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CAZyme Information: MGYG000003863_01139

You are here: Home > Sequence: MGYG000003863_01139

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; Hydrogeniiclostridium;
CAZyme ID MGYG000003863_01139
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
569 MGYG000003863_118|CGC1 63118.86 7.822
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003863 2725478 MAG United States North America
Gene Location Start: 1932;  End: 3641  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003863_01139.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01551 Peptidase_M23 3.55e-42 466 563 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 2.99e-39 303 569 4 263
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
cd12797 M23_peptidase 1.08e-38 468 554 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 5.51e-26 357 431 1 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.
COG4942 EnvC 1.01e-19 438 563 291 414
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
QNK41238.1 1.22e-186 22 567 28 570
QEY33975.1 4.05e-182 24 568 26 570
CAB1247221.1 1.58e-174 24 568 19 562
CAB1250016.1 2.80e-96 183 568 93 474
QNO17065.1 6.91e-76 209 568 95 454

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5J1L_A 3.07e-17 448 568 39 165
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 4.85e-15 436 568 113 247
ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni]
3SLU_A 1.23e-14 456 569 228 344
Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A 1.51e-14 456 569 248 364
1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
6UE4_A 8.36e-14 447 564 238 360
ShyAEndopeptidase from Vibrio cholerae (Closed form) [Vibrio cholerae O1 biovar El Tor str. N16961],6UE4_B ShyA Endopeptidase from Vibrio cholerae (Closed form) [Vibrio cholerae O1 biovar El Tor str. N16961]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q56131 1.22e-13 414 567 222 370
Murein hydrolase activator NlpD OS=Salmonella typhi OX=90370 GN=nlpD PE=3 SV=2
P40827 1.25e-13 414 567 226 374
Murein hydrolase activator NlpD OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=nlpD PE=3 SV=2
P39700 1.25e-13 414 567 226 374
Murein hydrolase activator NlpD OS=Salmonella dublin OX=98360 GN=nlpD PE=2 SV=2
P45682 3.43e-13 434 567 168 294
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
P0AFT1 4.22e-13 438 564 277 408
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 OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.999939 0.000088 0.000002 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

start end
20 37
119 141