ID   SSEL_SALPA              Reviewed;         340 AA.
AC   Q5PI48;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 68.
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=SPA0576;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAV76578.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000026; AAV76578.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001017746.1; NC_006511.1.
DR   AlphaFoldDB; Q5PI48; -.
DR   SMR; Q5PI48; -.
DR   EnsemblBacteria; AAV76578; AAV76578; SPA0576.
DR   KEGG; spt:SPA0576; -.
DR   HOGENOM; CLU_069513_0_0_6; -.
DR   Proteomes; UP000008185; 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_0000323572"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        285
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   340 AA;  38206 MW;  513037167B14B7D9 CRC64;
     MNICVNSLYR LSTPQFHSLY SEEVSDETLA LLIGEVENGN QNCIDLLCNL ALRNDNLGHK
     VEKLLFDLFS GKRSGSPDID KKINQACLVL HQIANNDITK NNTEWKKLHA PSRLLYMAGS
     ATTDLSKKIE IAHKIMGDQF AQTDQEQVGV ENLWCGARML SSDELAAATQ GLAQESPLLS
     VNYPIGLIHP TTKENILSTQ LLEKIAQSGL SHNEVFLVNT GDHWLLCLFY KLAEKIKCLI
     FNTYYDLNEN TKQEIIEAAK IAGISENEDI DFIETNLQNN VPNGCGLFCY HTIQLLSNAG
     QNDPATTLRE FAENFLTLSV EEQTLFNTQT RRQIYEYSLQ