IPA3_SHIFL
ID IPA3_SHIFL Reviewed; 571 AA.
AC Q83RJ4;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=E3 ubiquitin-protein ligase ipaH3;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase ipaH3 {ECO:0000305};
GN Name=ipaH3; OrderedLocusNames=SF1383;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
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 [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), FUNCTION, UBIQUITINATION, DOMAIN,
RP LEUCINE-RICH REPEATS, AND MUTAGENESIS OF CYS-363 AND ASP-365.
RC STRAIN=301 / Serotype 2a;
RX PubMed=18997779; DOI=10.1038/nsmb.1517;
RA Zhu Y., Li H., Hu L., Wang J., Zhou Y., Pang Z., Liu L., Shao F.;
RT "Structure of a Shigella effector reveals a new class of ubiquitin
RT ligases.";
RL Nat. Struct. Mol. Biol. 15:1302-1308(2008).
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 Synthesizes a 'Lys-48'-linked ubiquitin chain, which requires non-
CC covalent binding between ubiquitin and the host ubiquitin-conjugating
CC enzyme UBE2D1. {ECO:0000269|PubMed:18997779}.
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 {ECO:0000250}. Host cytoplasm
CC {ECO:0000250}. Note=Secreted via Mxi-Spa type III secretion system
CC (TTSS), and delivered into the host cytoplasm. {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:0000269|PubMed:18997779}.
CC -!- PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating
CC enzyme, E2 ubiquitin-conjugating enzyme UBE2D3 and ubiquitin.
CC {ECO:0000269|PubMed:18997779}.
CC -!- SIMILARITY: Belongs to the LRR-containing bacterial E3 ligase family.
CC {ECO:0000305}.
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DR EMBL; AE005674; AAN42986.1; -; Genomic_DNA.
DR RefSeq; NP_707279.1; NC_004337.2.
DR PDB; 3CVR; X-ray; 2.80 A; A=1-571.
DR PDBsum; 3CVR; -.
DR AlphaFoldDB; Q83RJ4; -.
DR SMR; Q83RJ4; -.
DR STRING; 198214.SF1383; -.
DR EnsemblBacteria; AAN42986; AAN42986; SF1383.
DR GeneID; 1024395; -.
DR KEGG; sfl:SF1383; -.
DR PATRIC; fig|198214.7.peg.1628; -.
DR HOGENOM; CLU_018533_2_0_6; -.
DR EvolutionaryTrace; Q83RJ4; -.
DR Proteomes; UP000001006; 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:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
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; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Leucine-rich repeat; Reference proteome;
KW Repeat; Secreted; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Virulence.
FT CHAIN 1..571
FT /note="E3 ubiquitin-protein ligase ipaH3"
FT /id="PRO_0000391754"
FT REPEAT 58..81
FT /note="LRR 1"
FT /evidence="ECO:0000269|PubMed:18997779"
FT REPEAT 83..99
FT /note="LRR 2"
FT /evidence="ECO:0000269|PubMed:18997779"
FT REPEAT 100..119
FT /note="LRR 3"
FT /evidence="ECO:0000269|PubMed:18997779"
FT REPEAT 120..144
FT /note="LRR 4"
FT /evidence="ECO:0000269|PubMed:18997779"
FT REPEAT 146..159
FT /note="LRR 5"
FT /evidence="ECO:0000269|PubMed:18997779"
FT REPEAT 160..184
FT /note="LRR 6"
FT /evidence="ECO:0000269|PubMed:18997779"
FT REPEAT 186..202
FT /note="LRR 7"
FT /evidence="ECO:0000269|PubMed:18997779"
FT REPEAT 205..229
FT /note="LRR 8"
FT /evidence="ECO:0000269|PubMed:18997779"
FT REPEAT 232..260
FT /note="LRR 9"
FT /evidence="ECO:0000269|PubMed:18997779"
FT REGION 1..260
FT /note="Interaction with target proteins"
FT REGION 269..278
FT /note="Linker"
FT REGION 279..571
FT /note="E3 ubiquitin-protein ligase catalytic domain"
FT ACT_SITE 363
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000305"
FT MUTAGEN 363
FT /note="C->A,S: Loss of ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:18997779"
FT MUTAGEN 365
FT /note="D->N: Loss of ubiquitin ligase activity, but acts as
FT a thioesterase that uses Cys-363 to hydrolyze the
FT ubiquitin-E2 thioester."
FT /evidence="ECO:0000269|PubMed:18997779"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:3CVR"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:3CVR"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:3CVR"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:3CVR"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:3CVR"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3CVR"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3CVR"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3CVR"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:3CVR"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:3CVR"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:3CVR"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:3CVR"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:3CVR"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:3CVR"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:3CVR"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:3CVR"
FT HELIX 296..301
FT /evidence="ECO:0007829|PDB:3CVR"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:3CVR"
FT HELIX 309..321
FT /evidence="ECO:0007829|PDB:3CVR"
FT TURN 322..325
FT /evidence="ECO:0007829|PDB:3CVR"
FT HELIX 331..344
FT /evidence="ECO:0007829|PDB:3CVR"
FT HELIX 346..358
FT /evidence="ECO:0007829|PDB:3CVR"
FT HELIX 367..383
FT /evidence="ECO:0007829|PDB:3CVR"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:3CVR"
FT HELIX 392..416
FT /evidence="ECO:0007829|PDB:3CVR"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:3CVR"
FT HELIX 424..435
FT /evidence="ECO:0007829|PDB:3CVR"
FT TURN 436..440
FT /evidence="ECO:0007829|PDB:3CVR"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:3CVR"
FT HELIX 458..481
FT /evidence="ECO:0007829|PDB:3CVR"
FT HELIX 484..492
FT /evidence="ECO:0007829|PDB:3CVR"
FT HELIX 495..504
FT /evidence="ECO:0007829|PDB:3CVR"
FT HELIX 543..559
FT /evidence="ECO:0007829|PDB:3CVR"
SQ SEQUENCE 571 AA; 64943 MW; B0DF655E1540D77D CRC64;
MSIMLPINNN FSLSQNSFYN TISGTYADYF SAWDKWEKQA LPGENRNEAV SLLKECLINQ
FSELQLNRLN LSSLPDNLPP QITVLEITQN ALISLPELPA SLEYLDACDN RLSTLPELPA
SLKHLDVDNN QLTMLPELPA LLEYINADNN QLTMLPELPT SLEVLSVRNN QLTFLPELPE
SLEALDVSTN LLESLPAVPV RNHHSEETEI FFRCRENRIT HIPENILSLD PTCTIILEDN
PLSSRIRESL SQQTAQPDYH GPRIYFSMSD GQQNTLHRPL ADAVTAWFPE NKQSDVSQIW
HAFEHEEHAN TFSAFLDRLS DTVSARNTSG FREQVAAWLE KLSTSAELRQ QSFAVAADAT
ESCEDRVALT WNNLRKTLLV HQASEGLFDN DTGALLSLGR EMFRLEILED IARDKVRTLH
FVDEIEVYLA FQTMLAEKLQ LSTAVKEMRF YGVSGVTAND LRTAEAMVRS REENEFTDWF
SLWGPWHAVL KRTEADRWAQ AEEQKYEMLE NEYSQRVADR LKASGLSGDA DAEREAGAQV
MRETEQQIYR QVTDEVLALR LSENGSQLHH S
