SSPH2_SALT1
ID SSPH2_SALT1 Reviewed; 788 AA.
AC D0ZPH9; Q7CQ69; Q9RPH0;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=E3 ubiquitin-protein ligase SspH2;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase SspH2 {ECO:0000305};
DE AltName: Full=Salmonella secreted protein H2;
DE AltName: Full=Secreted effector protein sspH2;
GN Name=sspH2; OrderedLocusNames=STM14_2769;
OS Salmonella typhimurium (strain 14028s / SGSC 2262).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=588858;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP SECRETION VIA TYPE III SECRETION SYSTEM, AND INDUCTION.
RX PubMed=10564523; DOI=10.1046/j.1365-2958.1999.01651.x;
RA Miao E.A., Scherer C.A., Tsolis R.M., Kingsley R.A., Adams L.G.,
RA Baumler A.J., Miller S.I.;
RT "Salmonella typhimurium leucine-rich repeat proteins are targeted to the
RT SPI1 and SPI2 type III secretion systems.";
RL Mol. Microbiol. 34:850-864(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19897643; DOI=10.1128/jb.01233-09;
RA Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT "Short-term signatures of evolutionary change in the Salmonella enterica
RT serovar typhimurium 14028 genome.";
RL J. Bacteriol. 192:560-567(2010).
RN [3]
RP SUBCELLULAR LOCATION, AND SECRETION VIA TYPE III SECRETION SYSTEM.
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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=12819095; DOI=10.1128/iai.71.7.4052-4058.2003;
RA Haraga A., Miller S.I.;
RT "A Salmonella enterica serovar typhimurium translocated leucine-rich repeat
RT effector protein inhibits NF-kappa B-dependent gene expression.";
RL Infect. Immun. 71:4052-4058(2003).
RN [5]
RP FUNCTION AS E3 UBIQUITIN-PROTEIN LIGASE, UBIQUITINATION, SUBCELLULAR
RP LOCATION, DOMAIN, AND MUTAGENESIS OF ILE-479; PHE-481; MET-483 AND CYS-580.
RX PubMed=19273841; DOI=10.1073/pnas.0811058106;
RA Quezada C.M., Hicks S.W., Galan J.E., Stebbins C.E.;
RT "A family of Salmonella virulence factors functions as a distinct class of
RT autoregulated E3 ubiquitin ligases.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:4864-4869(2009).
CC -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC promote bacterial survival in host tissues. This protein is an E3
CC ubiquitin ligase that interferes with host's ubiquitination pathway.
CC Contributes to virulence in calves. {ECO:0000269|PubMed:10564523,
CC ECO:0000269|PubMed:19273841}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- ACTIVITY REGULATION: Exists in an autoinhibited state in the absence of
CC substrate protein, due to interactions of the leucine-rich repeat
CC domain with the catalytic domain. Is activated upon binding to a
CC substrate protein (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Host cytoplasm. Host apical cell
CC membrane; Peripheral membrane protein; Cytoplasmic side. Note=Secreted
CC via type III secretion system 2 (SPI-2 TTSS), and delivered into the
CC host cytoplasm. Localizes at the periphery of the host cell,
CC specifically in areas of actin polymerization. Localizes to the apical
CC membrane of polarized epithelial cells.
CC -!- INDUCTION: Transcription is induced in the intracellular environment
CC and is dependent on the SsrA/SsrB system.
CC {ECO:0000269|PubMed:10564523}.
CC -!- DOMAIN: The LRR (leucine-rich repeat) domain forms a slightly curved
CC solenoid and may mediate interaction with target proteins. It is
CC involved in autoinhibition of the enzyme activity by interacting with
CC the catalytic domain. {ECO:0000269|PubMed:19273841}.
CC -!- PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating
CC enzyme UBA1, E2 ubiquitin-conjugating enzyme UBE2D2 and ubiquitin.
CC {ECO:0000269|PubMed:19273841}.
CC -!- SIMILARITY: Belongs to the LRR-containing bacterial E3 ligase family.
CC {ECO:0000305}.
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DR EMBL; AF160727; AAF00615.1; -; Genomic_DNA.
DR EMBL; CP001363; ACY89210.1; -; Genomic_DNA.
DR RefSeq; WP_001115840.1; NZ_CP043402.1.
DR AlphaFoldDB; D0ZPH9; -.
DR SMR; D0ZPH9; -.
DR IntAct; D0ZPH9; 17.
DR MINT; D0ZPH9; -.
DR EnsemblBacteria; ACY89210; ACY89210; STM14_2769.
