Species | Aeromonas caviae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Aeromonadaceae; Aeromonas; Aeromonas caviae | |||||||||||
CAZyme ID | MGYG000002527_00092 | |||||||||||
CAZy Family | CBM50 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 71589; End: 72659 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK10871 | nlpD | 3.81e-77 | 12 | 356 | 18 | 319 | murein hydrolase activator NlpD. |
COG0739 | NlpD | 2.66e-45 | 127 | 356 | 4 | 267 | Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis]. |
pfam01551 | Peptidase_M23 | 4.64e-35 | 254 | 349 | 1 | 96 | Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown. |
COG4942 | EnvC | 3.09e-29 | 215 | 353 | 272 | 418 | Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning]. |
cd12797 | M23_peptidase | 8.62e-27 | 256 | 340 | 1 | 85 | M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins. This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AUY09263.1 | 2.78e-251 | 1 | 356 | 1 | 356 |
BBR12030.1 | 2.78e-251 | 1 | 356 | 1 | 356 |
ATP89564.1 | 2.78e-251 | 1 | 356 | 1 | 356 |
AUV16214.1 | 2.78e-251 | 1 | 356 | 1 | 356 |
QLL81935.1 | 2.78e-251 | 1 | 356 | 1 | 356 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4B8V_A | 1.16e-08 | 58 | 169 | 44 | 160 | ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva] |
6SMK_A | 4.92e-08 | 258 | 352 | 31 | 129 | Crystalstructure of catalytic domain A109H mutant of prophage-encoded M23 protein EnpA from Enterococcus faecalis. [Enterococcus faecalis V583],6SMK_B Crystal structure of catalytic domain A109H mutant of prophage-encoded M23 protein EnpA from Enterococcus faecalis. [Enterococcus faecalis V583],6SMK_C Crystal structure of catalytic domain A109H mutant of prophage-encoded M23 protein EnpA from Enterococcus faecalis. [Enterococcus faecalis V583],6SMK_D Crystal structure of catalytic domain A109H mutant of prophage-encoded M23 protein EnpA from Enterococcus faecalis. [Enterococcus faecalis V583],6SMK_E Crystal structure of catalytic domain A109H mutant of prophage-encoded M23 protein EnpA from Enterococcus faecalis. [Enterococcus faecalis V583] |
4QP5_A | 2.60e-06 | 258 | 339 | 35 | 118 | Catalyticdomain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the presence of phosphate [Staphylococcus simulans bv. staphylolyticus],4QP5_B Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the presence of phosphate [Staphylococcus simulans bv. staphylolyticus],4QPB_A Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the absence of phosphate [Staphylococcus simulans],4QPB_B Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the absence of phosphate [Staphylococcus simulans] |
2HSI_A | 8.50e-06 | 256 | 349 | 180 | 273 | Crystalstructure of putative peptidase M23 from pseudomonas aeruginosa, New York Structural Genomics Consortium [Pseudomonas aeruginosa PAO1],2HSI_B Crystal structure of putative peptidase M23 from pseudomonas aeruginosa, New York Structural Genomics Consortium [Pseudomonas aeruginosa PAO1] |
6UE4_A | 9.00e-06 | 256 | 350 | 266 | 360 | ShyAEndopeptidase from Vibrio cholerae (Closed form) [Vibrio cholerae O1 biovar El Tor str. N16961],6UE4_B ShyA Endopeptidase from Vibrio cholerae (Closed form) [Vibrio cholerae O1 biovar El Tor str. N16961] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q56131 | 4.53e-61 | 116 | 356 | 106 | 373 | Murein hydrolase activator NlpD OS=Salmonella typhi OX=90370 GN=nlpD PE=3 SV=2 |
P40827 | 5.04e-61 | 116 | 356 | 110 | 377 | Murein hydrolase activator NlpD OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=nlpD PE=3 SV=2 |
P39700 | 5.04e-61 | 116 | 356 | 110 | 377 | Murein hydrolase activator NlpD OS=Salmonella dublin OX=98360 GN=nlpD PE=2 SV=2 |
P0ADA3 | 4.51e-59 | 116 | 356 | 113 | 379 | Murein hydrolase activator NlpD OS=Escherichia coli (strain K12) OX=83333 GN=nlpD PE=1 SV=1 |
P0ADA4 | 4.51e-59 | 116 | 356 | 113 | 379 | Murein hydrolase activator NlpD OS=Shigella flexneri OX=623 GN=nlpD PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000000 | 0.000114 | 0.999931 | 0.000000 | 0.000000 | 0.000000 |
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