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CAZyme Information: MGYG000004508_00761

You are here: Home > Sequence: MGYG000004508_00761

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 UMGS2068 sp900769635
Lineage Bacteria; Firmicutes; Bacilli; RF39; UBA660; UMGS2068; UMGS2068 sp900769635
CAZyme ID MGYG000004508_00761
CAZy Family CBM50
CAZyme Description Cell division suppressor protein YneA
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
339 MGYG000004508_24|CGC1 37314.27 9.8943
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004508 947290 MAG Israel Asia
Gene Location Start: 1170;  End: 2189  Strand: -

Full Sequence      Download help

MKVIIDPARG  GNDTGVSGGG  ITEKDWNLAI  SKYIYNILKN  KGIDVYLTRT  EDVDIPEAER60
ATKIKNYATT  SNDIIVISNR  LNEGKDDGAE  IIYPLRSTNN  LAKALATALE  STGQNVNKYY120
QRRLPSDLAS  DYDYIIRNTS  PYETIIIKYG  YVDSPEDDIT  QLKNYQSLGN  AIANTIISRA180
SSSGTYTVKK  GDTLYSIAKK  YNTTVNNIKS  LNNLSSNTLR  IGQKLKIPLK  ETTTPSTTPT240
PNTLTYTIKK  GDTLYGIATK  YSTTISAIKS  LNNLDTNTLT  IGKTLKIPTT  TSYTTHTIKK300
GDTLYSIAKK  YNTTVNNLIN  LNNLKTTTLS  IGQTLKVPL339

Enzyme Prediction      help

No EC number prediction in MGYG000004508_00761.

CAZyme Signature Domains help

Created with Snap1633506784101118135152169186203220237254271288305322186228CBM50296338CBM50
Family Start End Evalue family coverage
CBM50 186 228 1.4e-18 0.975
CBM50 296 338 7.4e-16 0.975

CDD Domains      download full data without filtering help

Created with Snap16335067841011181351521691862032202372542712883053222177MurNAc-LAA3176Amidase_3178337PRK06347164337PRK063471178AmiC
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02696 MurNAc-LAA 2.28e-26 2 177 1 172
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.
pfam01520 Amidase_3 3.56e-24 3 176 1 172
N-acetylmuramoyl-L-alanine amidase. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.
PRK06347 PRK06347 1.00e-21 178 337 400 591
1,4-beta-N-acetylmuramoylhydrolase.
PRK06347 PRK06347 4.05e-21 164 337 311 523
1,4-beta-N-acetylmuramoylhydrolase.
COG0860 AmiC 2.98e-20 1 178 43 226
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Created with Snap16335067841011181351521691862032202372542712883053223288QVK20078.1|CBM503172QIC05530.1|GH732287AGY48195.1|CBM502287AGE61023.1|CBM503172AYB39952.1|GH73
Hit ID E-Value Query Start Query End Hit Start Hit End
QVK20078.1 8.64e-39 3 288 2 284
QIC05530.1 8.96e-26 3 172 85 248
AGY48195.1 6.59e-25 2 287 3 302
AGE61023.1 2.42e-24 2 287 3 302
AYB39952.1 2.58e-24 3 172 157 320

PDB Hits      download full data without filtering help

Created with Snap163350678410111813515216918620322023725427128830532211775EMI_A1852334UZ2_A1852334XCM_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
5EMI_A 1.03e-08 1 177 5 175
ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
4UZ2_A 6.52e-08 185 233 4 52
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 5.93e-07 185 233 4 52
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

Created with Snap1633506784101118135152169186203220237254271288305322172292sp|P54421|LYTE_BACSU170287sp|Q49UX4|SLE1_STAS1172292sp|O31852|CWLS_BACSU178288sp|Q8CMN2|SLE1_STAES178288sp|Q5HRU2|SLE1_STAEQ
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P54421 1.01e-16 172 292 14 134
Probable peptidoglycan endopeptidase LytE OS=Bacillus subtilis (strain 168) OX=224308 GN=lytE PE=1 SV=1
Q49UX4 8.08e-16 170 287 13 129
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 5.28e-14 172 292 15 136
D-gamma-glutamyl-meso-diaminopimelic acid endopeptidase CwlS OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlS PE=1 SV=1
Q8CMN2 3.46e-13 178 288 75 191
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1
Q5HRU2 3.46e-13 178 288 75 191
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 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
1.000061 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004508_00761.