SSEL_SALTY
ID SSEL_SALTY Reviewed; 340 AA.
AC Q8ZNG2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 95.
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=STM2287;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP ROLE IN VIRULENCE, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=SL1344;
RX PubMed=17158898; DOI=10.1128/iai.00985-06;
RA Coombes B.K., Lowden M.J., Bishop J.L., Wickham M.E., Brown N.F., Duong N.,
RA Osborne S., Gal-Mor O., Finlay B.B.;
RT "SseL is a salmonella-specific translocated effector integrated into the
RT SsrB-controlled salmonella pathogenicity island 2 type III secretion
RT system.";
RL Infect. Immun. 75:574-580(2007).
RN [3]
RP FUNCTION AS A DEUBIQUITINASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, INDUCTION, AND MUTAGENESIS OF CYS-285.
RC STRAIN=ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=17360673; DOI=10.1073/pnas.0610095104;
RA Rytkoenen A., Poh J., Garmendia J., Boyle C., Thompson A., Liu M.,
RA Freemont P., Hinton J.C.D., Holden D.W.;
RT "SseL, a Salmonella deubiquitinase required for macrophage killing and
RT virulence.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:3502-3507(2007).
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. Specifically hydrolyzes mono- and polyubiquitin substrates
CC in vitro with a preference for 'Lys-63'-linked ubiquitin chains,
CC suggesting that it interferes with a signaling pathway rather than
CC inhibiting proteasomal-dependent degradation of its targets. Does not
CC possess desumoylating activity. Is required for the Salmonella-induced
CC delayed cytotoxicity in macrophages and full virulence. Is not required
CC for intracellular bacterial replication. {ECO:0000269|PubMed:17158898,
CC ECO:0000269|PubMed:17360673}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for ubiquitin-1-amido methyl coumarin (Ub-AMC)
CC {ECO:0000269|PubMed:17360673};
CC Note=The Vmax of the reaction with ubiquitin-1-amido methyl coumarin
CC (Ub-AMC) as substrate is 2354 pM/sec/uM enzyme.;
CC -!- INTERACTION:
CC Q8ZNG2; P22059: OSBP; Xeno; NbExp=4; IntAct=EBI-10690213, EBI-2681902;
CC -!- SUBCELLULAR LOCATION: Secreted. Host cytoplasm. Note=Secreted via type
CC III secretion system 2 (SPI-2 TTSS), and delivered into the host
CC cytoplasm. In phagocytic cells localizes to the Salmonella-containing
CC vacuole (SCV). In epithelial cells localizes to the Salmonella-
CC containing vacuole (SCV) and to the Salmonella-induced filaments
CC (Sifs), which are tubular membrane extensions from the SCV that are
CC formed at late stages of infection.
CC -!- INDUCTION: Expression of the gene is induced inside phagocytic cells
CC and is dependent on the SsrA/SsrB system. {ECO:0000269|PubMed:17158898,
CC ECO:0000269|PubMed:17360673}.
CC -!- SIMILARITY: Belongs to the peptidase C79 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL21188.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006468; AAL21188.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_461229.3; NC_003197.2.
DR PDB; 5HAF; X-ray; 2.70 A; A/B=24-340.
DR PDB; 5UBW; X-ray; 2.39 A; A/B=158-340.
DR PDBsum; 5HAF; -.
DR PDBsum; 5UBW; -.
DR AlphaFoldDB; Q8ZNG2; -.
DR SMR; Q8ZNG2; -.
DR DIP; DIP-60877N; -.
DR IntAct; Q8ZNG2; 1.
DR STRING; 99287.STM2287; -.
DR PaxDb; Q8ZNG2; -.
DR EnsemblBacteria; AAL21188; AAL21188; STM2287.
DR GeneID; 1253809; -.
DR KEGG; stm:STM2287; -.
DR PATRIC; fig|99287.12.peg.2421; -.
DR HOGENOM; CLU_069513_0_0_6; -.
DR OMA; YRLSTPQ; -.
DR PhylomeDB; Q8ZNG2; -.
DR PHI-base; PHI:2623; -.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Hydrolase; Protease; Reference proteome;
KW Secreted; Thiol protease; Virulence.
FT CHAIN 1..340
FT /note="Deubiquitinase SseL"
FT /id="PRO_0000323575"
FT ACT_SITE 223
FT /evidence="ECO:0000250"
FT ACT_SITE 285
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT MUTAGEN 285
FT /note="C->A: Abolishes deubiquitinating activity."
FT /evidence="ECO:0000269|PubMed:17360673"
FT HELIX 26..38
FT /evidence="ECO:0007829|PDB:5HAF"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:5HAF"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:5HAF"
FT HELIX 77..94
FT /evidence="ECO:0007829|PDB:5HAF"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:5HAF"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:5HAF"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:5HAF"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:5HAF"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:5HAF"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:5UBW"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:5HAF"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:5HAF"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:5UBW"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:5UBW"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:5UBW"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:5UBW"
FT STRAND 224..242
FT /evidence="ECO:0007829|PDB:5UBW"
FT HELIX 249..262
FT /evidence="ECO:0007829|PDB:5UBW"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:5HAF"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:5UBW"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:5UBW"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:5UBW"
FT HELIX 285..299
FT /evidence="ECO:0007829|PDB:5UBW"
FT HELIX 304..316
FT /evidence="ECO:0007829|PDB:5UBW"
FT HELIX 320..337
FT /evidence="ECO:0007829|PDB:5UBW"
SQ SEQUENCE 340 AA; 38221 MW; 612D4A8C18D19CF3 CRC64;
MNICVNSLYR LSIPQFHSLY TEEVSDEALT LLFSAVENGD QNCIDLLCNL ALRNDDLGHR
VEKFLFDLFS GKRTGSSDID KKINQACLVL HQIANNDITK DNTEWKKLHA PSRLLYMAGS
ATTDLSKKIG IAHKIMGDQF AQTDQEQVGV ENLWCGARML SSDELAAATQ GLVQESPLLS
VNYPIGLIHP TTKENILSTQ LLEKIAQSGL SHNEVFLVNT GDHWLLCLFY KLAEKIKCLI
FNTYYDLNEN TKQEIIEAAK IAGISESDEV NFIEMNLQNN VPNGCGLFCY HTIQLLSNAG
QNDPATTLRE FAENFLTLSV EEQALFNTQT RRQIYEYSLQ
