(data stored in SCRATCH zone)

HOGENOM: ACIF5_1_PE1011

ID   ACIF5_1_PE1011                       STANDARD;      PRT;   214 AA.
AC   ACIF5_1_PE1011; B5EQ28;
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; EC=3.4.21
DE   92;AltName: Full=Endopeptidase Clp; (ACIF5_1.PE1011).
GN   Name=clpP; OrderedLocusNames=Lferr_1031;
OS   ACIDITHIOBACILLUS FERROOXIDANS ATCC 53993.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=380394;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIF5_1.PE1011.
CC       Acidithiobacillus ferrooxidans ATCC 53993 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:B5EQ28_ACIF5
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; B5EQ28; -.
DR   EMBL; CP001132; ACH83273.1; -; Genomic_DNA.
DR   RefSeq; YP_002219480.1; NC_011206.1.
DR   STRING; B5EQ28; -.
DR   MEROPS; S14.001; -.
DR   GeneID; 6877000; -.
DR   GenomeReviews; CP001132_GR; Lferr_1031.
DR   KEGG; afe:Lferr_1031; -.
DR   OMA; ELMAKHT; -.
DR   ProtClustDB; CLSK2407753; -.
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; ACIF5_1.PE1011; -.
KW   ATP-binding; Complete proteome; Cytoplasm; Hydrolase;
KW   Nucleotide-binding; Protease; Serine protease.
SQ   SEQUENCE   214 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MWKQTGDQMA PAVQGLGYVP MVVEQTGRGE RSYDIYSRLL KERVVFLVGQ VEDMMANLVV
     AQLLFLEAEN PDKDIALYIN SPGGSVTAGM AIYDTMQFVR PKISTVCIGQ AASMGAVLLA
     AGAEGKRYAL PNARIMLHQP SGGFQGQAHD IEIHTKEILR IRERLNDILV HHTGQGRERI
     EQDLDRDFFM SAEEAQTYHL VDAVISHRGE NETA
//

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