(data stored in SCRATCH zone)

SWISSPROT: B7UIK8_ECO27

ID   B7UIK8_ECO27            Unreviewed;       474 AA.
AC   B7UIK8;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 59.
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:CAS07716.1};
GN   OrderedLocusNames=E2348C_0168 {ECO:0000313|EMBL:CAS07716.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07716.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07716.1, 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   -!- 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; FM180568; CAS07716.1; -; Genomic_DNA.
DR   RefSeq; WP_000753936.1; NC_011601.1.
DR   EnsemblBacteria; CAS07716; CAS07716; E2348C_0168.
DR   KEGG; ecg:E2348C_0168; -.
DR   HOGENOM; HOG000223642; -.
DR   KO; K04771; -.
DR   OMA; ASFITFK; -.
DR   BioCyc; ECOL574521:E2348C_RS00865-MONOMER; -.
DR   Proteomes; UP000008205; 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; B7UIK8.
DR   SWISS-2DPAGE; B7UIK8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Hydrolase {ECO:0000256|RuleBase:RU364067};
KW   Protease {ECO:0000256|RuleBase:RU364067, ECO:0000313|EMBL:CAS07716.1};
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_5010599213.
FT   DOMAIN      280    371       PDZ. {ECO:0000259|PROSITE:PS50106}.
FT   DOMAIN      377    466       PDZ. {ECO:0000259|PROSITE:PS50106}.
SQ   SEQUENCE   474 AA;  49339 MW;  7B147CE548CE4AE2 CRC64;
     MKKTTLALSA LALSLGLALS PLSATAAETS SATTAQQMPS LAPMLEKVMP SVVSINVEGS
     TTVNTPRMPR NFQQFFGDDS PFCQEGSPFQ SSPFCQGGLG GNGGGQQQKF MALGSGVIID
     ADKGYVVTNN HVVDNATVIK VQLSDGRKFD AKMVGKDPRS DIALIQIQNP KNLTAIKMAD
     SDALRVGDYT VAIGNPFGLG ETVTSGIVSA LGRSGLNAEN YENFIQTDAA INRGNSGGAL
     VNLNGELIGI NTAILAPDGG NIGIGFAIPS NMVKNLTSQM VEYGQVKRGE LGIMGTELNS
     DLAKAMKVDA QRGAFVSQVL PNSSAAKAGI KAGDVITSLN GKPISSFAAL RAQVGTMPVG
     SKLTLGLLRD GKQVNVNLEL QQSSQNQVDS STIFNGIEGA EMSNKGKDQG VVVNNVKTGT
     PAAQIGLKKG DVIIGANQQA VKNIAELRKV LDSKPSVLAL NIQRGDSTIY LLMQ
//

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