(data stored in SCRATCH zone)

SWISSPROT: A5GRJ0_SYNR3

ID   A5GRJ0_SYNR3            Unreviewed;       224 AA.
AC   A5GRJ0;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|RuleBase:RU003567};
DE            EC=3.4.21.92 {ECO:0000256|HAMAP-Rule:MF_00444};
DE   AltName: Full=Endopeptidase Clp {ECO:0000256|HAMAP-Rule:MF_00444};
GN   Name=clpP {ECO:0000256|HAMAP-Rule:MF_00444,
GN   ECO:0000313|EMBL:CAK27499.1};
GN   OrderedLocusNames=SynRCC307_0596 {ECO:0000313|EMBL:CAK27499.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27499.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK27499.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) 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.
CC       {ECO:0000256|HAMAP-Rule:MF_00444}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins to small peptides in the presence
CC         of ATP and magnesium. Alpha-casein is the usual test substrate.
CC         In the absence of ATP, only oligopeptides shorter than five
CC         residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and
CC         Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and
CC         -Tyr-|-Trp bonds also occurs).; EC=3.4.21.92;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00444};
CC   -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings
CC       which stack back to back to give a disk-like structure with a
CC       central cavity, resembling the structure of eukaryotic
CC       proteasomes. {ECO:0000256|HAMAP-Rule:MF_00444}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00444}.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|RuleBase:RU003567}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00444}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CT978603; CAK27499.1; -; Genomic_DNA.
DR   RefSeq; WP_011935014.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0596; -.
DR   MEROPS; S14.001; -.
DR   EnsemblBacteria; CAK27499; CAK27499; SynRCC307_0596.
DR   KEGG; syr:SynRCC307_0596; -.
DR   eggNOG; ENOG41084IE; Bacteria.
DR   eggNOG; COG0740; LUCA.
DR   HOGENOM; HOG000285833; -.
DR   KO; K01358; -.
DR   OMA; IKPPIHT; -.
DR   OrthoDB; 1728970at2; -.
DR   BioCyc; SSP316278:G1GJL-582-MONOMER; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd07017; S14_ClpP_2; 1.
DR   HAMAP; MF_00444; ClpP; 1.
DR   InterPro; IPR001907; ClpP.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR023562; ClpP/TepA.
DR   PANTHER; PTHR10381; PTHR10381; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   SUPFAM; SSF52096; SSF52096; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GRJ0.
DR   SWISS-2DPAGE; A5GRJ0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00444};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00444,
KW   ECO:0000313|EMBL:CAK27499.1};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00444,
KW   ECO:0000313|EMBL:CAK27499.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Serine protease {ECO:0000256|HAMAP-Rule:MF_00444}.
FT   ACT_SITE    147    147       {ECO:0000256|HAMAP-Rule:MF_00444}.
SQ   SEQUENCE   224 AA;  24529 MW;  549861C2FC6B8107 CRC64;
     MDIRSVSAPY GDSGGASFRT PPPDLPSLLL KERIVYLGLP LFSDDDAKRQ MGVDVTELII
     AQLLYLEFDN PDKPIFFYIN STGTSWYSGD AIGFETEAFA ICDTIRYVKP PVHTICIGQA
     MGTAAMILSA GAKGQRASLP NASIVLHQPR SGARGQATDI QIRAQEVLHN KRTMLSMLSE
     NTGRTVEQLT ADSDRMTYLT PDQAMDYGLI DRVLSSRKEL PVAV
//

If you have problems or comments...

PBIL Back to PBIL home page