(data stored in ACNUC7421 zone)

HOGENOM: BURP8_1_PE1003

ID   BURP8_1_PE1003                       STANDARD;      PRT;   219 AA.
AC   BURP8_1_PE1003; B2JGL5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit 2; EC=3.4.21
DE   92;AltName: Full=Endopeptidase Clp 2; (BURP8_1.PE1003).
GN   Name=clpP2; OrderedLocusNames=Bphy_1011;
OS   BURKHOLDERIA PHYMATUM STM815.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=391038;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BURP8_1.PE1003.
CC       Burkholderia phymatum STM815 chromosome chromosome 1, complete sequence
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:B2JGL5_BURP8
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.
CC   -!- GENE_FAMILY: HOG000285833 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B2JGL5; -.
DR   EMBL; CP001043; ACC70200.1; -; Genomic_DNA.
DR   RefSeq; YP_001857246.1; NC_010622.1.
DR   ProteinModelPortal; B2JGL5; -.
DR   SMR; B2JGL5; 28-218.
DR   STRING; B2JGL5; -.
DR   MEROPS; S14.001; -.
DR   GeneID; 6242509; -.
DR   GenomeReviews; CP001043_GR; Bphy_1011.
DR   KEGG; bph:Bphy_1011; -.
DR   OMA; MEAQDFG; -.
DR   ProtClustDB; PRK00277; -.
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; ClpP; 1; -.
DR   InterPro; IPR023562; Pept_S14/S49.
DR   InterPro; IPR001907; Pept_S14_ClpP.
DR   InterPro; IPR018215; Pept_S14_ClpP_AS.
DR   PANTHER; PTHR10381; Pept_S14_ClpP; 1.
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.
DR   HOGENOMDNA; BURP8_1.PE1003; -.
KW   ATP-binding; Complete proteome; Cytoplasm; Hydrolase;
KW   Nucleotide-binding; Protease; Serine protease.
SQ   SEQUENCE   219 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTFRAQMLDT LTSQSSRDRD LEAQALGLVP IVVETSGRGE RSYDIYSRLL KERVVFLVGE
     VNDQTANLVI AQLLFLESEN PDKDISFYIN SPGGSVSAGM AIYDTMQFIK PDVSTLCMGL
     AASMGAFLLA AGAKGKRFAL PNARVMIHQP LGGARGQASD IEIQAREILY LKERLNQLLS
     HHTGQPVERI QRDTDRDNFM SGDDAQAYGL VDQVLHKRP
//

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