CAZyme Information: MGYG000004288_00811

Basic Information

• Species: Faecalicoccus pleomorphus
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Faecalicoccus; Faecalicoccus pleomorphus
• CAZyme ID: MGYG000004288_00811
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
577		65160.17	4.3042

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004288	2108901	MAG	China	Asia

• Gene Location: Start: 56352; End: 58085 Strand: +

Full Sequence      

MPNYQEFKNQVLGRAYDIDGYYGAQCWDGYAKYAQYLGQPICHCTSSGYVKDIWNLRGSN
GILNYNSEVNILQAGDIVVFRECSATPLSHIAIFDSDAGGGYGNFLGQNQGAAGGAFNIV
RLPYSATFDTAFRPNQFAENALDHLQAETGVATLTYDNIQARLNGPTGSVVRKYMAGDQI
TYAWKYVGNGHRYIVWKEGDNYIFLAVSNSEIQGMEPWATFAPVQQDIGYSDSQLIQENG
VAHFTHDNIIIRKGSPDGEDTGKRFMSGQSQEYTEKWIGNGHRYISWVEDGVRYFAAVSG
SETQGEDPWATFTAPEEVEEKPTDPVTPPEEKPEKPEFPESVKMVGIDVSEHNADDIDFT
PYDFVILRANWWTTTDKKFDQFADKLEELGIPYGVYCYDYCGDEASALEQAEYTYNLIRD
RNIQMGVWMDMEDADGWKQKNGYLTKEHCSMVCKVFCDFFKTKGYFTGVYSTKYWFETYC
PTDYPKWVANWGTNDGTCQDDFADYGVLHQYTSYGGMDKNVAYHDLDYYKSDPIVDTPET
PADPETPEEGESIDGGLVNKLVKLLIKLVNKLLSIFK

Enzyme Prediction     

EC	3.2.1.17

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	347	515	6.2e-24	0.9661016949152542

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	3.02e-36	346	528	3	189	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	4.23e-15	346	529	2	186	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	1.74e-13	346	529	2	184	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.
pfam01183	Glyco_hydro_25	9.86e-08	347	515	1	175	Glycosyl hydrolases family 25.
cd06417	GH25_LysA-like	2.33e-04	344	525	1	191	LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASI65996.1	2.73e-54	1	137	1	138
QHO93288.1	1.02e-53	1	137	1	138
AYZ05204.1	1.80e-53	1	137	1	138
ABA45123.1	1.80e-53	1	137	1	138
QBX18018.1	1.80e-53	1	137	1	138

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	1.58e-08	288	441	222	371	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	2.76e-08	288	441	222	371	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8HA43	3.60e-54	1	137	1	138	D-alanyl-L-alanine endopeptidase OS=Streptococcus phage B30 OX=209152 PE=1 SV=2

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
1.000049	0.000006	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004288_00811.