ID   CLPP2_ANAVT             Reviewed;         197 AA.
AC   Q3MDK7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit 2;
DE            EC=3.4.21.92;
DE   AltName: Full=Endopeptidase Clp 2;
GN   Name=clpP2; OrderedLocusNames=Ava_1305;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000117; ABA20929.1; -; Genomic_DNA.
DR   RefSeq; YP_321824.1; -.
DR   MEROPS; S14.001; -.
DR   GeneID; 3683048; -.
DR   GenomeReviews; CP000117_GR; Ava_1305.
DR   KEGG; ava:Ava_1305; -.
DR   NMPDR; fig|240292.3.peg.2150; -.
DR   HOGENOM; Q3MDK7; -.
DR   OMA; Q3MDK7; DGVANSL.
DR   BioCyc; AVAR240292:AVA_1305-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    197       ATP-dependent Clp protease proteolytic
FT                                subunit 2.
FT                                /FTId=PRO_0000236380.
FT   ACT_SITE    101    101       By similarity.
FT   ACT_SITE    126    126       By similarity.
SQ   SEQUENCE   197 AA;  22205 MW;  42DE88ED2880B853 CRC64;
     MPIGVPKVPY RMPGGQFTDW ISIYDRLYRE RIIFLGRDVD DEIANQIIAV MLYLDSEDPG
     KDIYLYINSP GGMVTSGLAI YDTMQHIKSD VVTICVGLAA SMGSFLLAAG TKGKRLALPH
     SRIMIHQPSG GTRGQATDIE IEAREILRIR HQLNQIYANN TNQPLAKIEK DMDRDFFMSA
     QEAKEYGLID RVIEERI
//