SSPH2_SALTY
ID SSPH2_SALTY Reviewed; 788 AA.
AC P0CE12; Q7CQ69; Q9RPH0;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=STM2241;
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 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 166-783, DOMAIN, AND ACTIVITY
RP REGULATION.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
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 {ECO:0000250}.
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. {ECO:0000269|PubMed:19273841}.
CC -!- INTERACTION:
CC P0CE12; P61077: UBE2D3; Xeno; NbExp=7; IntAct=EBI-10761075, EBI-348268;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host cytoplasm
CC {ECO:0000250}. Host apical cell membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC Note=Secreted via type III secretion system 2 (SPI-2 TTSS), and
CC delivered into the host cytoplasm. {ECO:0000250}.
CC -!- DOMAIN: The LRR (leucine-rich repeat) domain is involved in
CC autoinhibition of the enzyme activity by interacting with the catalytic
CC 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:0000250}.
CC -!- SIMILARITY: Belongs to the LRR-containing bacterial E3 ligase family.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL21143.1; -; Genomic_DNA.
DR RefSeq; NP_461184.1; NC_003197.2.
DR RefSeq; WP_001115840.1; NC_003197.2.
DR PDB; 3G06; X-ray; 1.90 A; A=166-783.
DR PDBsum; 3G06; -.
DR AlphaFoldDB; P0CE12; -.
DR SMR; P0CE12; -.
DR DIP; DIP-59215N; -.
DR IntAct; P0CE12; 1.
DR STRING; 99287.STM2241; -.
DR PaxDb; P0CE12; -.
DR EnsemblBacteria; AAL21143; AAL21143; STM2241.
DR GeneID; 1253763; -.
DR KEGG; stm:STM2241; -.
DR PATRIC; fig|99287.12.peg.2374; -.
DR HOGENOM; CLU_018533_1_0_6; -.
DR OMA; PRINCSE; -.
DR PhylomeDB; P0CE12; -.
DR BioCyc; SENT99287:STM2241-MON; -.
DR EvolutionaryTrace; P0CE12; -.
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:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IMP:AgBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:AgBase.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:AgBase.
DR GO; GO:0070430; P:positive regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway; IMP:AgBase.
DR GO; GO:0034052; P:positive regulation of plant-type hypersensitive response; IMP:AgBase.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS: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 3D-structure; Host cell membrane; Host cytoplasm; Host membrane;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat; Secreted;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Virulence.
FT CHAIN 1..788
FT /note="E3 ubiquitin-protein ligase SspH2"
FT /id="PRO_0000391758"
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 /evidence="ECO:0000305|PubMed:19273841"
FT REGION 482..491
FT /note="Linker"
FT /evidence="ECO:0000305|PubMed:19273841"
FT REGION 492..788
FT /note="E3 ubiquitin-protein ligase catalytic domain"
FT /evidence="ECO:0000305|PubMed:19273841"
FT ACT_SITE 580
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8VSC3"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 185..201
FT /evidence="ECO:0007829|PDB:3G06"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:3G06"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:3G06"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:3G06"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:3G06"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:3G06"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:3G06"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:3G06"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:3G06"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:3G06"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:3G06"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:3G06"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 439..443
FT /evidence="ECO:0007829|PDB:3G06"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 459..470
FT /evidence="ECO:0007829|PDB:3G06"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 495..500
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 515..520
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 526..536
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 540..544
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 548..560
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 563..572
FT /evidence="ECO:0007829|PDB:3G06"
FT TURN 573..578
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 581..602
FT /evidence="ECO:0007829|PDB:3G06"
FT TURN 603..607
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 609..634
FT /evidence="ECO:0007829|PDB:3G06"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 641..651
FT /evidence="ECO:0007829|PDB:3G06"
FT TURN 652..657
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 668..670
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 675..698
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 701..710
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 712..736
FT /evidence="ECO:0007829|PDB:3G06"
FT TURN 737..740
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 747..777
FT /evidence="ECO:0007829|PDB:3G06"
FT HELIX 778..780
FT /evidence="ECO:0007829|PDB:3G06"
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
