Journal:

Article Title: The AsaP1 Peptidase of Aeromonas salmonicida subsp. achromogenes Is a Highly Conserved Deuterolysin Metalloprotease (Family M35) and a Major Virulence Factor ▿

doi: 10.1128/JB.00847-08

Figure Lengend Snippet: Bacterial peptidases with highest amino acid sequence similarity to the mature 172-aa AsaP1 peptidase of A. salmonicida subsp. achromogenes a

Article Snippet: This sequence was cloned into EcoRI-digested pUC18 vector and used as a probe in Southern blotting and screening of recombinant phage. table ft1 table-wrap mode="anchored" t5 TABLE 3. caption a7 Homologous protein Organism Strain GenBank accession no. % E value Gaps aa identity aa positive Extracellular protease Aeromonas hydrophila ATCC 7966 ABK37697 0 92 97 1e−87 Extracellular protease, EprA1 Aeromonas hydrophila AH-1 AAB88221 0 91 95 4e−86 Epr protein Aeromonas hydrophila J-1 AAY21066 0 88 96 6e−63 Metalloprotease Aeromonas punctata NR b BAE72122 0 91 97 2e−69 Peptidyl-Lys metalloendopeptidase Shewanella loihica PV-4 ABO23113 0 60 81 4e−57 Peptidyl-Lys metalloendopeptidase Shewanella woodyi ATCC 51908 EAV37755 0 60 81 3e−57 Peptidyl-Lys metalloendopeptidase Shewanella denitrificans OS217 ABE55895 1 59 80 2e−56 Peptidyl-Lys metalloendopeptidase Shewanella amazonensis SB2B ABL99412 2 59 80 9e−53 Extracellular protease Pseudoalteromonas tunicata D2 EAR28299 2 62 79 5e−49 Probable protease Chromobacterium violaceum ATCC 12472 AAQ61167 1 56 73 8e−49 Open in a separate window a According to BLAST analyses ( 1 ). b NR, not reported.

Techniques: Sequencing