(data stored in ACNUC7421 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   16-JAN-2019, entry version 26.
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.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73251.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73251.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73251.1,
RC   ECO:0000313|Proteomes:UP000002034};
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.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., 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
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, ECO:0000256|PROSITE-
CC         ProRule:PRU10086, ECO:0000256|RuleBase:RU000549,
CC         ECO:0000256|SAAS:SAAS01119754};
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       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   Proteomes; UP000002034; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00444};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00444,
KW   ECO:0000256|RuleBase:RU000549, ECO:0000256|SAAS:SAAS00674918,
KW   ECO:0000313|EMBL:ADP73251.1};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00444,
KW   ECO:0000256|RuleBase:RU000549, ECO:0000256|SAAS:SAAS00674844,
KW   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     98       {ECO:0000256|PROSITE-ProRule:PRU10085}.
FT   ACT_SITE     98     98       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00444}.
FT   ACT_SITE    123    123       {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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