Calcium binding to a disordered domain of a type III-secreted protein from a coral pathogen promotes secondary structure formation and catalytic activity.
Amino Acid Sequence
Animals
Anthozoa
/ microbiology
Bacterial Proteins
/ chemistry
Binding Sites
Biocatalysis
Calcium
/ metabolism
Calorimetry
EF Hand Motifs
Escherichia coli
/ genetics
Mass Spectrometry
Molecular Dynamics Simulation
Protein Domains
Protein Structure, Secondary
Spectrometry, Fluorescence
Symbiosis
/ physiology
Type III Secretion Systems
/ chemistry
Vibrio
/ metabolism
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
08 05 2019
08 05 2019
Historique:
received:
24
01
2019
accepted:
10
04
2019
entrez:
10
5
2019
pubmed:
10
5
2019
medline:
28
10
2020
Statut:
epublish
Résumé
Strains of the Gram-negative bacterium Vibrio coralliilyticus cause the bleaching of corals due to decomposition of symbiotic microalgae. The V. coralliilyticus strain ATCC BAA-450 (Vc450) encodes a type III secretion system (T3SS). The gene cluster also encodes a protein (locus tag VIC_001052) with sequence homology to the T3SS-secreted nodulation proteins NopE1 and NopE2 of Bradyrhizobium japonicum (USDA110). VIC_001052 has been shown to undergo auto-cleavage in the presence of Ca
Identifiants
pubmed: 31068617
doi: 10.1038/s41598-019-42898-0
pii: 10.1038/s41598-019-42898-0
pmc: PMC6506597
doi:
Substances chimiques
Bacterial Proteins
0
Type III Secretion Systems
0
Calcium
SY7Q814VUP
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
7115Références
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