IPA4_SHIFL
ID IPA4_SHIFL Reviewed; 574 AA.
AC P18009; Q99QQ2;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 3.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Probable E3 ubiquitin-protein ligase ipaH4.5;
DE EC=2.3.2.27;
DE AltName: Full=Probable RING-type E3 ubiquitin transferase ipaH4.5 {ECO:0000305};
GN Name=ipaH4.5; OrderedLocusNames=CP0079;
OS Shigella flexneri.
OG Plasmid pWR100, and Plasmid pCP301.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-7, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=1791758; DOI=10.1111/j.1365-2958.1991.tb02089.x;
RA Venkatesan M.M., Buysse J.M., Hartman A.B.;
RT "Sequence variation in two ipaH genes of Shigella flexneri 5 and homology
RT to the LRG-like family of proteins.";
RL Mol. Microbiol. 5:2435-2445(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-7, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11115111; DOI=10.1046/j.1365-2958.2000.02179.x;
RA Buchrieser C., Glaser P., Rusniok C., Nedjari H., d'Hauteville H.,
RA Kunst F., Sansonetti P.J., Parsot C.;
RT "The virulence plasmid pWR100 and the repertoire of proteins secreted by
RT the type III secretion apparatus of Shigella flexneri.";
RL Mol. Microbiol. 38:760-771(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11292750; DOI=10.1128/iai.69.5.3271-3285.2001;
RA Venkatesan M.M., Goldberg M.B., Rose D.J., Grotbeck E.J., Burland V.,
RA Blattner F.R.;
RT "Complete DNA sequence and analysis of the large virulence plasmid of
RT Shigella flexneri.";
RL Infect. Immun. 69:3271-3285(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a; PLASMID=pCP301;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-208.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=1690703; DOI=10.1128/jb.172.4.1905-1915.1990;
RA Hartman A.B., Venkatesan M.M., Oaks E.V., Buysse J.M.;
RT "Sequence and molecular characterization of a multicopy invasion plasmid
RT antigen gene, ipaH, of Shigella flexneri.";
RL J. Bacteriol. 172:1905-1915(1990).
RN [6]
RP SUBCELLULAR LOCATION, AND SECRETION VIA TYPE III SECRETION SYSTEM.
RC STRAIN=YSH6000 / Serotype 2a;
RX PubMed=11418613; DOI=10.1074/jbc.m101882200;
RA Toyotome T., Suzuki T., Kuwae A., Nonaka T., Fukuda H., Imajoh-Ohmi S.,
RA Toyofuku T., Hori M., Sasakawa C.;
RT "Shigella protein IpaH(9.8) is secreted from bacteria within mammalian
RT cells and transported to the nucleus.";
RL J. Biol. Chem. 276:32071-32079(2001).
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 -!- SUBCELLULAR LOCATION: Secreted. Host cytoplasm {ECO:0000305}.
CC Note=Secreted via Mxi-Spa type III secretion system (TTSS), and
CC delivered into the host cytoplasm. {ECO:0000305}.
CC -!- DOMAIN: The LRR (leucine-rich repeat) domain forms a slightly curved
CC solenoid and may mediate interaction with target proteins.
CC {ECO:0000250|UniProtKB:P0CE12}.
CC -!- PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating
CC enzyme, E2 ubiquitin-conjugating enzyme and ubiquitin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LRR-containing bacterial E3 ligase family.
CC {ECO:0000305}.
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DR EMBL; M76445; AAA26528.1; -; Genomic_DNA.
DR EMBL; AL391753; CAC05788.1; -; Genomic_DNA.
DR EMBL; AF348706; AAK18395.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72347.1; -; Genomic_DNA.
DR EMBL; M32063; AAA26527.1; -; Genomic_DNA.
DR PIR; S18248; B35149.
DR RefSeq; NP_085239.1; NC_002698.1.
DR RefSeq; NP_858212.1; NC_004851.1.
DR RefSeq; WP_010921638.1; NZ_CP026800.1.
DR RefSeq; YP_009062470.1; NC_024996.1.
