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CAZyme Information: MGYG000001604_01812

You are here: Home > Sequence: MGYG000001604_01812

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 Barnesiella sp002159975
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae; Barnesiella; Barnesiella sp002159975
CAZyme ID MGYG000001604_01812
CAZy Family GH23
CAZyme Description Membrane-bound lytic murein transglycosylase F
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
464 53098.17 6.3226
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001604 2665014 MAG China Asia
Gene Location Start: 9291;  End: 10685  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001604_01812.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH23 302 459 2.3e-26 0.837037037037037

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10859 PRK10859 4.75e-97 1 457 1 449
membrane-bound lytic murein transglycosylase MltF.
cd13403 MLTF-like 1.17e-85 295 459 1 160
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins. This subfamily includes membrane-bound lytic murein transglycosylase F (MltF, murein lyase F) that degrades murein glycan strands. It is responsible for catalyzing the release of 1,6-anhydromuropeptides from peptidoglycan. Lytic transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do goose-type lysozymes. However, in addition, it also makes a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
COG4623 MltF 4.14e-76 34 455 14 428
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms].
cd01009 PBP2_YfhD_N 1.26e-67 43 270 1 223
The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold protein superfamily. This subfamily includes the solute binding domain YfhD_N. These domains are found in the YfhD proteins that are predicted to function as lytic transglycosylases that cleave the glycosidic bond between N-acetylmuramic acid and N-acetylglucosamin in peptidoglycan, while the YfhD_N domain might act as an auxiliary or regulatory subunit. In addition to periplasmic solute binding domain, they have an SLT domain, typically found in soluble lytic transglycosylases, and a C-terminal low complexity domain. The YfhD proteins might have been recruited to create localized cell wall openings required for transport of large substrates such as DNA. They belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
pfam01464 SLT 1.10e-21 305 410 11 114
Transglycosylase SLT domain. This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AHF13148.1 0.0 1 464 1 464
BCI64481.1 1.77e-212 9 463 5 458
QMW89280.1 1.34e-176 12 462 12 461
AAO75290.1 1.34e-176 12 462 12 461
QUT70490.1 1.70e-176 12 462 19 468

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4OYV_A 1.62e-47 31 457 6 427
Crystalstructure of MltF from Pseudomonas aeruginosa complexed with leucine [Pseudomonas aeruginosa PAO1]
4OWD_A 1.62e-47 31 457 6 427
Crystalstructure of MltF from Pseudomonas aeruginosa complexed with cysteine [Pseudomonas aeruginosa PAO1],4OXV_A Crystal structure of MltF from Pseudomonas aeruginosa complexed with valine [Pseudomonas aeruginosa PADK2_CF510],4P0G_A Crystal structure of MltF from Pseudomonas aeruginosa complexed with bulgecin and muropeptide [Pseudomonas aeruginosa PAO1],4P11_A Native crystal structure of MltF Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1]
4OZ9_A 1.95e-47 33 457 1 420
Crystalstructure of MltF from Pseudomonas aeruginosa complexed with isoleucine [Pseudomonas aeruginosa PAO1]
5AA2_D 7.65e-47 8 457 23 461
Crystalstructure of MltF from Pseudomonas aeruginosa in complex with NAM-pentapeptide. [Pseudomonas aeruginosa BWHPSA013]
5AA2_A 7.65e-47 8 457 23 461
Crystalstructure of MltF from Pseudomonas aeruginosa in complex with NAM-pentapeptide. [Pseudomonas aeruginosa BWHPSA013],5AA2_C Crystal structure of MltF from Pseudomonas aeruginosa in complex with NAM-pentapeptide. [Pseudomonas aeruginosa BWHPSA013]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A8ZWR8 5.45e-56 39 461 37 451
Membrane-bound lytic murein transglycosylase F OS=Desulfococcus oleovorans (strain DSM 6200 / JCM 39069 / Hxd3) OX=96561 GN=mltF PE=3 SV=2
Q4KHS7 1.13e-54 6 457 12 450
Membrane-bound lytic murein transglycosylase F OS=Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5) OX=220664 GN=mltF PE=3 SV=2
Q3KHL5 2.21e-54 6 457 12 450
Membrane-bound lytic murein transglycosylase F OS=Pseudomonas fluorescens (strain Pf0-1) OX=205922 GN=mltF PE=3 SV=1
B0KRE9 8.36e-53 3 457 9 450
Membrane-bound lytic murein transglycosylase F OS=Pseudomonas putida (strain GB-1) OX=76869 GN=mltF PE=3 SV=1
A4SNZ5 1.04e-52 34 456 38 451
Membrane-bound lytic murein transglycosylase F OS=Aeromonas salmonicida (strain A449) OX=382245 GN=mltF PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000001 1.000038 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001604_01812.