ID   STXA_BPH30              Reviewed;         315 AA.
AC   P10149;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   29-SEP-2021, entry version 91.
DE   RecName: Full=Shiga-like toxin 1 subunit A;
DE            Short=SLT-1 A subunit;
DE            Short=SLT-1a;
DE            Short=SLT-Ia;
DE            EC=3.2.2.22;
DE   AltName: Full=Verocytotoxin 1 subunit A;
DE   AltName: Full=Verotoxin 1 subunit A;
DE   AltName: Full=rRNA N-glycosidase 1;
DE   Flags: Precursor;
GN   Name=stxA;
OS   Bacteriophage H30.
OC   Viruses; unclassified bacterial viruses.
OX   NCBI_TaxID=12371;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3049254; DOI=10.1016/0378-1119(88)90398-8;
RA   Kozlov Y.V., Kabishev A.A., Lukyanov E.V., Bayev A.A.;
RT   "The primary structure of the operons coding for Shigella dysenteriae toxin
RT   and temperature phage H30 shiga-like toxin.";
RL   Gene 67:213-221(1988).
CC   -!- FUNCTION: The A subunit is responsible for inhibiting protein synthesis
CC       through the catalytic inactivation of 60S ribosomal subunits. After
CC       endocytosis, the A subunit is cleaved by furin in two fragments, A1 and
CC       A2: A1 is the catalytically active fragment, and A2 is essential for
CC       holotoxin assembly with the B subunits.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of the N-glycosidic bond at one specific
CC         adenosine on the 28S rRNA.; EC=3.2.2.22;
CC   -!- SUBUNIT: Shiga-like toxin contains a single subunit A and five copies
CC       of subunit B.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the ribosome-inactivating protein family.
CC       {ECO:0000305}.
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DR   EMBL; M23980; AAA72732.1; -; Genomic_DNA.
DR   SMR; P10149; -.
DR   DIP; DIP-6144N; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0098676; P:modulation of host virulence by virus; IEA:UniProtKB-KW.
DR   GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.420.10; -; 1.
DR   Gene3D; 4.10.470.10; -; 1.
DR   InterPro; IPR036041; Ribosome-inact_prot_sf.
DR   InterPro; IPR001574; Ribosome_inactivat_prot.
DR   InterPro; IPR017988; Ribosome_inactivat_prot_CS.
DR   InterPro; IPR016138; Ribosome_inactivat_prot_sub1.
DR   InterPro; IPR016139; Ribosome_inactivat_prot_sub2.
DR   InterPro; IPR016331; Shiga-like_toxin_subunit_A.
DR   Pfam; PF00161; RIP; 1.
DR   PIRSF; PIRSF001924; Shigella_toxin_subunit_A; 1.
DR   SUPFAM; SSF56371; SSF56371; 1.
DR   PROSITE; PS00275; SHIGA_RICIN; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Modulation of host virulence by virus;
KW   Protein synthesis inhibitor; Secreted; Signal; Toxin; Viral exotoxin;
KW   Virulence.
FT   SIGNAL          1..22
FT   CHAIN           23..315
FT                   /note="Shiga-like toxin 1 subunit A"
FT                   /id="PRO_0000030790"
FT   REGION          23..273
FT                   /note="A1"
FT                   /evidence="ECO:0000250"
FT   REGION          274..315
FT                   /note="A2"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        189
FT                   /evidence="ECO:0000250"
FT   SITE            273..274
FT                   /note="Cleavage; by furin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        264..283
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   315 AA;  34814 MW;  8A423DF7ABF58F30 CRC64;
     MKIIIFRVLT FFFVIFSVNV VAKEFTLDFS TAKTYVDSLN VIRSAIGTPL QTISSGGTSL
     LMIDSGTGDN LFAVDVRGID PEEGRFNNLR LIVERNNLYV TGFVNRTNNV FYRFADFSHV
     TFPGTTAVTL SGDSSYTTLQ RVAGISRTGM QINRHSLTTS YLDLMSHSGT SLTQSVARAM
     LRFVTVTAEA LRFRQIQRGF RTTLDDLSGR SYVMTAEDVD LTLNWGRLSS VLPDYHGQDS
     VRVGRISFGS INAILGSVAL ILNCHHHASR VARMASDEFP SMCPADGRVR GITHNKILWD
     SSTLGAILMR RTISS