(data stored in ACNUC10821 zone)

SWISSPROT: C8U2C4_ECO10

ID   C8U2C4_ECO10            Unreviewed;       207 AA.
AC   C8U2C4;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, 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, 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   ECO:0000313|EMBL:BAI29282.1};
GN   OrderedLocusNames=ECO103_0414 {ECO:0000313|EMBL:BAI29282.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29282.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29282.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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. Component of the ClpAP and ClpXP complexes.
CC       {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; AP010958; BAI29282.1; -; Genomic_DNA.
DR   RefSeq; WP_000122253.1; NC_013353.1.
DR   SMR; C8U2C4; -.
DR   EnsemblBacteria; BAI29282; BAI29282; ECO103_0414.
DR   KEGG; eoh:ECO103_0414; -.
DR   HOGENOM; HOG000285833; -.
DR   KO; K01358; -.
DR   OMA; ERDHFMT; -.
DR   BioCyc; ECOL585395:ECO103_RS02170-MONOMER; -.
DR   Proteomes; UP000000959; 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; C8U2C4.
DR   SWISS-2DPAGE; C8U2C4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
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   Protease {ECO:0000256|HAMAP-Rule:MF_00444,
KW   ECO:0000256|RuleBase:RU000549, ECO:0000256|SAAS:SAAS00674844,
KW   ECO:0000313|EMBL:BAI29282.1};
KW   Serine protease {ECO:0000256|HAMAP-Rule:MF_00444,
KW   ECO:0000256|RuleBase:RU000549, ECO:0000256|SAAS:SAAS00674861}.
FT   ACT_SITE    111    111       {ECO:0000256|PROSITE-ProRule:PRU10085}.
FT   ACT_SITE    111    111       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00444}.
FT   ACT_SITE    136    136       {ECO:0000256|HAMAP-Rule:MF_00444,
FT                                ECO:0000256|PROSITE-ProRule:PRU10086}.
SQ   SEQUENCE   207 AA;  23187 MW;  A7843D036C8CB3C2 CRC64;
     MSYSGERDNF APHMALVPMV IEQTSRGERS FDIYSRLLKE RVIFLTGQVE DHMANLIVAQ
     MLFLEAENPE KDIYLYINSP GGVITAGMSI YDTMQFIKPD VSTICMGQAA SMGAFLLTAG
     AKGKRFCLPN SRVMIHQPLG GYQGQATDIE IHAREILKVK GRMNELMALH TGQSLEQIER
     DTERDRFLSA PEAVEYGLVD SILTHRN
//

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