ID B6DZW0_9CAUD Unreviewed; 319 AA.
AC B6DZW0;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=rRNA N-glycosylase {ECO:0000256|ARBA:ARBA00012001};
DE EC=3.2.2.22 {ECO:0000256|ARBA:ARBA00012001};
OS Stx2-converting phage 1717.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Pankowvirus; Pankowvirus pv1717.
OX NCBI_TaxID=563769 {ECO:0000313|EMBL:ACI43138.1, ECO:0000313|Proteomes:UP000001042};
RN [1] {ECO:0000313|EMBL:ACI43138.1, ECO:0000313|Proteomes:UP000001042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang Y., Laing C., Hallewell J., Kropinski A., Gannon V.;
RT "Lineage and host source are both predictors of virulence among Escherichia
RT coli O157:H7 strains.";
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000256|ARBA:ARBA00043904}.
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 Evidence={ECO:0000256|ARBA:ARBA00000237};
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family.
CC {ECO:0000256|ARBA:ARBA00043966}.
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DR EMBL; FJ188381; ACI43138.1; -; Genomic_DNA.
DR RefSeq; YP_002274251.1; NC_011357.1.
DR SMR; B6DZW0; -.
DR GeneID; 6973138; -.
DR KEGG; vg:6973138; -.
DR OrthoDB; 4295at10239; -.
DR Proteomes; UP000001042; Genome.
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:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.420.10; Ricin (A subunit), domain 1; 1.
DR Gene3D; 4.10.470.10; Ricin (A Subunit), domain 2; 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 PANTHER; PTHR33453; -; 1.
DR PANTHER; PTHR33453:SF48; RRNA N-GLYCOSYLASE; 1.
DR Pfam; PF00161; RIP; 1.
DR PIRSF; PIRSF001924; Shigella_toxin_subunit_A; 1.
DR SUPFAM; SSF56371; Ribosome inactivating proteins (RIP); 1.
DR PROSITE; PS00275; SHIGA_RICIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein synthesis inhibitor {ECO:0000256|ARBA:ARBA00023193};
KW Reference proteome {ECO:0000313|Proteomes:UP000001042};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
SQ SEQUENCE 319 AA; 35700 MW; 98F73248E9BB48D6 CRC64;
MKCILFKWVL CLLLGFSSVS YSREFTIDFS TQQSYVSSLN SIRTEISTPL EHISQGTTSV
SVINHTPPGS YFAVDIRGLD VYQARFDHLR LIIEQNNLYV AGFVNTATNT FYRFSDFTHI
SVPGVTTVSM TTDSSYTTLQ RVAALERSGM QISRHSLVSS YLALMEFSGN TMTRDASRAV
LRFVTVTAEA LRFRQIQREF RQALSETAPV YTMTPGDVDL TLNWGRISNV LPEYRGEDGV
RVGRISFNNI SAILGTVAVI LNCHHQGARS VRAVNEDSQP ECQITGDRPV IKINNTLWES
NTAAAFLNRK SQFLYTTGK
//
