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CAZyme Information: MGYG000004015_02399

You are here: Home > Sequence: MGYG000004015_02399

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 Psychrobacillus sp012843435
Lineage Bacteria; Firmicutes; Bacilli; Bacillales_A; Planococcaceae; Psychrobacillus; Psychrobacillus sp012843435
CAZyme ID MGYG000004015_02399
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
491 MGYG000004015_15|CGC1 54181.33 4.8667
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004015 3783055 MAG United Kingdom Europe
Gene Location Start: 32669;  End: 34144  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004015_02399.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0739 NlpD 2.00e-37 231 491 2 262
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551 Peptidase_M23 5.69e-33 391 486 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 1.09e-30 393 477 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.
pfam07501 G5 6.25e-17 290 362 3 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.
PRK11649 PRK11649 9.83e-14 393 489 313 409
putative peptidase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QEY21410.1 8.52e-289 1 490 1 490
QGM31923.1 2.44e-288 1 490 1 490
ALC87164.1 4.35e-252 1 491 1 493
QUG43663.1 1.33e-243 1 490 1 490
QFG01279.1 7.77e-237 25 491 1 467

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3SLU_A 6.45e-21 381 489 228 341
Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A 8.78e-21 381 489 248 361
1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
5J1L_A 5.25e-18 393 491 65 165
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]
5KVP_A 6.02e-17 358 477 1 125
Solutionstructure of the catalytic domain of zoocin A [Streptococcus equi subsp. zooepidemicus]
2HSI_A 1.01e-13 393 486 180 273
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A0A0H3C9Q9 1.63e-15 364 490 474 607
Cell division protein DipM OS=Caulobacter vibrioides (strain NA1000 / CB15N) OX=565050 GN=dipM PE=3 SV=1
O64046 1.42e-13 381 486 1564 1674
Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1
O31976 1.42e-13 381 486 1564 1674
SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2
Q89AI9 4.01e-13 393 486 251 344
Uncharacterized metalloprotease bbp_296 OS=Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) OX=224915 GN=bbp_296 PE=3 SV=1
P0AFT1 5.53e-13 393 488 314 409
Murein DD-endopeptidase MepM OS=Shigella flexneri OX=623 GN=mepM PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.057091 0.938715 0.003201 0.000445 0.000285 0.000251

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004015_02399.