ID   CLPP2_BACLD             Reviewed;         190 AA.
AC   Q65E10; Q62PI1;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   16-JUN-2009, entry version 31.
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=BLi03890, BL05355;
OS   Bacillus licheniformis (strain DSM 13 / ATCC 14580).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H.,
RA   Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R.,
RA   Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an
RT   organism with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G.,
RA   Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L.,
RA   Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N.,
RA   Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004).
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; AE017333; AAU42704.1; -; Genomic_DNA.
DR   EMBL; CP000002; AAU25330.1; -; Genomic_DNA.
DR   RefSeq; YP_080968.1; -.
DR   RefSeq; YP_093397.1; -.
DR   MEROPS; S14.001; -.
DR   GeneID; 3028091; -.
DR   GeneID; 3101125; -.
DR   GenomeReviews; AE017333_GR; BLi03890.
DR   GenomeReviews; CP000002_GR; BL05355.
DR   KEGG; bld:BLi03890; -.
DR   KEGG; bli:BL05355; -.
DR   NMPDR; fig|279010.5.peg.4133; -.
DR   HOGENOM; Q65E10; -.
DR   OMA; Q65E10; DMEISAK.
DR   BioCyc; BLIC279010:BL05355-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; FALSE_NEG.
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    190       ATP-dependent Clp protease proteolytic
FT                                subunit 2.
FT                                /FTId=PRO_0000179498.
FT   ACT_SITE     98     98       By similarity.
FT   ACT_SITE    123    123       By similarity.
SQ   SEQUENCE   190 AA;  21049 MW;  D5325BCB7C954FFC CRC64;
     MNTIPYVIEK TAAGERSYDI FSRLLKDRII MIGSEFNDDL ANRVTAQLLF LSAEDNEKDI
     SIYINSPGGS TSAGYAILDT MDYVKPDVRT ICVGMAASMG AILLAGGAKG KRYALKNSEI
     MIHQPLGGVK GQATDMEISA KRIIKLREKI ERFFHERTGQ PIEKLKADME RDYFMDADEA
     KAYGVIDAVL
//