ID A0A0N7C1X2_9CAUD Unreviewed; 319 AA.
AC A0A0N7C1X2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=rRNA N-glycosylase {ECO:0000256|ARBA:ARBA00012001};
DE EC=3.2.2.22 {ECO:0000256|ARBA:ARBA00012001};
OS Escherichia phage PA28.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Sepvirinae; Traversvirus; Traversvirus PA28.
OX NCBI_TaxID=1660368 {ECO:0000313|EMBL:AKI86768.1, ECO:0000313|Proteomes:UP000225471};
RN [1] {ECO:0000313|EMBL:AKI86768.1, ECO:0000313|Proteomes:UP000225471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26416807; DOI=10.1186/s12864-015-1934-1;
RA Yin S., Rusconi B., Sanjar F., Goswami K., Xiaoli L., Eppinger M.,
RA Dudley E.G.;
RT "Escherichia coli O157:H7 strains harbor at least three distinct sequence
RT types of Shiga toxin 2a-converting phages.";
RL BMC Genomics 16:733-733(2015).
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; KP682381; AKI86768.1; -; Genomic_DNA.
DR SMR; A0A0N7C1X2; -.
DR OrthoDB; 4295at10239; -.
DR Proteomes; UP000225471; 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:0008152; P:metabolic process; 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 Glycosidase {ECO:0000313|EMBL:AKI86768.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AKI86768.1};
KW Protein synthesis inhibitor {ECO:0000256|ARBA:ARBA00023193};
KW Reference proteome {ECO:0000313|Proteomes:UP000225471};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
SQ SEQUENCE 319 AA; 35714 MW; 98F73319ACAE48D6 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 VRAVNEESQP ECQITGDRPV IKINNTLWES
NTAAAFLNRK SQFLYTTGK
//
