ID   SSEL_SALCH              Reviewed;         340 AA.
AC   Q57M66;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Deubiquitinase SseL;
DE            EC=3.4.22.-;
DE   AltName: Full=Deubiquitinating enzyme;
DE            Short=DUB;
DE   AltName: Full=Deubiquitinating protease;
DE   AltName: Full=Salmonella secreted effector L;
GN   Name=sseL; Synonyms=elaD; OrderedLocusNames=SCH_2290;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
CC   -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC       promote bacterial survival in host tissues. This protease targets the
CC       host cell ubiquitin pathway by acting as a deubiquitinase in infected
CC       host cells (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host cytoplasm
CC       {ECO:0000250}. Note=Secreted via type III secretion system 2 (SPI-2
CC       TTSS), and delivered into the host cytoplasm. In phagocytic cells
CC       localizes to the Salmonella-containing vacuole (SCV). In epithelial
CC       cells localizes to the Salmonella-containing vacuole (SCV) and to the
CC       Salmonella-induced filaments (Sifs), which are tubular membrane
CC       extensions from the SCV that are formed at late stages of infection (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C79 family. {ECO:0000305}.
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DR   EMBL; AE017220; AAX66196.1; -; Genomic_DNA.
DR   RefSeq; WP_011264333.1; NC_006905.1.
DR   AlphaFoldDB; Q57M66; -.
DR   SMR; Q57M66; -.
DR   EnsemblBacteria; AAX66196; AAX66196; SCH_2290.
DR   KEGG; sec:SCH_2290; -.
DR   HOGENOM; CLU_069513_0_0_6; -.
DR   OMA; YRLSTPQ; -.
DR   Proteomes; UP000000538; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Host cytoplasm; Hydrolase; Protease; Secreted; Thiol protease; Virulence.
FT   CHAIN           1..340
FT                   /note="Deubiquitinase SseL"
FT                   /id="PRO_0000323571"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        285
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   340 AA;  38265 MW;  68A93EEFF48488E6 CRC64;
     MNICVNSLYR LSTPQFHSLY SEDVSDEVLA LLIGEVENGN QNCIDLLCNL ALRNDDLGHK
     VEKLLFDLFS GKRSGSPDID KKINQACLVL HQIANNDITK NNTEWKKLHA PSRLLYMAGS
     ATTDLSKKIG IAHKIMGDQF AQTDQEQVGV ENLWCSARML SSDELAAATQ GLVQESPFLS
     VNYPIGLIHP TTKENILSTQ LLEKMAQSGL SENEVFLINT GDHWLICLFY KLAEKIKCLI
     FNTYYDLNEN TKQEIIEAAK IAGISESDEV NFIEMNLQNN VPNGCSLFCY HTIQLLSNAG
     QNDPVTTLRE FAEKFLTLSV EEQALFNTQT RRQIYEYSLQ