SSEJ_SALTY
ID SSEJ_SALTY Reviewed; 408 AA.
AC Q9FD10; Q7BIM8;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Secreted effector protein SseJ;
DE EC=3.-.-.-;
DE AltName: Full=Salmonella-translocated effector J;
DE Short=STE J;
GN Name=sseJ; OrderedLocusNames=STM1631;
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 [GENOMIC DNA], SUBCELLULAR LOCATION, AND SECRETION VIA
RP TYPE III SECRETION SYSTEM.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=10861017; DOI=10.1073/pnas.97.13.7539;
RA Miao E.A., Miller S.I.;
RT "A conserved amino acid sequence directing intracellular type III secretion
RT by Salmonella typhimurium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:7539-7544(2000).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION, AND SECRETION VIA TYPE III SECRETION SYSTEM.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=12496192; DOI=10.1128/iai.71.1.418-427.2003;
RA Freeman J.A., Ohl M.E., Miller S.I.;
RT "The Salmonella enterica serovar typhimurium translocated effectors SseJ
RT and SifB are targeted to the Salmonella-containing vacuole.";
RL Infect. Immun. 71:418-427(2003).
RN [4]
RP FUNCTION, DEACYLASE ACTIVITY, AND MUTAGENESIS OF SER-151; SER-153; ASP-247
RP AND HIS-384.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=16177296; DOI=10.1128/iai.73.10.6249-6259.2005;
RA Ohlson M.B., Fluhr K., Birmingham C.L., Brumell J.H., Miller S.I.;
RT "SseJ deacylase activity by Salmonella enterica serovar Typhimurium
RT promotes virulence in mice.";
RL Infect. Immun. 73:6249-6259(2005).
RN [5]
RP INTERACTION WITH RHOA AND SIFA.
RX PubMed=18996344; DOI=10.1016/j.chom.2008.08.012;
RA Ohlson M.B., Huang Z., Alto N.M., Blanc M.-P., Dixon J.E., Chai J.,
RA Miller S.I.;
RT "Structure and function of Salmonella SifA indicate that its interactions
RT with SKIP, SseJ, and RhoA family GTPases induce endosomal tubulation.";
RL Cell Host Microbe 4:434-446(2008).
RN [6]
RP FUNCTION, ESTERIFICATION ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18333886; DOI=10.1111/j.1365-2958.2008.06142.x;
RA Nawabi P., Catron D.M., Haldar K.;
RT "Esterification of cholesterol by a type III secretion effector during
RT intracellular Salmonella infection.";
RL Mol. Microbiol. 68:173-185(2008).
CC -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC promote bacterial survival in host tissues. This protein is required
CC for endosomal tubulation and negatively regulates the formation of
CC Salmonella-induced filaments (Sifs) in epithelial cells. Has both
CC deacylase and esterification activities in vitro, but esterification is
CC probably the dominant activity in host cells. Significantly contributes
CC to cholesterol esterification, which reduces cellular cholesterol in
CC cells and abrogates the ability of SifA to associate with cholesterol
CC and LAMP-1 vesicles. {ECO:0000269|PubMed:16177296,
CC ECO:0000269|PubMed:18333886}.
CC -!- SUBUNIT: Interacts with RhoA and indirectly with SifA.
CC {ECO:0000269|PubMed:18996344}.
CC -!- INTERACTION:
CC Q9FD10; P61586: RHOA; Xeno; NbExp=3; IntAct=EBI-10690199, EBI-446668;
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. Localizes to the Salmonella-containing vacuole (SCV) at
CC early time points following invasion and subsequently traffics away
CC from the SCV along Salmonella-induced filaments (Sifs) in epithelial
CC cells.
CC -!- DISRUPTION PHENOTYPE: Mutants have reduced cholesterol esterification
CC activity as well as reduced lipid droplets.
CC {ECO:0000269|PubMed:18333886}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF294582; AAG02230.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20549.1; -; Genomic_DNA.
DR RefSeq; NP_460590.1; NC_003197.2.
DR RefSeq; WP_001131430.1; NC_003197.2.
DR AlphaFoldDB; Q9FD10; -.
DR SMR; Q9FD10; -.
DR IntAct; Q9FD10; 2.
DR STRING; 99287.STM1631; -.
DR PaxDb; Q9FD10; -.
DR EnsemblBacteria; AAL20549; AAL20549; STM1631.
DR GeneID; 1253149; -.
DR KEGG; stm:STM1631; -.
DR PATRIC; fig|99287.12.peg.1723; -.
DR HOGENOM; CLU_674196_0_0_6; -.
DR OMA; CIFKLYH; -.
DR BioCyc; SENT99287:STM1631-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044174; C:host cell endosome; IMP:AgBase.
DR GO; GO:0033644; C:host cell membrane; IMP:AgBase.
DR GO; GO:0034736; F:cholesterol O-acyltransferase activity; IDA:AgBase.
DR GO; GO:0047178; F:glycerophospholipid acyltransferase (CoA-dependent) activity; IDA:AgBase.
DR GO; GO:0016298; F:lipase activity; IDA:AgBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:AgBase.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR010637; Sif.
DR Pfam; PF00657; Lipase_GDSL; 1.
DR Pfam; PF06767; Sif; 1.
PE 1: Evidence at protein level;
KW Host cytoplasm; Hydrolase; Reference proteome; Secreted; Virulence.
FT CHAIN 1..408
FT /note="Secreted effector protein SseJ"
FT /id="PRO_0000391492"
FT ACT_SITE 151
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 381
FT /evidence="ECO:0000250"
FT ACT_SITE 384
FT /evidence="ECO:0000305"
FT MUTAGEN 151
FT /note="S->A: 5-fold decrease in deacylase activity. Does
FT not affect translocation by TTSS and cellular
FT localization."
FT /evidence="ECO:0000269|PubMed:16177296"
FT MUTAGEN 153
FT /note="S->A: No change in deacylase activity."
FT /evidence="ECO:0000269|PubMed:16177296"
FT MUTAGEN 247
FT /note="D->N: 5-fold decrease in deacylase activity. Does
FT not affect translocation by TTSS and cellular
FT localization."
FT /evidence="ECO:0000269|PubMed:16177296"
FT MUTAGEN 384
FT /note="H->N: 5-fold decrease in deacylase activity. Does
FT not affect translocation by TTSS and cellular
FT localization."
FT /evidence="ECO:0000269|PubMed:16177296"
SQ SEQUENCE 408 AA; 46077 MW; 8917A5A5590566F4 CRC64;
MPLSVGQGYF TSSISSEKFN AIKESARLPE LSLWEKIKAY FFTTHHAEAL ECIFNLYHHQ
ELNLTPVQVR GAYIKLRALA SQGCKEQFII ESQEHADKLI IKDDNGENIL SIEVECHPEA
FGLAKEINKS HPKPKNISLG DITRLVFFGD SLSDSLGRMF EKTHHILPSY GQYFGGRFTN
GFTWTEFLSS PHFLGKEMLN FAEGGSTSAS YSCFNCIGDF VSNTDRQVAS YTPSHQDLAI
FLLGANDYMT LHKDNVIMVV EQQIDDIEKI ISGGVNNVLV MGIPDLSLTP YGKHSDEKRK
LKDESIAHNA LLKTNVEELK EKYPQHKICY YETADAFKVI MEAASNIGYD TENPYTHHGY
VHVPGAKDPQ LDICPQYVFN DLVHPTQEVH HCFAIMLESF IAHHYSTE
