Entry sw:STXA_BPH30

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   30-NOV-2016, entry version 80.
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 phages.
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
RT   toxin and temperature phage H30 shiga-like toxin.";
RL   Gene 67:213-221(1988).
CC   -!- FUNCTION: The A subunit is responsible for inhibiting protein
CC       synthesis through the catalytic inactivation of 60S ribosomal
CC       subunits. After endocytosis, the A subunit is cleaved by furin in
CC       two fragments, A1 and A2: A1 is the catalytically active fragment,
CC       and A2 is essential for holotoxin assembly with the B subunits.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of the N-glycosidic bond at one
CC       specific adenosine on the 28S rRNA.
CC   -!- SUBUNIT: Shiga-like toxin contains a single subunit A and five
CC       copies of subunit B.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the ribosome-inactivating protein family.
CC       {ECO:0000305}.
DR   EMBL; M23980; AAA72732.1; -; Genomic_DNA.
DR   ProteinModelPortal; P10149; -.
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:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.420.10; -; 1.
DR   Gene3D; 4.10.470.10; -; 1.
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       Shiga-like toxin 1 subunit A.
FT                                /FTId=PRO_0000030790.
FT   REGION       23    273       A1. {ECO:0000250}.
FT   REGION      274    315       A2. {ECO:0000250}.
FT   ACT_SITE    189    189       {ECO:0000250}.
FT   SITE        273    274       Cleavage; by furin. {ECO:0000250}.
FT   DISULFID    264    283       {ECO:0000250}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        31    232       ipfam:RIP [T]
FT   MYHIT       184    200       ipat:SHIGA_RICIN [T]
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
//