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Protein

Shiga-like toxin 1 subunit B

Gene

stxB

Organism
Enterobacteria phage H19B (Bacteriophage H19B)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The B subunit is responsible for the binding of the holotoxin to specific receptors on the target cell surface, such as globotriaosylceramide (Gb3) in human intestinal microvilli.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Shiga-like toxin 1 subunit B
Short name:
SLT-1 B subunit
Short name:
SLT-1b
Short name:
SLT-Ib
Alternative name(s):
Verocytotoxin 1 subunit B
Short name:
Verotoxin 1 subunit B
Gene namesi
Name:stxB
Synonyms:sltB
OrganismiEnterobacteria phage H19B (Bacteriophage H19B)
Taxonomic identifieri69932 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambdalikevirusunclassified Lambda-like viruses
Virus hostiEscherichia coli [TaxID: 562]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi33 – 331K → A: No effect on binding to receptor. 1 Publication
Mutagenesisi37 – 371D → A: No effect on binding to receptor. 2 Publications
Mutagenesisi37 – 371D → E: Decrease in binding affinity for Gb3, and in binding capacity. Reduced cytotoxicity. 2 Publications
Mutagenesisi50 – 501F → A: 4-fold decrease in binding affinity for Gb3; 10-fold reduction in binding capacity; great decrease in cell cytotoxicity. 1 Publication
Mutagenesisi54 – 541W → A: Decrease in binding capacity; no effect on binding affinity; moderate effect on cytotoxicity. 1 Publication
Mutagenesisi82 – 821G → T: Decrease in binding affinity for Gb3, and in binding capacity. Reduced cytotoxicity. 1 Publication
Mutagenesisi85 – 851E → A: No effect on binding to receptor. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 8969Shiga-like toxin 1 subunit BPRO_0000030794Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 77

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP69179.

Interactioni

Subunit structurei

Shiga-like toxin contains a single subunit A and five copies of subunit B.2 Publications

Structurei

Secondary structure

1
89
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 3412Combined sources
Beta strandi36 – 383Combined sources
Beta strandi40 – 445Combined sources
Beta strandi47 – 515Combined sources
Helixi56 – 6611Combined sources
Beta strandi69 – 735Combined sources
Beta strandi77 – 804Combined sources
Beta strandi85 – 895Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BOSX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T21-89[»]
1C48X-ray1.60A/B/C/D/E21-89[»]
1C4QX-ray1.52A/B/C/D/E21-89[»]
1CQFX-ray2.20A/B/C/D/E21-89[»]
1CZGX-ray2.50A/B/C/D/E21-89[»]
1CZWX-ray2.50A/B/C/D/E/F/G/H/I/J21-89[»]
1D1IX-ray1.70A/B/C/D/E21-89[»]
1QNUX-ray2.23A/B/C/D/E21-89[»]
2XSCX-ray2.05A/B/C/D/E21-89[»]
4ULLNMR-A21-89[»]
ProteinModelPortaliP69179.
SMRiP69179. Positions 21-89.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69179.

Family & Domainsi

Domaini

There are three Gb3-binding sites in each subunit B monomer, allowing for a tighter binding to the target cell. Binding sites 1 and 2 have higher binding affinities than site 3.

Sequence similaritiesi

Belongs to the stxB family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.40.50.70. 1 hit.
InterProiIPR008992. Enterotoxin.
IPR003189. SLT_beta.
[Graphical view]
PfamiPF02258. SLT_beta. 1 hit.
[Graphical view]
ProDomiPD006042. SLT_beta. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50203. SSF50203. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P69179-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKTLLIAAS LSFFSASALA TPDCVTGKVE YTKYNDDDTF TVKVGDKELF
60 70 80
TNRWNLQSLL LSAQITGMTV TIKTNACHNG GGFSEVIFR
Length:89
Mass (Da):9,743
Last modified:August 1, 1988 - v1
Checksum:iC78F7795CCD7242E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16625 Genomic DNA. Translation: AAA98100.1.
M17358 Genomic DNA. Translation: AAA32230.1.
PIRiB27052. XVBPH9.
B53887.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16625 Genomic DNA. Translation: AAA98100.1.
M17358 Genomic DNA. Translation: AAA32230.1.
PIRiB27052. XVBPH9.
B53887.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BOSX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T21-89[»]
1C48X-ray1.60A/B/C/D/E21-89[»]
1C4QX-ray1.52A/B/C/D/E21-89[»]
1CQFX-ray2.20A/B/C/D/E21-89[»]
1CZGX-ray2.50A/B/C/D/E21-89[»]
1CZWX-ray2.50A/B/C/D/E/F/G/H/I/J21-89[»]
1D1IX-ray1.70A/B/C/D/E21-89[»]
1QNUX-ray2.23A/B/C/D/E21-89[»]
2XSCX-ray2.05A/B/C/D/E21-89[»]
4ULLNMR-A21-89[»]
ProteinModelPortaliP69179.
SMRiP69179. Positions 21-89.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP69179.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP69179.

Family and domain databases

Gene3Di2.40.50.70. 1 hit.
InterProiIPR008992. Enterotoxin.
IPR003189. SLT_beta.
[Graphical view]
PfamiPF02258. SLT_beta. 1 hit.
[Graphical view]
ProDomiPD006042. SLT_beta. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50203. SSF50203. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequence and promoter mapping of the Escherichia coli Shiga-like toxin operon of bacteriophage H-19B."
    de Grandis S., Ginsberg J., Toone M., Climie S., Friesen J., Brunton J.L.
    J. Bacteriol. 169:4313-4319(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Phenylalanine 30 plays an important role in receptor binding of verotoxin-1."
    Clark C., Bast D.J., Sharp A.M., St Hilaire P.M., Agha R., Stein P.E., Toone E.J., Read R.J., Brunton J.L.
    Mol. Microbiol. 19:891-899(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-33; ASP-37; PHE-50 AND GLU-85.
  4. "The identification of three biologically relevant globotriaosyl ceramide receptor binding sites on the Verotoxin 1 B subunit."
    Bast D.J., Banerjee L., Clark C., Read R.J., Brunton J.L.
    Mol. Microbiol. 32:953-960(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-37; TRP-54 AND GLY-82.
  5. "Crystal structure of the cell-binding B oligomer of verotoxin-1 from E. coli."
    Stein P.E., Boodhoo A., Tyrrell G.J., Brunton J.L., Read R.J.
    Nature 355:748-750(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-89.
  6. "Solution structure of the carbohydrate-binding B-subunit homopentamer of verotoxin VT-1 from E. coli."
    Richardson J.M., Evans P.D., Homans S.W., Donohue-Rolfe A.
    Nat. Struct. Biol. 4:190-193(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 21-89.
  7. "Structure of the shiga-like toxin I B-pentamer complexed with an analogue of its receptor Gb3."
    Ling H., Boodhoo A., Hazes B., Cummings M.D., Armstrong G.D., Brunton J.L., Read R.J.
    Biochemistry 37:1777-1788(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 21-89 IN COMPLEX WITH RECEPTOR GB3.
  8. "Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands."
    Kitov P.I., Sadowska J.M., Mulvey G., Armstrong G.D., Ling H., Pannu N.S., Read R.J., Bundle D.R.
    Nature 403:669-672(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 21-89 IN COMPLEX WITH INHIBITOR.

Entry informationi

Entry nameiSTXB_BPH19
AccessioniPrimary (citable) accession number: P69179
Secondary accession number(s): P08027
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 14, 2015
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.