DR KEGG; seo:STM14_2769; -.
DR PATRIC; fig|588858.6.peg.2578; -.
DR HOGENOM; CLU_018533_1_0_6; -.
DR OMA; PRINCSE; -.
DR BioCyc; SENT588858:STM14_RS12420-MON; -.
DR PHI-base; PHI:3771; -.
DR Proteomes; UP000002695; 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:0020002; C:host cell plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR029487; NEL_dom.
DR Pfam; PF14496; NEL; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR PROSITE; PS51450; LRR; 8.
PE 1: Evidence at protein level;
KW Host cell membrane; Host cytoplasm; Host membrane; Leucine-rich repeat;
KW Membrane; Repeat; Secreted; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Virulence.
FT CHAIN 1..788
FT /note="E3 ubiquitin-protein ligase SspH2"
FT /id="PRO_0000391759"
FT REPEAT 223..242
FT /note="LRR 1"
FT REPEAT 243..264
FT /note="LRR 2"
FT REPEAT 265..282
FT /note="LRR 3"
FT REPEAT 283..302
FT /note="LRR 4"
FT REPEAT 303..324
FT /note="LRR 5"
FT REPEAT 325..342
FT /note="LRR 6"
FT REPEAT 343..364
FT /note="LRR 7"
FT REPEAT 365..382
FT /note="LRR 8"
FT REPEAT 383..404
FT /note="LRR 9"
FT REPEAT 405..422
FT /note="LRR 10"
FT REPEAT 423..445
FT /note="LRR 11"
FT REPEAT 446..466
FT /note="LRR 12"
FT REGION 1..481
FT /note="Interaction with host membrane and with target
FT proteins"
FT REGION 482..491
FT /note="Linker"
FT REGION 492..788
FT /note="E3 ubiquitin-protein ligase catalytic domain"
FT ACT_SITE 580
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000305"
FT MUTAGEN 479
FT /note="I->A: Increase of ubiquitin ligase activity; when
FT associated with A-481 and A-483."
FT /evidence="ECO:0000269|PubMed:19273841"
FT MUTAGEN 481
FT /note="F->A: Increase of ubiquitin ligase activity; when
FT associated with A-479 and A-483."
FT /evidence="ECO:0000269|PubMed:19273841"
FT MUTAGEN 483
FT /note="M->A: Increase of ubiquitin ligase activity; when
FT associated with A-479 and A-481."
FT /evidence="ECO:0000269|PubMed:19273841"
FT MUTAGEN 580
FT /note="C->A: Loss of ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:19273841"
SQ SEQUENCE 788 AA; 87223 MW; E12C103027294080 CRC64;
MPFHIGSGCL PATISNRRIY RIAWSDTPPE MSSWEKMKEF FCSTHQTEAL ECIWTICHPP
AGTTREDVIN RFELLRTLAY AGWEESIHSG QHGENYFCIL DEDSQEILSV TLDDAGNYTV
NCQGYSETHR LTLDTAQGEE GTGHAEGASG TFRTSFLPAT TAPQTPAEYD AVWSAWRRAA
PAEESRGRAA VVQKMRACLN NGNAVLNVGE SGLTTLPDCL PAHITTLVIP DNNLTSLPAL
PPELRTLEVS GNQLTSLPVL PPGLLELSIF SNPLTHLPAL PSGLCKLWIF GNQLTSLPVL
PPGLQELSVS DNQLASLPAL PSELCKLWAY NNQLTSLPML PSGLQELSVS DNQLASLPTL
PSELYKLWAY NNRLTSLPAL PSGLKELIVS GNRLTSLPVL PSELKELMVS GNRLTSLPML
PSGLLSLSVY RNQLTRLPES LIHLSSETTV NLEGNPLSER TLQALREITS APGYSGPIIR
FDMAGASAPR ETRALHLAAA DWLVPAREGE PAPADRWHMF GQEDNADAFS LFLDRLSETE
NFIKDAGFKA QISSWLAQLA EDEALRANTF AMATEATSSC EDRVTFFLHQ MKNVQLVHNA
EKGQYDNDLA ALVATGREMF RLGKLEQIAR EKVRTLALVD EIEVWLAYQN KLKKSLGLTS
VTSEMRFFDV SGVTVTDLQD AELQVKAAEK SEFREWILQW GPLHRVLERK APERVNALRE
KQISDYEETY RMLSDTELRP SGLVGNTDAE RTIGARAMES AKKTFLDGLR PLVEEMLGSY
LNVQWRRN
