(data stored in SCRATCH zone)

SWISSPROT: B7UJR0_ECO27

ID   B7UJR0_ECO27            Unreviewed;       207 AA.
AC   B7UJR0;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-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:CAS07920.1};
GN   OrderedLocusNames=E2348C_0372 {ECO:0000313|EMBL:CAS07920.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07920.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07920.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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; FM180568; CAS07920.1; -; Genomic_DNA.
DR   RefSeq; WP_000122253.1; NC_011601.1.
DR   SMR; B7UJR0; -.
DR   EnsemblBacteria; CAS07920; CAS07920; E2348C_0372.
DR   KEGG; ecg:E2348C_0372; -.
DR   HOGENOM; HOG000285833; -.
DR   KO; K01358; -.
DR   OMA; ERDHFMT; -.
DR   BioCyc; ECOL574521:E2348C_RS01955-MONOMER; -.
DR   Proteomes; UP000008205; 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; B7UJR0.
DR   SWISS-2DPAGE; B7UJR0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
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:CAS07920.1};
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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