ID   SSEL_SALAR              Reviewed;         340 AA.
AC   A9MJD1;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
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; OrderedLocusNames=SARI_00605;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000880; ABX20531.1; -; Genomic_DNA.
DR   RefSeq; WP_001017748.1; NC_010067.1.
DR   AlphaFoldDB; A9MJD1; -.
DR   SMR; A9MJD1; -.
DR   STRING; 41514.SARI_00605; -.
DR   EnsemblBacteria; ABX20531; ABX20531; SARI_00605.
DR   KEGG; ses:SARI_00605; -.
DR   HOGENOM; CLU_069513_0_0_6; -.
DR   OMA; YRLSTPQ; -.
DR   OrthoDB; 447148at2; -.
DR   Proteomes; UP000002084; 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; Reference proteome; Secreted;
KW   Thiol protease; Virulence.
FT   CHAIN           1..340
FT                   /note="Deubiquitinase SseL"
FT                   /id="PRO_0000323570"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        284
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   340 AA;  38153 MW;  71C1D5ECA561D35B CRC64;
     MNICVNSLYR LSTPQFQNLY SEEVSDEGLA LLIREVENGD QNCIDLLCNL ALRNDDLGHK
     VEKILFDLFS GKKHGSPDID KKINQACLML YQTANNDIAK NNTDFKKLHI PSRLLYMAGS
     ATPDFSKKLE IAHKILGDQI AQTEEEQVGV ENLWCPARMV SSDELSRATQ GMTQGLSLSV
     NYPIGLIHPT TGENVLSAQL HEKVAQSGLS DNEVFLINTE SHWIFCLFYK IAEKIKCLIF
     NTHHDLNQNT KQEIRAAAKI AGASEEGDVN FIEIDLQNNV PNGCGLFCFQ ALQLLSATGQ
     NDPVAVLREY SENFLRLSVE EQTLFNTETR RKIHEYSLTS