DR AlphaFoldDB; P18009; -.
DR SMR; P18009; -.
DR STRING; 198214.CP0079; -.
DR EnsemblBacteria; AAL72347; AAL72347; SF_p0079.
DR GeneID; 1238050; -.
DR KEGG; sfl:CP0079; -.
DR PATRIC; fig|198214.7.peg.5326; -.
DR HOGENOM; CLU_018533_2_0_6; -.
DR OMA; IKGETME; -.
DR Proteomes; UP000001006; Plasmid pCP301.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0044074; P:negative regulation by symbiont of host translation; IDA:CACAO.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:CACAO.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:CACAO.
DR GO; GO:0052083; P:suppression by symbiont of host cell-mediated immune response; IMP:CACAO.
DR GO; GO:0052170; P:suppression by symbiont of host innate immune response; IMP:CACAO.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:CACAO.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR032674; LRR_E3_ligase_N.
DR InterPro; IPR029487; NEL_dom.
DR Pfam; PF14496; NEL; 1.
DR Pfam; PF12468; TTSSLRR; 1.
DR PROSITE; PS51450; LRR; 5.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Host cytoplasm; Leucine-rich repeat; Plasmid;
KW Reference proteome; Repeat; Secreted; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Virulence.
FT CHAIN 1..574
FT /note="Probable E3 ubiquitin-protein ligase ipaH4.5"
FT /id="PRO_0000084217"
FT REPEAT 63..82
FT /note="LRR 1"
FT REPEAT 83..104
FT /note="LRR 2"
FT REPEAT 105..122
FT /note="LRR 3"
FT REPEAT 123..143
FT /note="LRR 4"
FT REPEAT 144..165
FT /note="LRR 5"
FT REPEAT 166..183
FT /note="LRR 6"
FT REPEAT 184..205
FT /note="LRR 7"
FT REPEAT 206..223
FT /note="LRR 8"
FT REPEAT 224..246
FT /note="LRR 9"
FT REPEAT 247..270
FT /note="LRR 10"
FT REGION 1..284
FT /note="Interaction with target proteins"
FT /evidence="ECO:0000250|UniProtKB:P0CE12"
FT REGION 285..292
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:P0CE12"
FT REGION 293..574
FT /note="E3 ubiquitin-protein ligase catalytic domain"
FT /evidence="ECO:0000250|UniProtKB:P0CE12"
FT ACT_SITE 379
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8VSC3"
FT CONFLICT 261
FT /note="H -> R (in Ref. 1; AAA26528)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="E -> Q (in Ref. 1; AAA26528)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 65391 MW; 08E8241542978A52 CRC64;
MKPINNHSFF RSLCGLSCIS RLSVEEQCTR DYHRIWDDWA REGTTTENRI QAVRLLKICL
DTREPVLNLS LLKLRSLPPL PLHIRELNIS NNELISLPEN SPLLTELHVN GNNLNILPTL
PSQLIKLNIS FNRNLSCLPS LPPYLQSLSA RFNSLETLPE LPSTLTILRI EGNRLTVLPE
LPHRLQELFV SGNRLQELPE FPQSLKYLKV GENQLRRLSR LPQELLALDV SNNLLTSLPE
NIITLPICTN VNISGNPLST HVLQSLQRLT SSPDYHGPQI YFSMSDGQQN TLHRPLADAV
TAWFPENKQS DVSQIWHAFE HEEHANTFSA FLDRLSDTVS ARNTSGFREQ VAAWLEKLSA
SAELRQQSFA VAADATESCE DRVALTWNNL RKTLLVHQAS EGLFDNDTGA LLSLGREMFR
LEILEDIARD KVRTLHFVDE IEVYLAFQTM LAEKLQLSTA VKEMRFYGVS GVTANDLRTA
EAMVRSREEN EFTDWFSLWG PWHAVLKRTE ADRWAQAEEQ KYEMLENEYS QRVADRLKAS
GLSGDADAER EAGAQVMRET EQQIYRQLTD EVLA
