ID   AEXT_AERSA              Reviewed;         475 AA.
AC   Q93Q17;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=ADP-ribosyltransferase toxin AexT;
DE            EC=2.4.2.-;
DE   AltName: Full=Exoenzyme T;
GN   Name=aexT;
OS   Aeromonas salmonicida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=645;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TOXICITY.
RC   STRAIN=ATCC 33658 / DSM 19634 / JCM 7874 / NCIMB 1102 / NCTC 12959, and
RC   JF2267;
RX   PubMed=11889090; DOI=10.1128/jb.184.7.1851-1858.2002;
RA   Braun M., Stuber K., Schlatter Y., Wahli T., Kuhnert P., Frey J.;
RT   "Characterization of an ADP-ribosyltransferase toxin (AexT) from Aeromonas
RT   salmonicida subsp. salmonicida.";
RL   J. Bacteriol. 184:1851-1858(2002).
RN   [2]
RP   SECRETION VIA TYPE III SECRETION PATHWAY.
RX   PubMed=14594831; DOI=10.1128/jb.185.22.6583-6591.2003;
RA   Burr S.E., Stuber K., Frey J.;
RT   "The ADP-ribosylating toxin, AexT, from Aeromonas salmonicida subsp.
RT   salmonicida is translocated via a type III secretion pathway.";
RL   J. Bacteriol. 185:6583-6591(2003).
CC   -!- FUNCTION: Directly involved in the toxicity for RTG-2 (rainbow trout
CC       gonad) fish cells.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Translocated into the cytosol of
CC       fish cells via a type III secretion system.
CC   -!- MISCELLANEOUS: Although the gene exists in strain ATCC 33658, it is not
CC       expressed.
CC   -!- SIMILARITY: Belongs to the YopE family. {ECO:0000305}.
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DR   EMBL; AF288366; AAK83052.1; -; Genomic_DNA.
DR   EMBL; AJ578475; CAE17664.1; -; Genomic_DNA.
DR   RefSeq; WP_005320615.1; NZ_UFSF01000001.1.
DR   AlphaFoldDB; Q93Q17; -.
DR   SMR; Q93Q17; -.
DR   STRING; 1233098.GCA_000315855_01091; -.
DR   OMA; MQIQANT; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   CDD; cd00219; ToxGAP; 1.
DR   Gene3D; 1.20.120.260; -; 1.
DR   InterPro; IPR003540; ADP-ribosyltransferase.
DR   InterPro; IPR003537; YopE-like.
DR   InterPro; IPR014773; YopE_GAP_dom.
DR   InterPro; IPR037168; YopE_GAP_dom_sf.
DR   Pfam; PF03496; ADPrib_exo_Tox; 1.
DR   Pfam; PF03545; YopE; 1.
DR   PRINTS; PR01372; YERSINIAYOPE.
DR   SUPFAM; SSF47233; SSF47233; 1.
DR   PROSITE; PS51996; TR_MART; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Secreted; Toxin; Transferase; Virulence.
FT   CHAIN           1..475
FT                   /note="ADP-ribosyltransferase toxin AexT"
FT                   /id="PRO_0000064470"
FT   DOMAIN          260..436
FT                   /note="TR mART core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        340
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        364
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        403
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
SQ   SEQUENCE   475 AA;  50105 MW;  95069F91E8820877 CRC64;
     MQIQANTVGT QAVAHHSDAT TGVGRMGQME ARQVATGQDA ILLGSRSEPQ KGQGLLSRLG
     AQLARPFVAI KEWISNLLGT DKRAAAPKAQ TAVSPEDLQR LMKQAAFGSS LGGFAKADVL
     NNITGEQLGK DHASLATGNG PLRSLCTALQ AVVIGSQQPQ LRELATGLLA RPIAGIPLQQ
     WGSVGGKVTE LLTSAPPELL KEAMSQLHTA MGEVADLQRA VKAEVAGEPA RSATTAAAVA
     PLQSGESEVN VEPADKALAE GLQEQFGLEA EQYLGEQPHG TYSDAEVMAL GLYTNGEYQH
     LNRSLRQEKQ LDAGQALIDQ GMSTAFEKST PTEQLIKTFR GTHGGDAFNE VAEGQVGHDV
     AYLSTSRDPK VATNFGGSGS ISTIFGRSGI DVSDISVEGD EQEILYNKET DMRVLLSAKD
     ERGVTRRVLE EASLGEQSGH SKGLLDGLDL ARGAGGADKP QEQDIRLKMR GLDLA