(data stored in ACNUC7421 zone)

HOGENOM: IDLOI1_1_PE1001

ID   IDLOI1_1_PE1001                      STANDARD;      PRT;   206 AA.
AC   IDLOI1_1_PE1001; Q5QXN8;
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; (IDLOI1_1.PE1001).
GN   Name=clpP; OrderedLocusNames=IL1005;
OS   IDIOMARINA LOIHIENSIS L2TR.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS IDLOI1_1.PE1001.
CC       Idiomarina loihiensis L2TR chromosome, complete genome.
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:CLPP_IDILO
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; Q5QXN8; -.
DR   EMBL; AE017340; AAV81845.1; -; Genomic_DNA.
DR   RefSeq; YP_155394.1; NC_006512.1.
DR   ProteinModelPortal; Q5QXN8; -.
DR   SMR; Q5QXN8; 12-202.
DR   MEROPS; S14.001; -.
DR   GeneID; 3173950; -.
DR   GenomeReviews; AE017340_GR; IL1005.
DR   KEGG; ilo:IL1005; -.
DR   NMPDR; fig|283942.3.peg.1053; -.
DR   OMA; MEAQDFG; -.
DR   ProtClustDB; PRK00277; -.
DR   BioCyc; ILOI283942:IL1005-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:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IDLOI1_1.PE1001; -.
KW   ATP-dependent Clp protease proteolytic subunit;
KW   ATP-binding; Complete proteome; Cytoplasm; Hydrolase;
KW   Nucleotide-binding; Protease; Serine protease.
SQ   SEQUENCE   206 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSSDIQDPMA QLVPMVVEQT SKGERSYDIY SRLLKERVIF CCGQVEDHMA NLIVAQLLFL
     ESDNPDKDIY LYINSPGGVV TAGMAIYDTM RFIKPDVSTV CMGQAASMGA FLLAGGAQGK
     RYCLPNSRVM IHQPLGGFQG QASDFEIHAK QILDLKERLN RMLAENTGQD YEKVARDTDR
     DHFLSAEESI DYGLVDGILR QRGEES
//

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