ID   CLPP_AZOBR     STANDARD;      PRT;   210 AA.
AC   Q9X6W8;
DT   30-MAY-2000 (Rel. 39, Created)
DT   30-MAY-2000 (Rel. 39, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92)
DE   (Endopeptidase Clp).
GN   Name=clpP;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SpF94;
RA   Indorato C., Giannelli L., Bazzicalupo M.;
RT   "Azospirillum brasilense tig-clp-clpx-lon.";
RL   Submitted (MAY-1999) 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: Cytoplasmic (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase S14 family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; AF150957; AAD37435.1; -.
DR   HSSP; P19245; 1TYF.
DR   HAMAP; MF_00444; -; 1.
DR   InterPro; IPR001907; Pept_S14_ClpP.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   TIGRFAMs; TIGR00493; clpP; 1.
DR   PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR   PROSITE; PS00381; CLP_PROTEASE_SER; 1.
KW   Hydrolase; Serine protease.
FT   ACT_SITE    106    106       By similarity.
FT   ACT_SITE    131    131       By similarity.
SQ   SEQUENCE   210 AA;  22902 MW;  E0061EDA4BE52F3E CRC64;
     MYDFEPKMNA LVPMVIEQTN RGERGYDIYS RLLKERIIFL IGGVNDAVAS LICSQLLFLE
     SENPSKDIAL YINSPGGYVS AGLAIYDTMQ YIRPQVSTVC MGQAASMGSL LLAAGAPGKR
     FSLPNSRIMI HQPSGGAQGQ ASDIEIQAQE ILKLRSRLND IYVKHTGQSL DTIEAXMERD
     KFMSPEEAKA FGLIDEVVEK RPGSIGDGAA
//