(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIK0_GEOS0

ID   A0A0F6BIK0_GEOS0        Unreviewed;       196 AA.
AC   A0A0F6BIK0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 30.
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, ECO:0000256|RuleBase:RU000549};
DE   AltName: Full=Endopeptidase Clp {ECO:0000256|HAMAP-Rule:MF_00444};
GN   Name=clpP {ECO:0000256|HAMAP-Rule:MF_00444};
GN   OrderedLocusNames=GY4MC1_0410 {ECO:0000313|EMBL:ADP73251.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73251.1};
RN   [1] {ECO:0000313|EMBL:ADP73251.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73251.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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, ECO:0000256|RuleBase:RU000550,
CC       ECO:0000256|SAAS:SAAS00674840}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins to small peptides in the presence of
CC         ATP and magnesium. Alpha-casein is the usual test substrate. In the
CC         absence of ATP, only oligopeptides shorter than five residues are
CC         hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-
CC         Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also
CC         occurs).; EC=3.4.21.92; Evidence={ECO:0000256|HAMAP-Rule:MF_00444,
CC         ECO:0000256|PROSITE-ProRule:PRU10086, ECO:0000256|RuleBase:RU000549,
CC         ECO:0000256|SAAS:SAAS01119754};
CC   -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings which
CC       stack back to back to give a disk-like structure with a central cavity,
CC       resembling the structure of eukaryotic proteasomes. {ECO:0000256|HAMAP-
CC       Rule:MF_00444}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00444}.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000256|HAMAP-
CC       Rule:MF_00444, ECO:0000256|RuleBase:RU003567,
CC       ECO:0000256|SAAS:SAAS00674837}.
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DR   EMBL; CP002293; ADP73251.1; -; Genomic_DNA.
DR   RefSeq; WP_003248099.1; NC_014650.1.
DR   EnsemblBacteria; ADP73251; ADP73251; GY4MC1_0410.
DR   GeneID; 29236932; -.
DR   KEGG; gmc:GY4MC1_0410; -.
DR   KO; K01358; -.
DR   OMA; GIFDTMQ; -.
DR   OrthoDB; 1728970at2; -.
DR   BioCyc; GSP581103:G1GOQ-455-MONOMER; -.
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   InterPro; IPR033135; ClpP_His_AS.
DR   InterPro; IPR018215; ClpP_Ser_AS.
DR   PANTHER; PTHR10381; PTHR10381; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR00493; clpP; 1.
DR   PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR   PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BIK0.
DR   SWISS-2DPAGE; A0A0F6BIK0.
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00444};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|RuleBase:RU000549,
KW   ECO:0000256|SAAS:SAAS00674918, ECO:0000313|EMBL:ADP73251.1};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|RuleBase:RU000549,
KW   ECO:0000256|SAAS:SAAS00674844, ECO:0000313|EMBL:ADP73251.1};
KW   Serine protease {ECO:0000256|HAMAP-Rule:MF_00444,
KW   ECO:0000256|RuleBase:RU000549, ECO:0000256|SAAS:SAAS00674861}.
FT   ACT_SITE        98
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10085"
FT   ACT_SITE        98
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00444"
FT   ACT_SITE        123
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00444,
FT                   ECO:0000256|PROSITE-ProRule:PRU10086"
SQ   SEQUENCE   196 AA;  21541 MW;  9F938D853173FA83 CRC64;
     MNLIPTVIEQ TSRGERAYDI YSRLLKDRII ILGSPIDDQV ANSIVSQLLF LAAEDPEKDI
     SLYINSPGGS ITAGLAIYDT MQFIKPDVST ICIGMAASMG AFLLAAGAKG KRFALPNSEI
     MIHQPLGGAQ GQATEIEIAA KRILFLRDKL NRILSENTGQ PIDVIERDTD RDNFMTAQKA
     QEYGIIDRVL TRVDEK
//

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