CAZyme Information: MGYG000001994_01545

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Schaedlerella
• CAZyme ID: MGYG000001994_01545
• CAZy Family: GH25
• CAZyme Description: Autolytic lysozyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
346		38736.66	4.7213

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001994	2695341	MAG	Spain	Europe

• Gene Location: Start: 25613; End: 26653 Strand: +

Full Sequence      

MNLLIRFLFLIKMHILYRYLFYERRMFMSFKGLDVSKYQGTIDWSQVKAAGYDFAMLRAG
YGFNTIDPQFQRNASECNRLGIPIGAYWFCYALNPDIAVQEATGCLNAISGYRLDYPVCY
DIEQDSVNYAAQNGVTITSSLATDIVTAFCNYIEEQGYYAMFYTNKNFLNTYFPADFSSR
YALWYAYYTNSFDGTNCGIWQYTNQGSIPGISGNVDLDIGFIDYPSVIRNAGLNHLNGGT
PTPPPNIDYTTYIIQPGDTLSEIAQRFGTTTQALAQINGISNPNLIYAGNTLKIPETTSE
RYYTIQPGDTLSGIAQKFGTTVQALAQINGISNPNLIYAGTTIRIP

Enzyme Prediction     

No EC number prediction in MGYG000001994_01545.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	34	211	4.1e-47	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.56e-86	30	221	1	191	The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.
cd00599	GH25_muramidase	4.94e-42	31	219	1	185	Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.
cd06525	GH25_Lyc-like	3.07e-30	31	218	1	182	Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
cd06413	GH25_muramidase_1	8.47e-28	31	217	4	186	Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
pfam01183	Glyco_hydro_25	2.33e-26	34	211	2	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHB23957.1	4.33e-134	28	297	1	268
QEI31463.1	4.33e-134	28	297	1	268
QRT30197.1	4.33e-134	28	297	1	268
QYX27151.1	6.96e-130	28	345	1	325
QEK16471.1	1.00e-124	28	345	1	325

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	4.82e-16	31	219	270	466	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A	1.17e-15	31	219	270	466	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
1JFX_A	1.03e-12	31	216	6	198	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A	5.18e-11	34	216	26	197	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
4B8V_A	1.61e-10	246	346	41	161	ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8CMN2	2.89e-15	250	346	84	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	2.89e-15	250	346	84	191	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1
Q37896	3.55e-15	251	345	164	262	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
Q49UX4	1.01e-14	250	345	86	193	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
Q6GC24	8.87e-14	199	345	37	201	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MSSA476) OX=282459 GN=sle1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.991902	0.007386	0.000629	0.000030	0.000016	0.000067

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001994_01545.