STXB_BP933
ID STXB_BP933 Reviewed; 89 AA.
AC P09386; Q96198;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Shiga-like toxin 2 subunit B;
DE Short=SLT-2 B subunit;
DE Short=SLT-2b;
DE Short=SLT-IIb;
DE AltName: Full=Verocytotoxin 2 subunit B;
DE Short=Verotoxin 2 subunit B;
DE Flags: Precursor;
GN Name=stxB2; Synonyms=stx2B; OrderedLocusNames=L0104;
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].
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 [3]
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 [4]
RP MUTAGENESIS OF ARG-51; ALA-61 AND GLY-78.
RX PubMed=1991714; DOI=10.1128/jb.173.3.1151-1160.1991;
RA Perera L.P., Samuel J.E., Holmes R.K., O'Brien A.D.;
RT "Identification of three amino acid residues in the B subunit of Shiga
RT toxin and Shiga-like toxin type II that are essential for holotoxin
RT activity.";
RL J. Bacteriol. 173:1151-1160(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 20-89.
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 20-89.
RX PubMed=16820678; DOI=10.1107/s1744309106021968;
RA Fraser M.E., Cherney M.M., Marcato P., Mulvey G.L., Armstrong G.D.,
RA James M.N.;
RT "Binding of adenine to Stx2, the protein toxin from Escherichia coli
RT O157:H7.";
RL Acta Crystallogr. F 62:627-630(2006).
CC -!- FUNCTION: The B subunit is responsible for the binding of the holotoxin
CC to specific receptors on the target cell surface, such as
CC globotriaosylceramide (Gb3) in human intestinal microvilli.
CC -!- SUBUNIT: Shiga-like toxin contains a single subunit A and five copies
CC of subunit B.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: There are three Gb3-binding sites in each subunit B monomer,
CC allowing for a tighter binding to the target cell. Binding sites 1 and
CC 2 have higher binding affinities than site 3.
CC -!- SIMILARITY: Belongs to the stxB family. {ECO:0000305}.
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DR EMBL; X07865; CAA30715.1; -; Genomic_DNA.
DR EMBL; Y10775; CAA71748.1; -; Genomic_DNA.
DR EMBL; AF125520; AAD25446.1; -; Genomic_DNA.
DR PIR; S01033; S01033.
DR RefSeq; NP_049501.1; NC_000924.1.
DR PDB; 1R4P; X-ray; 1.77 A; B/C/D/E/F=20-89.
DR PDB; 2GA4; X-ray; 1.80 A; B/C/D/E/F=20-89.
DR PDB; 6FE4; X-ray; 3.00 A; A/B/C/D/E=20-89.
DR PDBsum; 1R4P; -.
DR PDBsum; 2GA4; -.
DR PDBsum; 6FE4; -.
DR SMR; P09386; -.
DR IntAct; P09386; 1.
DR ChEMBL; CHEMBL4662932; -.
DR UniLectin; P09386; -.
DR ABCD; P09386; 1 sequenced antibody.
DR GeneID; 1262010; -.
DR KEGG; vg:1262010; -.
DR EvolutionaryTrace; P09386; -.
DR Proteomes; UP000002135; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; IEA:InterPro.
DR GO; GO:0098676; P:modulation of host virulence by virus; IEA:UniProtKB-KW.
DR InterPro; IPR008992; Enterotoxin.
DR InterPro; IPR003189; SLT_beta.
DR Pfam; PF02258; SLT_beta; 1.
DR SUPFAM; SSF50203; SSF50203; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Modulation of host virulence by virus;
KW Reference proteome; Secreted; Signal; Toxin; Viral exotoxin; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..89
FT /note="Shiga-like toxin 2 subunit B"
FT /id="PRO_0000030795"
FT DISULFID 22..75
FT MUTAGEN 51
FT /note="R->C: Complete loss of cytotoxicity."
FT /evidence="ECO:0000269|PubMed:1991714"
FT MUTAGEN 61
FT /note="A->T: Complete loss of cytotoxicity."
FT /evidence="ECO:0000269|PubMed:1991714"
FT MUTAGEN 78
FT /note="G->D: Complete loss of cytotoxicity."
FT /evidence="ECO:0000269|PubMed:1991714"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:1R4P"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1R4P"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1R4P"
SQ SEQUENCE 89 AA; 9874 MW; 0EFEDB5B7CC581D9 CRC64;
MKKMFMAVLF ALASVNAMAA DCAKGKIEFS KYNEDDTFTV KVDGKEYWTS RWNLQPLLQS
AQLTGMTVTI KSSTCESGSG FAEVQFNND
