ID   ELAD_ECO24              Reviewed;         406 AA.
AC   A7ZP88;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 58.
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=EcE24377A_2566;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABV20865.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000800; ABV20865.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001307307.1; NC_009801.1.
DR   AlphaFoldDB; A7ZP88; -.
DR   SMR; A7ZP88; -.
DR   MEROPS; C79.001; -.
DR   EnsemblBacteria; ABV20865; ABV20865; EcE24377A_2566.
DR   KEGG; ecw:EcE24377A_2566; -.
DR   HOGENOM; CLU_069513_0_0_6; -.
DR   Proteomes; UP000001122; 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; Thiol protease.
FT   CHAIN           1..406
FT                   /note="Protease ElaD"
FT                   /id="PRO_0000323568"
FT   ACT_SITE        234
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        316
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   406 AA;  46290 MW;  59722F6E8206E1E5 CRC64;
     MMVTVVSNYC QLSQKQLSQT FAEKFTVTEE LLQSLKKTAL SGDEESIELL HNIALGYDKF
     GKEAEDILYH IVRNPTNETL SIIRLIKNAC LKLYNLAHTA TNFPLKPTGP DNSDVLLFKK
     LFSPSKLMTI IGDEIPLISE KQSLSKVLLN DENNELSDGT NFWDKNRQLT TDEIDCYLQK
     IAANAKNTEV NYPTGLYVPY STRTHLEDAL NENIKSDPSW PKAVQLFPIN TGGHWILVSL
     QKIVNEKNNT QQIKCVIFNS LRALGHDKEN SLKRVINSFN SEFMGEMSNN NIKVHLTEPE
     IIFLHADLQQ YLSQSCGAFV CMAAQEVIEQ RESNSDSAPY TLLKNYADRF KKYSAEEQYE
     IDFQHRLVNR NCYLDKYGDA RINASYTQLE IKHSQPKNRA SGKRVS