ID   ELAD_ECOLI              Reviewed;         403 AA.
AC   Q47013; P76480; Q2MAM9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 3.
DT   03-AUG-2022, entry version 119.
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=b2269, JW5840;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Huisman G.W.;
RT   "Characterization of the ela locus from Escherichia coli.";
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION AS A DEUBIQUITINASE, SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF
RP   CYS-313.
RX   PubMed=17440617; DOI=10.1371/journal.pone.0000381;
RA   Catic A., Misaghi S., Korbel G.A., Ploegh H.L.;
RT   "ElaD, a deubiquitinating protease expressed by E. coli.";
RL   PLoS ONE 2:E381-E381(2007).
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.
CC       {ECO:0000269|PubMed:17440617}.
CC   -!- SIMILARITY: Belongs to the peptidase C79 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB02733.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U58768; AAB02733.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC75329.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76677.1; -; Genomic_DNA.
DR   PIR; C64998; C64998.
DR   RefSeq; NP_416772.1; NC_000913.3.
DR   RefSeq; WP_001393504.1; NZ_LN832404.1.
DR   AlphaFoldDB; Q47013; -.
DR   SMR; Q47013; -.
DR   BioGRID; 4261774; 39.
DR   STRING; 511145.b2269; -.
DR   MEROPS; C79.001; -.
DR   PaxDb; Q47013; -.
DR   PRIDE; Q47013; -.
DR   EnsemblBacteria; AAC75329; AAC75329; b2269.
DR   EnsemblBacteria; BAE76677; BAE76677; BAE76677.
DR   GeneID; 946742; -.
DR   KEGG; ecj:JW5840; -.
DR   KEGG; eco:b2269; -.
DR   PATRIC; fig|511145.12.peg.2362; -.
DR   EchoBASE; EB4009; -.
DR   eggNOG; COG5160; Bacteria.
DR   HOGENOM; CLU_069513_0_0_6; -.
DR   OMA; YRLSTPQ; -.
DR   PhylomeDB; Q47013; -.
DR   BioCyc; EcoCyc:G7176-MON; -.
DR   BioCyc; MetaCyc:G7176-MON; -.
DR   PRO; PR:Q47013; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IMP:EcoCyc.
DR   GO; GO:0016579; P:protein deubiquitination; IDA:EcoCyc.
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   1: Evidence at protein level;
KW   Hydrolase; Protease; Reference proteome; Thiol protease.
FT   CHAIN           1..403
FT                   /note="Protease ElaD"
FT                   /id="PRO_0000086950"
FT   ACT_SITE        231
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        313
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         313
FT                   /note="C->S: Abolishes deubiquitinating activity."
FT                   /evidence="ECO:0000269|PubMed:17440617"
FT   CONFLICT        16
FT                   /note="Q -> QQ (in Ref. 1; AAB02733)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   403 AA;  46078 MW;  775AFB6D5AE37DC0 CRC64;
     MMVTVVSNYC QLSQTQLSQT FAEKFTVTEE LLQSLKKTAL SGDEESIELL HNIALGYDKF
     GKEAEDILYH IVRTPTNETL SIIRLIKNAC LKLYNLAHIA TNSPLKSHDS DDLLFKKLFS
     PSKLMTIIGD EIPLISEKQS LSKVLLNDEN NELSDGTNFW DKNRQLTTDE IACYLQKIAA
     NAKNTQVNYP TGLYVPYSTR THLEDALNEN IKSDPSWPNE VQLFPINTGG HWILVSLQKI
     VNKKNNKLQI KCVIFNSLRA LGYDKENSLK RVINSFNSEL MGEMSNNNIK VHLNEPEIIF
     LHADLQQYLS QSCGAFVCMA AQEVIEQRES NSDSAPYTLL KNHADRFKKY SAEEQYEIDF
     QHRLANRNCY LDKYGDANIN HYYRNLEIKH SQPKNRASGK RVS