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CAZyme Information: MGYG000001507_04676

You are here: Home > Sequence: MGYG000001507_04676

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 Paenibacillus ihuae
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus ihuae
CAZyme ID MGYG000001507_04676
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
509 55263.94 9.2285
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001507 6631509 Isolate not provided not provided
Gene Location Start: 601031;  End: 602560  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001507_04676.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0739 NlpD 2.20e-50 253 509 3 262
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551 Peptidase_M23 3.63e-44 410 504 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.
cd12797 M23_peptidase 2.06e-37 412 495 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 5.32e-24 360 509 267 419
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning].
PRK10871 nlpD 7.81e-20 254 508 63 316
murein hydrolase activator NlpD.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QSF45092.1 0.0 1 509 1 509
AIQ50058.1 5.35e-305 1 509 1 515
AIQ55501.1 6.58e-299 1 509 1 515
CQR59134.1 6.23e-281 1 509 1 516
QQZ62596.1 7.25e-280 1 509 1 516

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3SLU_A 6.23e-19 382 505 210 339
Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A 8.20e-19 382 505 230 359
1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
5J1L_A 8.84e-17 412 509 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]
6JMX_A 1.01e-14 326 508 79 246
ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni]
2HSI_A 1.07e-13 394 508 157 277
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
P45682 1.00e-15 383 508 170 294
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
Q46798 2.28e-15 253 508 41 242
Uncharacterized lipoprotein YgeR OS=Escherichia coli (strain K12) OX=83333 GN=ygeR PE=3 SV=2
P0ADA3 2.35e-15 393 508 262 376
Murein hydrolase activator NlpD OS=Escherichia coli (strain K12) OX=83333 GN=nlpD PE=1 SV=1
P0ADA4 2.35e-15 393 508 262 376
Murein hydrolase activator NlpD OS=Shigella flexneri OX=623 GN=nlpD PE=3 SV=1
Q56131 3.01e-15 393 508 256 370
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
0.999729 0.000268 0.000001 0.000000 0.000000 0.000001

TMHMM  Annotations      download full data without filtering help

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