ID   IPA9_SHIB3              Reviewed;         545 AA.
AC   B2TT54;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=SbBS512_A0253;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OG   Plasmid pBS512_211.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP001062; ACD06243.1; -; Genomic_DNA.
DR   RefSeq; WP_012421769.1; NC_010660.1.
DR   AlphaFoldDB; B2TT54; -.
DR   SMR; B2TT54; -.
DR   STRING; 344609.SbBS512_E1692; -.
DR   EnsemblBacteria; ACD06243; ACD06243; SbBS512_A0253.
DR   KEGG; sbc:SbBS512_A0253; -.
DR   HOGENOM; CLU_018533_2_0_6; -.
DR   OMA; VQHNELE; -.
DR   Proteomes; UP000001030; Plasmid pBS512_211.
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; Repeat;
KW   Secreted; Transferase; Ubl conjugation; Ubl conjugation pathway; Virulence.
FT   CHAIN           1..545
FT                   /note="E3 ubiquitin-protein ligase ipaH9.8"
FT                   /id="PRO_0000395756"
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;  62012 MW;  DBE54D3057803E1D 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 SQIWHAFEHE EHANTFSAFL DRLSDTVSAR
     NTSGFREQVA AWLEKLSASA ELRQQSFAVA ADATESCEDR VALTWNNLRK TLLVHQASEG
     LFDNDTGALL SLGREMFRLE ILEDIARDKV RTLHFVDEIE VYLAFQTMLA EKLQLSTAVK
     EMRFYGVSGV TANDLRTAEA MVRSREENEF KDWFSLWGPW HAVLKRTEAD RWAQAEEQKY
     EMLENEYPQR VADRLKASGL SGDADAEREA GAQVMRETEQ LIYRQLTDEV LALRLSENGS
     QLHHS