ELAD_ECO57
ID ELAD_ECO57 Reviewed; 407 AA.
AC Q8XCY9; Q7AC13;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Protease ElaD;
DE EC=3.4.22.-;
DE AltName: Full=Deubiquitinase;
DE AltName: Full=Deubiquitinating enzyme;
DE Short=DUB;
DE AltName: Full=Deubiquitinating protease;
GN Name=elaD; OrderedLocusNames=Z3529, ECs3157;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Protease that can act as an efficient and specific
CC deubiquitinating enzyme in vitro. Does not possess desumoylating and
CC deneddylating activities. The physiological substrate is unknown (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C79 family. {ECO:0000305}.
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DR EMBL; AE005174; AAG57402.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36580.1; -; Genomic_DNA.
DR PIR; E91023; E91023.
DR PIR; F85867; F85867.
DR RefSeq; NP_311184.1; NC_002695.1.
DR AlphaFoldDB; Q8XCY9; -.
DR SMR; Q8XCY9; -.
DR STRING; 155864.EDL933_3436; -.
DR MEROPS; C79.001; -.
DR EnsemblBacteria; AAG57402; AAG57402; Z3529.
DR EnsemblBacteria; BAB36580; BAB36580; ECs_3157.
DR GeneID; 916865; -.
DR KEGG; ece:Z3529; -.
DR KEGG; ecs:ECs_3157; -.
DR PATRIC; fig|386585.9.peg.3295; -.
DR eggNOG; COG5160; Bacteria.
DR HOGENOM; CLU_069513_0_0_6; -.
DR OMA; YRLSTPQ; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR Pfam; PF02902; Peptidase_C48; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 3: Inferred from homology;
KW Hydrolase; Protease; Reference proteome; Thiol protease.
FT CHAIN 1..407
FT /note="Protease ElaD"
FT /id="PRO_0000323569"
FT ACT_SITE 231
FT /evidence="ECO:0000250"
FT ACT_SITE 317
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 407 AA; 46648 MW; B8BCD1F6328A654C CRC64;
MMVTVVSNYC QLSQTQLSQT FAEKFTVTEE LLQSLKKTAL SGDEESIELL HNIALGYDEF
GKKAEDILYH IVRNPTNDTL SIIKLIKNAC LKLYNLAHTA TKHPLKSHDS DNLLFKKLFS
PSKLMAIIGE DIPLISEKQS LSKVLLNDKN NELSDGTNFW DKNRQLTTDE IACYLKKIAA
NAKNTQVNYP TDFYLPNSNS TYLEVALNDN IKSDPSWPKE VQLFPINTGG HWILVSLQKI
VNEKNNTQQI KCIIFNSLRA LGHEKENSLK RIINSFNSFN CDPTRETPNN KNITDHLTEP
EIIFLHADLQ QYLSQSCGAF VCMAAQEVIE QMESNSDSAP YTLLKNYADR FKKYSAEEQY
EIDFQHRLEN RNCYLDKYGD ANINHYYRNL EIKNSHPKNR ASSKRVS