IPA9_SHIDS
ID IPA9_SHIDS Reviewed; 545 AA.
AC Q326Z6;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=E3 ubiquitin-protein ligase ipaH9.8;
DE EC=2.3.2.27;
DE AltName: Full=Invasion plasmid antigen ipaH9.8;
DE AltName: Full=RING-type E3 ubiquitin transferase ipaH9.8 {ECO:0000305};
GN Name=ipaH9.8; OrderedLocusNames=SDY_P099;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OG Plasmid pSD1_197.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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 and
CC modulates the acute inflammatory responses, thus facilitating bacterial
CC colonization within the host cell. {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, probably due to interactions of the leucine-rich
CC repeat domain with the catalytic domain. Is activated upon binding to a
CC substrate protein (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host cytoplasm
CC {ECO:0000250}. Host nucleus {ECO:0000250}. Note=Secreted via Mxi-Spa
CC type III secretion system (TTSS), and delivered into the host
CC cytoplasm. Transported into the host nucleus (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The LRR (leucine-rich repeat) domain forms a slightly curved
CC solenoid and may mediate interaction with target proteins.
CC {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB64612.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000035; ABB64612.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_406100.1; NC_007607.1.
DR AlphaFoldDB; Q326Z6; -.
DR SMR; Q326Z6; -.
DR STRING; 300267.SDY_2003; -.
DR EnsemblBacteria; ABB64612; ABB64612; SDY_P099.
DR KEGG; sdy:SDY_P099; -.
DR PATRIC; fig|300267.13.peg.5651; -.
DR HOGENOM; CLU_018533_2_0_6; -.
DR Proteomes; UP000002716; Plasmid pSD1_197.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0044164; C:host cell cytosol; ISS:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0044314; P:protein K27-linked ubiquitination; ISS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
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.
PE 3: Inferred from homology;
KW Host cytoplasm; Host nucleus; Leucine-rich repeat; Plasmid;
KW Reference proteome; Repeat; Secreted; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Virulence.
FT CHAIN 1..545
FT /note="E3 ubiquitin-protein ligase ipaH9.8"
FT /id="PRO_0000395758"
FT REPEAT 57..77
FT /note="LRR 1"
FT REPEAT 78..99
FT /note="LRR 2"
FT REPEAT 100..117
FT /note="LRR 3"
FT REPEAT 118..139
FT /note="LRR 4"
FT REPEAT 140..157
FT /note="LRR 5"
FT REPEAT 158..179
FT /note="LRR 6"
FT REPEAT 182..203
FT /note="LRR 7"
FT REPEAT 205..228
FT /note="LRR 8"
FT REGION 1..242
FT /note="Interaction with target proteins"
FT /evidence="ECO:0000250"
FT REGION 243..250
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 251..545
FT /note="E3 ubiquitin-protein ligase catalytic domain"
FT /evidence="ECO:0000250"
FT ACT_SITE 337
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 545 AA; 61973 MW; 52919F70DC1BDDE3 CRC64;
MLPINNNFSL PQNSFYNTIS GTYADYFSAW DKWEKQALPG EERDEAVSRL KECLINNSDE
LRLDRLNLSS LPDNLPAQIT LLNVSYNQLT NLPELPVTLK KLYSASNKLS ELPVLPPALE
SLQVQHNELE NLPALPDSLL TMNISYNEIV SLPSLPQALK NLRATRNFLT ELPAFSEGNN
PVVREYFFDR NQISHIPESI LNLRNECSIH ISDNPLSSHA LQALQRLTSS PDYHGPRIYF
SMSDGQQNTL HRPLADAVTA WFPENKQSDV SQTWHAFEHE EHANTFSAFL DRLSDTVSAR
NTSGFREQVA AWLEKLSASA ELRQQSFAVA ADATESCEDR VALTWNNLRK TLLVHQASEG
LFDNDTGALL SLGREMFRLE ILEDIARDKV RTLHFVDEIE VYLAFQTMLA EKLQLSTAVK
EMRFYGVSGV TANDLRTAEA MVRSREENEF TDWFSLWGPW HAVLKRTEAD RWALAEEQKY
EMLENEYPQR VADRLKASGL SGDADAEREA GAQVMRETEQ QIYRQLTDEV LALRLSENGS
QLHHS
