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CAZyme Information: MGYG000002208_00886

You are here: Home > Sequence: MGYG000002208_00886

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 RUG705 sp900551455
Lineage Bacteria; Firmicutes; Bacilli; RF39; UBA660; RUG705; RUG705 sp900551455
CAZyme ID MGYG000002208_00886
CAZy Family CBM50
CAZyme Description Cell division suppressor protein YneA
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
373 41601.76 9.1554
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002208 1058803 MAG Spain Europe
Gene Location Start: 15934;  End: 17055  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002208_00886.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM50 280 322 6.5e-16 0.975

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK06347 PRK06347 4.18e-37 174 371 332 592
1,4-beta-N-acetylmuramoylhydrolase.
PRK06347 PRK06347 1.42e-29 166 321 399 591
1,4-beta-N-acetylmuramoylhydrolase.
cd02696 MurNAc-LAA 4.96e-24 2 157 22 172
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.
PRK06347 PRK06347 1.46e-21 220 370 324 523
1,4-beta-N-acetylmuramoylhydrolase.
PRK10783 mltD 1.73e-21 206 319 320 444
membrane-bound lytic murein transglycosylase D; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QVK20078.1 4.13e-62 3 273 23 286
QIC05530.1 9.32e-34 1 166 103 262
AGR47373.1 3.83e-33 3 166 178 335
ACL69398.1 4.19e-33 164 322 136 303
QOS97536.1 1.46e-32 3 168 177 336

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4B8V_A 4.27e-13 175 323 44 218
ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva]
4UZ2_A 2.87e-08 174 219 4 49
Crystalstructure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_D Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ3_A Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8]
4XCM_A 2.87e-07 174 219 4 49
Crystalstructure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4XCM_B Crystal structure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O07532 1.38e-25 172 321 173 350
Peptidoglycan endopeptidase LytF OS=Bacillus subtilis (strain 168) OX=224308 GN=lytF PE=1 SV=2
Q5HRU2 9.79e-22 174 322 28 191
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1
Q8CMN2 9.79e-22 174 322 28 191
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1
Q49UX4 1.92e-21 174 319 28 191
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1
O31852 2.74e-21 166 321 81 268
D-gamma-glutamyl-meso-diaminopimelic acid endopeptidase CwlS OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlS 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
1.000037 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002208_00886.