IPA9_SHIF2
ID IPA9_SHIF2 Reviewed; 545 AA.
AC D2AJU0;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 55.
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=SFxv_5076;
OS Shigella flexneri serotype X (strain 2002017).
OG Plasmid pSFxv_1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=591020;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2002017;
RX PubMed=19955273; DOI=10.1128/jcm.00614-09;
RA Ye C., Lan R., Xia S., Zhang J., Sun Q., Zhang S., Jing H., Wang L., Li Z.,
RA Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., Luo X.,
RA Bai X., Wang Y., Wang P., Xu Q., Xu J.;
RT "Emergence of a new multidrug-resistant serotype X variant in an epidemic
RT clone of Shigella flexneri.";
RL J. Clin. Microbiol. 48:419-426(2010).
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; CP001384; ADA76971.1; -; Genomic_DNA.
DR RefSeq; WP_000936806.1; NC_017319.1.
DR PDB; 6LOJ; X-ray; 3.72 A; A=22-244.
DR PDB; 6LOL; X-ray; 2.75 A; A=22-545.
DR PDBsum; 6LOJ; -.
DR PDBsum; 6LOL; -.
DR AlphaFoldDB; D2AJU0; -.
DR SMR; D2AJU0; -.
DR EnsemblBacteria; ADA76971; ADA76971; SFxv_5076.
DR KEGG; sfe:SFxv_5076; -.
DR PATRIC; fig|591020.3.peg.5448; -.
DR HOGENOM; CLU_018533_2_0_6; -.
DR OMA; VQHNELE; -.
DR Proteomes; UP000001884; Plasmid pSFxv_1.
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 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Host nucleus; Leucine-rich repeat; Plasmid;
KW Repeat; Secreted; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Virulence.
FT CHAIN 1..545
FT /note="E3 ubiquitin-protein ligase ipaH9.8"
FT /id="PRO_0000395759"
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"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:6LOL"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:6LOL"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:6LOL"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:6LOL"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6LOL"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:6LOL"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6LOL"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6LOL"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:6LOL"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:6LOL"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:6LOL"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:6LOL"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:6LOL"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:6LOL"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:6LOL"
FT TURN 272..276
FT /evidence="ECO:0007829|PDB:6LOL"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:6LOL"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:6LOL"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:6LOL"
FT HELIX 305..318
FT /evidence="ECO:0007829|PDB:6LOL"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:6LOL"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:6LOL"
FT HELIX 342..359
FT /evidence="ECO:0007829|PDB:6LOL"
FT HELIX 366..390
FT /evidence="ECO:0007829|PDB:6LOL"
FT HELIX 398..409
FT /evidence="ECO:0007829|PDB:6LOL"
FT TURN 410..414
FT /evidence="ECO:0007829|PDB:6LOL"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:6LOL"
FT HELIX 433..456
FT /evidence="ECO:0007829|PDB:6LOL"
FT HELIX 458..466
FT /evidence="ECO:0007829|PDB:6LOL"
FT HELIX 471..477
FT /evidence="ECO:0007829|PDB:6LOL"
FT HELIX 481..484
FT /evidence="ECO:0007829|PDB:6LOL"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:6LOL"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:6LOL"
FT HELIX 513..526
FT /evidence="ECO:0007829|PDB:6LOL"
FT TURN 531..535
FT /evidence="ECO:0007829|PDB:6LOL"
SQ SEQUENCE 545 AA; 62000 MW; D48CBBB3FC1020F2 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 TDWFSLWGPW HAVLKRTEAD RWAQAEEQKY
EMLENEYPQR VADRLKASGL SGDADAEREA GAQVMRETEQ QIYRQLTDEV LALRLSENGS
QLHHS
