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CAZyme Information: MGYG000002143_00031

You are here: Home > Sequence: MGYG000002143_00031

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 CAG-83 sp900545585
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-83; CAG-83 sp900545585
CAZyme ID MGYG000002143_00031
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
577 64400.86 5.0835
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002143 2135856 MAG United States North America
Gene Location Start: 29481;  End: 31214  Strand: -

Full Sequence      Download help

MKQQLEQENK  QENTVHDPNR  EHMTLSALWQ  LWMDNLKSWR  QYRDEHPDLF  TLNLQAGLRH60
IAAWFRQVGG  SAHHLVDENR  HSSFPESEHG  AAQLFLFFWN  SLSRLGASLR  ERARNARKKL120
IRASDRRRSY  FEKLKLHPVA  FLAGAMGLAA  AATVLSLYTV  GAHAVYDGTD  LGVVSSQHAV180
ELAVSEVESI  TRETLHDSSY  TVDQSLLTTE  TGVYLRKDVI  GEEEFSSELT  DQLGLVEYAY240
VLYVDGEKVV  ATTFPGALDD  ILNQLKLGYQ  TEDTVDAYFV  EDVEIRQEYV  DSSYVMNLGY300
IAEILNETKE  GEVTYTVKKG  DSYYSIADEY  GLSVDALMKL  NPGYDPKILR  VGDVLTISNA360
VPYLTVVNVE  RQRYVQDVPY  PVEYTDDASM  YQGEYKVTSP  GVYGKADITA  NVTYINGTET420
ERQIVASATL  SQPVTEYQIR  GTKERPSWFP  TGSFGWPCSG  VITSYFGARN  TGIRGASTYH480
EAIDIANSYG  TPIYASDGGT  VIYAGWMGGY  GYLVKIDHGN  GYVTYYGHNS  SLLVSVGEHV540
HKGQQVARMG  STGVSSGNHC  DFRIQLNGTF  LNPLNYL577

Enzyme Prediction      help

No EC number prediction in MGYG000002143_00031.

CDD Domains      download full data without filtering help

Created with Snap285786115144173201230259288317346375403432461490519548314577NlpD478573Peptidase_M23480564M23_peptidase314577nlpD450577EnvC
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0739 NlpD 6.57e-46 314 577 3 261
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551 Peptidase_M23 1.24e-40 478 573 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 5.50e-35 480 564 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.
PRK10871 nlpD 5.61e-27 314 577 62 316
murein hydrolase activator NlpD.
COG4942 EnvC 2.01e-26 450 577 295 418
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning].

CAZyme Hits      help

Created with Snap28578611514417320123025928831734637540343246149051954827577BCK82550.1|CBM5015577QUO34525.1|CBM5042577BCK79529.1|CBM5075577QNL44258.1|CBM5074577QUO39608.1|CBM50
Hit ID E-Value Query Start Query End Hit Start Hit End
BCK82550.1 1.23e-242 27 577 17 568
QUO34525.1 3.84e-228 15 577 10 573
BCK79529.1 8.78e-212 42 577 12 553
QNL44258.1 2.70e-190 75 577 60 561
QUO39608.1 4.41e-177 74 577 63 565

PDB Hits      download full data without filtering help

Created with Snap2857861151441732012302592883173463754034324614905195484805765J1L_A4505774BH5_A4525776JMX_A4505776TPI_A4525776JN1_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
5J1L_A 1.44e-16 480 576 65 163
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]
4BH5_A 1.75e-14 450 577 17 140
LytMdomain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12],4BH5_B LytM domain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12],4BH5_C LytM domain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12],4BH5_D LytM domain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12]
6JMX_A 7.34e-14 452 577 121 246
ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni]
6TPI_A 5.92e-13 450 577 261 384
EnvCbound to the FtsX periplasmic domain [Escherichia coli K-12]
6JN1_A 1.31e-12 452 577 121 246
ChainA, Peptidase M23 [Campylobacter jejuni]

Swiss-Prot Hits      download full data without filtering help

Created with Snap285786115144173201230259288317346375403432461490519548311577sp|P39700|NLPD_SALDU311577sp|Q56131|NLPD_SALTI311577sp|P40827|NLPD_SALTY308577sp|Q46798|YGER_ECOLI314577sp|P0ADA3|NLPD_ECOLI
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P39700 4.26e-20 311 577 117 374
Murein hydrolase activator NlpD OS=Salmonella dublin OX=98360 GN=nlpD PE=2 SV=2
Q56131 5.47e-20 311 577 113 370
Murein hydrolase activator NlpD OS=Salmonella typhi OX=90370 GN=nlpD PE=3 SV=2
P40827 5.73e-20 311 577 117 374
Murein hydrolase activator NlpD OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=nlpD PE=3 SV=2
Q46798 6.75e-20 308 577 36 242
Uncharacterized lipoprotein YgeR OS=Escherichia coli (strain K12) OX=83333 GN=ygeR PE=3 SV=2
P0ADA3 2.57e-19 314 577 122 376
Murein hydrolase activator NlpD OS=Escherichia coli (strain K12) OX=83333 GN=nlpD PE=1 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
1.000057 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

start end
136 158