Phylogenetic
linkage of ZapA to the serralysin family of zinc metalloproteases.
Analysis of the deduced amino acid sequence of ZapA indicates the
presence of several signature peptide motifs that are held in common
with many other homologous metalloproteases belonging to the serralysin
family of metalloproteases, including the proteases of S. marcescens, E.
chrysanthemi, P. aeruginosa, and (from this research) P. mirabilis.
The
serralysin family has the zinc metalloprotease domain, the Met turn of
metzincins, and three or more Ca 2 binding motifs, and all are exported
by a COOH terminal secretory signal. The serralysin family of zinc
metalloproteases is in turn part of a larger set of proteins thought to
function as virulence factors in several genera of bacteria.
This set of
virulence proteins includes
Actinobacillus (Haemophilus)
pleuropneumoniae hemolysin protein, AppA (18),
Actinobacillus suis AppA
(17),
Pasteurella haemolytica LktA leukotoxin (20),
enterohemorrhagic E.
coli HlyA hemolysin (33),
Actinobacillus actinomycetemcomitans LktA
leukotoxin (40, 41),
Bordetella pertussis adenylate cyclase CyaA (16),
N. meningitidis Fe-regulated RTX cytotoxin homolog (FrpA) (64),
and
Pseudomonas fluorescens lipase LipA (27, 63).
All of these proteins have
the common feature of the Ca 2 binding GGXGXD repeat motif among other
characteristics.
The phylogenetic linkage map was established from
nucleotide and amino acid sequences stored in the GenBank, EMBL, and Pir
libraries and was analyzed with the Genetics Computer Group program
PILEUP.
....
. One of these factors, ZapA metalloprotease, is of distinctive significance. It is an IgA-degrading protease that is specifically expressed during differentiation of swimmer into swarmer cells ( Wassif et al., 1995). Now-a-days due to increasing antibiotic resistance in Enterobacteriaceae, the multidrug resistant (MDR) strains of Proteus species have also been reported worldwide. ...
....
. One of these factors, ZapA metalloprotease, is of distinctive significance. It is an IgA-degrading protease that is specifically expressed during differentiation of swimmer into swarmer cells ( Wassif et al., 1995). Now-a-days due to increasing antibiotic resistance in Enterobacteriaceae, the multidrug resistant (MDR) strains of Proteus species have also been reported worldwide. ...
Serralysiinin kaltaisten metalloproteaasien C-terminaalin piirteitä:
https://www.ebi.ac.uk/interpro/entry/InterPro/IPR011049/serralysin MeSH Supplementary Concept Data 2020
- MeSH Supplementary
- serralysin
- Unique ID
- C095666
- RDF Unique Identifier
- http://id.nlm.nih.gov/mesh/C095666
- Registry Number
- EC 3.4.24.40
- Heading Mapped to
- *Metalloendopeptidases
- Frequency
- 47
- Note
- zinc metalloproteinases with broad similar specificity for cleavage of the oxidized insulin B chain
- Source
- Methods Enzymol 1995;248:395-413
- Date of Entry
- 1995/10/17
- Revision Date
- 2004/08/06
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