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CAZyme Information: MGYG000000502_00268

You are here: Home > Sequence: MGYG000000502_00268

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 Brachyspira aalborgi
Lineage Bacteria; Spirochaetota; Brachyspirae; Brachyspirales; Brachyspiraceae; Brachyspira; Brachyspira aalborgi
CAZyme ID MGYG000000502_00268
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
371 41353.65 9.7163
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000502 2577668 MAG Fiji Oceania
Gene Location Start: 21169;  End: 22284  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000502_00268.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0739 NlpD 2.76e-50 125 371 1 267
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551 Peptidase_M23 2.34e-46 263 358 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.
cd12797 M23_peptidase 7.46e-42 265 349 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.
PRK11649 PRK11649 3.79e-28 241 358 287 406
putative peptidase; Provisional
COG4942 EnvC 3.52e-20 266 358 322 414
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CCG56270.1 5.57e-132 4 371 2 392
AGA66378.1 7.89e-132 4 371 2 392
AFR71270.1 2.25e-131 4 371 2 392
ASJ22283.1 3.55e-130 1 371 1 411
QTM05227.1 7.37e-130 20 371 58 412

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5J1L_A 2.46e-28 246 361 46 163
Crystalstructure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1L_C Crystal structure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1M_A Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695],5J1M_C Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695]
3SLU_A 2.31e-25 241 360 222 340
Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A 3.35e-25 241 360 242 360
1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
4RNY_A 1.13e-19 235 366 188 321
Structureof Helicobacter pylori Csd3 from the orthorhombic crystal [Helicobacter pylori 26695],4RNY_B Structure of Helicobacter pylori Csd3 from the orthorhombic crystal [Helicobacter pylori 26695],4RNZ_A Structure of Helicobacter pylori Csd3 from the hexagonal crystal [Helicobacter pylori 26695]
2HSI_A 4.20e-16 247 363 162 278
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8K9M4 1.81e-17 243 359 268 385
Uncharacterized metalloprotease BUsg_310 OS=Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) OX=198804 GN=BUsg_310 PE=3 SV=1
P0AFT0 2.78e-17 243 359 291 408
Murein DD-endopeptidase MepM OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mepM PE=3 SV=1
P0AFS9 2.78e-17 243 359 291 408
Murein DD-endopeptidase MepM OS=Escherichia coli (strain K12) OX=83333 GN=mepM PE=1 SV=1
P0AFT1 2.78e-17 243 359 291 408
Murein DD-endopeptidase MepM OS=Shigella flexneri OX=623 GN=mepM PE=3 SV=1
Q89AI9 2.81e-16 243 370 228 356
Uncharacterized metalloprotease bbp_296 OS=Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) OX=224915 GN=bbp_296 PE=3 SV=1

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
0.999948 0.000063 0.000000 0.000000 0.000000 0.000001

TMHMM  Annotations      download full data without filtering help

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