDKILTAEE ALEYGIVDQV FDYRKLKR
//