(data stored in SCRATCH zone)

SWISSPROT: C8U1N1_ECO10

ID   C8U1N1_ECO10            Unreviewed;       474 AA.
AC   C8U1N1;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Periplasmic serine endoprotease DegP-like {ECO:0000256|RuleBase:RU364067};
DE            EC=3.4.21.107 {ECO:0000256|RuleBase:RU364067};
GN   Name=degP {ECO:0000313|EMBL:BAI29039.1};
GN   OrderedLocusNames=ECO103_0161 {ECO:0000313|EMBL:BAI29039.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29039.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29039.1, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Acts on substrates that are at least partially unfolded.
CC         The cleavage site P1 residue is normally between a pair of
CC         hydrophobic residues, such as Val-|-Val.; EC=3.4.21.107;
CC         Evidence={ECO:0000256|RuleBase:RU364067};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|RuleBase:RU364067}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|RuleBase:RU364067}.
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DR   EMBL; AP010958; BAI29039.1; -; Genomic_DNA.
DR   RefSeq; WP_000753945.1; NC_013353.1.
DR   EnsemblBacteria; BAI29039; BAI29039; ECO103_0161.
DR   KEGG; eoh:ECO103_0161; -.
DR   HOGENOM; HOG000223642; -.
DR   KO; K04771; -.
DR   OMA; ASFITFK; -.
DR   BioCyc; ECOL585395:ECO103_RS00825-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011782; Pept_S1C_Do.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   Pfam; PF00595; PDZ; 2.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; SSF50156; 2.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   TIGRFAMs; TIGR02037; degP_htrA_DO; 1.
DR   PROSITE; PS50106; PDZ; 2.
PE   3: Inferred from homology;
DR   PRODOM; C8U1N1.
DR   SWISS-2DPAGE; C8U1N1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Hydrolase {ECO:0000256|RuleBase:RU364067};
KW   Protease {ECO:0000256|RuleBase:RU364067, ECO:0000313|EMBL:BAI29039.1};
KW   Serine protease {ECO:0000256|RuleBase:RU364067};
KW   Signal {ECO:0000256|RuleBase:RU364067};
KW   Stress response {ECO:0000256|RuleBase:RU364067}.
FT   SIGNAL        1     26       {ECO:0000256|RuleBase:RU364067}.
FT   CHAIN        27    474       Periplasmic serine endoprotease DegP-
FT                                like. {ECO:0000256|RuleBase:RU364067}.
FT                                /FTId=PRO_5010603046.
FT   DOMAIN      280    371       PDZ. {ECO:0000259|PROSITE:PS50106}.
FT   DOMAIN      377    466       PDZ. {ECO:0000259|PROSITE:PS50106}.
SQ   SEQUENCE   474 AA;  49340 MW;  5482E596F74B694F CRC64;
     MKKTTLALSA LALSLGLALS PLSATAAETS SATTAQQMPS LAPMLEKVMP SVVSINVEGS
     TTVNTPRMPR NFQQFFGDDS PFCQEGSPFQ SSPFCQGGQG GNGGGQQQKF MALGSGVIID
     ADKGYVVTNN HVVDNATVIK VQLSDGRKFD AKMVGKDPRS DIALIQIQNP KNLTAIKMAD
     SDALRVGDYT VAIGNPFGLG ETVTSGIVSA LGRSGLNAEN YENFIQTDAA INRGNSGGAL
     VNLNGELIGI NTAILAPDGG NIGIGFAIPS NMVKNLTSQM VEYGQVKRGE LGIMGTELNS
     ELAKAMKVDA QRGAFVSQVL PNSSAAKAGI KAGDVITSLN GKPISSFAAL RAQVGTMPVG
     SKLTLGLLRD GKQVNVNLEL QQSSQNQVDS SSIFNGIEGA EMSNKGKDQG VVVNNVKTGT
     PAAQIGLKKG DVIIGANQQA VKNIAELRKV LDSKPSVLAL NIQRGDSSIY LLMQ
//

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