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CAZyme Information: MGYG000004850_01262
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; ; | |||||||||||
| CAZyme ID | MGYG000004850_01262 | |||||||||||
| CAZy Family | CBM50 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 4592; End: 6121 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam01551 | Peptidase_M23 | 3.72e-40 | 406 | 504 | 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. |
| COG0739 | NlpD | 5.67e-38 | 316 | 509 | 56 | 265 | Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis]. |
| cd12797 | M23_peptidase | 6.07e-33 | 408 | 495 | 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. |
| COG4942 | EnvC | 1.97e-25 | 346 | 509 | 260 | 419 | Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning]. |
| pfam07501 | G5 | 2.78e-22 | 298 | 371 | 2 | 75 | G5 domain. This domain is found in a wide range of extracellular proteins. It is found tandemly repeated in up to 8 copies. It is found in the N-terminus of peptidases belonging to the M26 family which cleave human IgA. The domain is also found in proteins involved in metabolism of bacterial cell walls suggesting this domain may have an adhesive function. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| CAB1247221.1 | 1.67e-124 | 27 | 508 | 21 | 561 |
| QEY33975.1 | 3.35e-120 | 27 | 508 | 28 | 569 |
| QNK41238.1 | 5.49e-106 | 27 | 508 | 32 | 570 |
| QNO17065.1 | 7.66e-55 | 210 | 504 | 101 | 449 |
| CAB1250016.1 | 4.68e-54 | 210 | 508 | 124 | 473 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6JMX_A | 2.48e-14 | 383 | 508 | 120 | 246 | ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni] |
| 6JN1_A | 4.43e-13 | 383 | 508 | 120 | 246 | ChainA, Peptidase M23 [Campylobacter jejuni] |
| 6JN0_A | 4.49e-13 | 383 | 508 | 120 | 246 | ChainA, Peptidase M23 [Campylobacter jejuni],7E60_A Chain A, Peptidase M23 [Campylobacter jejuni],7E61_A Chain A, Peptidase M23 [Campylobacter jejuni],7E63_A Chain A, Peptidase M23 [Campylobacter jejuni],7E63_B Chain B, Peptidase M23 [Campylobacter jejuni],7E64_A Chain A, Peptidase M23 [Campylobacter jejuni],7E65_A Chain A, Peptidase M23 [Campylobacter jejuni],7E65_B Chain B, Peptidase M23 [Campylobacter jejuni],7E66_A Chain A, Peptidase M23 [Campylobacter jejuni],7E67_A Chain A, Peptidase M23 [Campylobacter jejuni],7E69_A Chain A, Peptidase M23 [Campylobacter jejuni] |
| 6JMZ_A | 4.94e-13 | 383 | 508 | 120 | 246 | ChainA, Peptidase M23 [Campylobacter jejuni] |
| 6JN7_A | 4.94e-13 | 383 | 508 | 120 | 246 | ChainA, Peptidase M23 [Campylobacter jejuni],6JN7_B Chain B, Peptidase M23 [Campylobacter jejuni],6JN7_C Chain C, Peptidase M23 [Campylobacter jejuni],6JN8_A Chain A, Peptidase M23 [Campylobacter jejuni] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P45682 | 1.50e-17 | 375 | 508 | 167 | 294 | Lipoprotein NlpD/LppB homolog OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=PA3623 PE=3 SV=1 |
| P44693 | 4.01e-15 | 408 | 505 | 348 | 443 | Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1 |
| P0ADA3 | 7.56e-15 | 387 | 508 | 259 | 376 | Murein hydrolase activator NlpD OS=Escherichia coli (strain K12) OX=83333 GN=nlpD PE=1 SV=1 |
| P0ADA4 | 7.56e-15 | 387 | 508 | 259 | 376 | Murein hydrolase activator NlpD OS=Shigella flexneri OX=623 GN=nlpD PE=3 SV=1 |
| Q56131 | 9.90e-14 | 388 | 508 | 254 | 370 | Murein hydrolase activator NlpD OS=Salmonella typhi OX=90370 GN=nlpD PE=3 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.999534 | 0.000442 | 0.000040 | 0.000002 | 0.000001 | 0.000007 |
