STXA_BP933
ID STXA_BP933 Reviewed; 319 AA.
AC P09385; Q9R398;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Shiga-like toxin 2 subunit A;
DE Short=SLT-2 A subunit;
DE Short=SLT-2a;
DE Short=SLT-IIa;
DE EC=3.2.2.22;
DE AltName: Full=Verocytotoxin 2 subunit A;
DE AltName: Full=Verotoxin 2 subunit A;
DE AltName: Full=rRNA N-glycosidase 2;
DE Flags: Precursor;
GN Name=stxA2; Synonyms=stx2A; OrderedLocusNames=L0103;
OS Escherichia phage 933W (Bacteriophage 933W).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae; Sepvirinae; Traversvirus.
OX NCBI_TaxID=10730;
OH NCBI_TaxID=83334; Escherichia coli O157:H7.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Jackson M.P., Neill R.J., O'Brien A.D., Holmes R.K., Newland J.W.;
RT "Nucleotide sequence analysis and comparison of the structural genes for
RT Shiga-like toxin I and Shiga-like toxin II encoded by bacteriophages from
RT Escherichia coli 933.";
RL FEMS Microbiol. Lett. 44:109-114(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=E32511;
RX PubMed=1997410; DOI=10.1128/iai.59.3.1065-1073.1991;
RA Schmitt C.K., McKee M.L., O'Brien A.D.;
RT "Two copies of Shiga-like toxin II-related genes common in
RT enterohemorrhagic Escherichia coli strains are responsible for the
RT antigenic heterogeneity of the O157:H-strain E32511.";
RL Infect. Immun. 59:1065-1073(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=OX3:H21;
RX PubMed=8412629; DOI=10.1006/mpat.1993.1058;
RA Paton A.W., Paton J.C., Manning P.A.;
RT "Polymerase chain reaction amplification, cloning and sequencing of variant
RT Escherichia coli Shiga-like toxin type II operons.";
RL Microb. Pathog. 15:77-82(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9103976; DOI=10.1111/j.1574-6968.1997.tb10305.x;
RA Schmidt H., Scheef J., Janetzki-Mittmann C., Datz M., Karch H.;
RT "An ileX tRNA gene is located close to the Shiga toxin II operon in
RT enterohemorrhagic Escherichia coli O157 and non-O157 strains.";
RL FEMS Microbiol. Lett. 149:39-44(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16232431; DOI=10.1016/s1389-1723(99)80014-0;
RA Kusumoto M., Nishiya Y., Kawamura Y., Shinagawa K.;
RT "Identification of an insertion sequence, IS1203 variant, in a Shiga toxin
RT 2 gene of Escherichia coli O157:H7.";
RL J. Biosci. Bioeng. 87:93-96(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FLY16;
RX PubMed=10071501; DOI=10.1093/jmedent/36.1.108;
RA Iwasa M., Makino S., Asakura H., Kobori H., Morimoto Y.;
RT "Detection of Escherichia coli O157:H7 from Musca domestica (Diptera:
RT Muscidae) at a cattle farm in Japan.";
RL J. Med. Entomol. 36:108-112(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CS1718;
RA Yu J.Y., Jeon H.G., Kang Y.H., Kim E.C., Sohn C.K., Lee B.K.;
RT "Characterization of Shiga toxin genes in Shiga toxin-producing Escherichia
RT coli isolated in Korea.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11561972; DOI=10.1017/s0950268801005635;
RA Asakura H., Makino S., Kobori H., Watarai M., Shirahata T., Ikeda T.,
RA Takeshi K.;
RT "Phylogenetic diversity and similarity of active sites of Shiga toxin (stx)
RT in Shiga toxin-producing Escherichia coli (STEC) isolates from humans and
RT animals.";
RL Epidemiol. Infect. 127:27-36(2001).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15466582; DOI=10.1128/aem.70.10.6309-6314.2004;
RA De Baets L., Van der Taelen I., De Filette M., Pierard D., Allison L.,
RA De Greve H., Hernalsteens J.P., Imberechts H.;
RT "Genetic typing of shiga toxin 2 variants of Escherichia coli by PCR-
RT restriction fragment length polymorphism analysis.";
RL Appl. Environ. Microbiol. 70:6309-6314(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10074068; DOI=10.1128/jb.181.6.1767-1778.1999;
RA Plunkett G. III, Rose D.J., Durfee T.J., Blattner F.R.;
RT "Sequence of Shiga toxin 2 phage 933W from Escherichia coli O157:H7: Shiga
RT toxin as a phage late-gene product.";
RL J. Bacteriol. 181:1767-1778(1999).
