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CAZyme Information: MGYG000002954_00109

You are here: Home > Sequence: MGYG000002954_00109

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 UBA1191 sp900543485
Lineage Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Anaerovoracaceae; UBA1191; UBA1191 sp900543485
CAZyme ID MGYG000002954_00109
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
929 104758.8 4.6827
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002954 2474898 MAG United States North America
Gene Location Start: 114622;  End: 117411  Strand: +

Full Sequence      Download help

MFSGDNKGKN  TVDKPVTPHQ  ENDVEPVTRD  TISKEELMAQ  NEDARKIFED  IRSLRESVEA60
LKGEDMDVLA  DSEPRQEPAK  DLIIEDSDEI  LAAKQAIIEQ  ARKDAEEERR  KKEEARRKEL120
AQMQARQEVL  EAQKRAALIE  EEAERKRRQA  AEAERRAKAI  SRKQALDAME  AELQAKNEEL180
AREEAATRET  SGSTGQQAGI  GGSRSADDRR  EATPEEKQAF  FNEQPEDSDV  REKTAVPSQE240
VMRDLEDAKQ  ELLMAQKQQG  EVLGAISQIA  EERTGKLAEE  QQKKLDQQQT  MLREEQEKLQ300
QLLEAHRNER  LERAEREKAE  RELKEQRAKV  ERLLKEERAR  AAREEKLARA  RKKREEKLHR360
AEEKERQKRA  KREAAEKARL  EREQLKQKSI  ADAELGGGVV  NVKGVKINTK  IKDTLSVSLK420
DFIGLADRQE  RKESSEEKAQ  QMKEEREKRR  EEAREAVELS  VKQKLDEYEK  SNFGKKMRSF480
KDFCEKHKVS  LLTSFSIFIM  LLVGVAGVFN  YYTAYAYSYN  GQRLGLVKEK  DDVLRITDLV540
QSALTEDKNV  DVVMDDIEFE  RVSALGDAEI  DSSEDVLKRL  SYMGNLNVKA  YGIYVNGEKV600
GAVENKDAAA  QVLQDIKDRY  SSGREGAEVE  EAVFIENVDI  RRSNTDLEDV  LSEKEMVEKL660
CTSGEKEVKH  QVAAGETLAD  IAKLYSVTEE  QLLEENPDID  QTKLEVGSVI  TFHQTAPILT720
VRITEQVTYE  QEIPYETEER  DDPDMYQGDS  ETSQQGENGL  EEVTSRIVLV  NGEQVEETPL780
VTTVKKEAVS  EIIMVGSKER  PPSVGSGNYI  WPLSGGYTLT  SNFGGRWGRA  HEGIDLGVSV840
GADVLAADGG  IVTYAGYSGA  YGYLVIIDHQ  NGMETRYAHN  SSLLVSEGDE  VFQGMHIAES900
GNSGRSTGPH  LHFEIRVNGV  AKDPLNYLP929

Enzyme Prediction      help

No EC number prediction in MGYG000002954_00109.

CDD Domains      download full data without filtering help

Created with Snap4692139185232278325371418464510557603650696743789836882672929NlpD829924Peptidase_M23831915M23_peptidase811925PRK11649795929nlpD
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0739 NlpD 2.50e-44 672 929 6 262
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551 Peptidase_M23 1.77e-43 829 924 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 3.77e-38 831 915 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.
PRK11649 PRK11649 1.44e-23 811 925 286 407
putative peptidase; Provisional
PRK10871 nlpD 3.31e-20 795 929 181 317
murein hydrolase activator NlpD.

CAZyme Hits      help

Created with Snap4692139185232278325371418464510557603650696743789836882474928QHI72223.1|CBM50481928QAT41769.1|CBM50474928QIB68001.1|CBM50481928QOX64923.1|CBM50499928AVM48688.1|CBM50
Hit ID E-Value Query Start Query End Hit Start Hit End
QHI72223.1 2.20e-117 474 928 257 712
QAT41769.1 1.56e-112 481 928 181 629
QIB68001.1 6.45e-111 474 928 262 717
QOX64923.1 4.73e-95 481 928 486 933
AVM48688.1 8.05e-80 499 928 156 590

PDB Hits      download full data without filtering help

Created with Snap46921391852322783253714184645105576036506967437898368828299263SLU_A8299266MUK_A8319275J1L_A8059155KVP_A8119196UE4_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
3SLU_A 1.40e-16 829 926 244 340
Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A 1.84e-16 829 926 264 360
1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
5J1L_A 2.21e-15 831 927 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]
5KVP_A 9.77e-15 805 915 11 125
Solutionstructure of the catalytic domain of zoocin A [Streptococcus equi subsp. zooepidemicus]
6UE4_A 4.20e-13 811 919 239 354
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

Created with Snap4692139185232278325371418464510557603650696743789836882807929sp|P45682|NLPD_PSEAE811925sp|P0AFS9|MEPM_ECOLI811925sp|P0AFT0|MEPM_ECOL6811925sp|P0AFT1|MEPM_SHIFL811929sp|Q56131|NLPD_SALTI
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P45682 1.38e-18 807 929 176 295
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
P0AFS9 1.37e-16 811 925 287 408
Murein DD-endopeptidase MepM OS=Escherichia coli (strain K12) OX=83333 GN=mepM PE=1 SV=1
P0AFT0 1.37e-16 811 925 287 408
Murein DD-endopeptidase MepM OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mepM PE=3 SV=1
P0AFT1 1.37e-16 811 925 287 408
Murein DD-endopeptidase MepM OS=Shigella flexneri OX=623 GN=mepM PE=3 SV=1
Q56131 1.42e-14 811 929 256 371
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
1.000064 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

start end
491 513