RN [11]
RP INDUCTION.
RX PubMed=8550198; DOI=10.1128/iai.64.2.495-502.1996;
RA Muhldorfer I., Hacker J., Keusch G.T., Acheson D.W., Tschape H., Kane A.V.,
RA Ritter A., Olschlager T., Donohue-Rolfe A.;
RT "Regulation of the Shiga-like toxin II operon in Escherichia coli.";
RL Infect. Immun. 64:495-502(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 23-319.
RX PubMed=15075327; DOI=10.1074/jbc.m401939200;
RA Fraser M.E., Fujinaga M., Cherney M.M., Melton-Celsa A.R., Twiddy E.M.,
RA O'Brien A.D., James M.N.G.;
RT "Structure of shiga toxin type 2 (Stx2) from Escherichia coli O157:H7.";
RL J. Biol. Chem. 279:27511-27517(2004).
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 A subunit and multiple
CC copies of a B subunit.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family.
CC {ECO:0000305}.
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DR EMBL; X07865; CAA30714.1; -; Genomic_DNA.
DR EMBL; M59432; AAA19623.1; -; Unassigned_DNA.
DR EMBL; L11079; AAA16362.1; -; Unassigned_DNA.
DR EMBL; Y10775; CAA71747.1; -; Genomic_DNA.
DR EMBL; AB017524; BAA33759.1; -; Genomic_DNA.
DR EMBL; AB015057; BAA34372.1; -; Genomic_DNA.
DR EMBL; AF461167; AAM70033.1; -; Genomic_DNA.
DR EMBL; AB048239; BAB83026.1; -; Genomic_DNA.
DR EMBL; AB048240; BAB83028.1; -; Genomic_DNA.
DR EMBL; AY443052; AAS07596.1; -; Genomic_DNA.
DR EMBL; AF125520; AAD25445.1; -; Genomic_DNA.
DR PIR; I76713; I76713.
DR PIR; S01032; S01032.
DR RefSeq; NP_049500.1; NC_000924.1.
DR PDB; 1R4P; X-ray; 1.77 A; A=23-319.
DR PDB; 2GA4; X-ray; 1.80 A; A=23-319.
DR PDBsum; 1R4P; -.
DR PDBsum; 2GA4; -.
DR SMR; P09385; -.
DR IntAct; P09385; 1.
DR ChEMBL; CHEMBL4662932; -.
DR GeneID; 1261950; -.
DR KEGG; vg:1261950; -.
DR EvolutionaryTrace; P09385; -.
DR Proteomes; UP000002135; Genome.
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 PANTHER; PTHR33453; PTHR33453; 1.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hydrolase;
KW Modulation of host virulence by virus; Protein synthesis inhibitor;
KW Reference proteome; Secreted; Signal; Toxin; Viral exotoxin; Virulence.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..319
FT /note="Shiga-like toxin 2 subunit A"
FT /id="PRO_0000030792"
FT REGION 23..272
FT /note="A1"
FT /evidence="ECO:0000250"
FT REGION 273..314
FT /note="A2"
FT /evidence="ECO:0000250"
FT ACT_SITE 189
FT /evidence="ECO:0000250"
FT SITE 272..273
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000250"
FT DISULFID 263..282
FT VARIANT 17
FT /note="S -> P (in strain: OX3:H21)"
FT VARIANT 26
FT /note="T -> M (in strain: OX3:H21)"
FT VARIANT 277
FT /note="E -> D (in strain: FLY16 and CS1718)"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:1R4P"
FT HELIX 32..46
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:1R4P"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:1R4P"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1R4P"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:1R4P"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:1R4P"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:1R4P"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:1R4P"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:1R4P"
FT HELIX 194..201
FT /evidence="ECO:0007829|PDB:1R4P"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:1R4P"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:1R4P"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:1R4P"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1R4P"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:1R4P"
FT HELIX 300..306
FT /evidence="ECO:0007829|PDB:1R4P"
FT HELIX 312..317
FT /evidence="ECO:0007829|PDB:1R4P"
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
