CAZyme Information: MGYG000000223_04300

Basic Information

• Species: NSJ-61 sp003433845
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; NSJ-61; NSJ-61 sp003433845
• CAZyme ID: MGYG000000223_04300
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
355		41858.2	5.2991

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000223	4367631	Isolate	China	Asia

• Gene Location: Start: 102; End: 1169 Strand: +

Full Sequence      

MFLGWREISGEKYYFNKDGYITTGFMSIDSKIYYFNEQGHMMIGNVYINGENYYFYEDGH
MAKNEWVIKDKKSLYYDENGILIKNKKIIIQGIEYNFDENGYITSWVFGKDGEVYYYNQG
VKLTGWQSLGGQKYYFNSLGQRIGNGNVKKVIDISEFDGIIDWIKVVEQGDIDHVIVRIG
FGDVREDYQLQRNIQKLKQYKIPFSLYLYSYAENNDEAIAEANFVVKILDKYNIDRNTKI
YYDIEKPTYLDGRDIKIKPSQYKKIIPTFMNILNKHGFKNCAVYTYTSYLYNKDSGFGGD
SDLIKLVEWIAQYNSDHVYYAGKDLKETDFKGWQYSEYEYIPGFLNNVDVSIFFN

Enzyme Prediction     

No EC number prediction in MGYG000000223_04300.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	152	343	5.7e-30	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.47e-40	149	354	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	1.62e-20	150	353	1	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.
cd06523	GH25_PlyB-like	4.20e-15	150	351	1	175	PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
cd06522	GH25_AtlA-like	6.55e-15	149	352	1	190	AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain.
NF033840	PspC_relate_1	5.02e-14	4	141	511	628	PspC-related protein choline-binding protein 1. Members of this family share C-terminal homology to the choline-binding form of the pneumococcal surface antigen PspC, but not to its allelic LPXTG-anchored forms because they lack the choline-binding repeat region. Members of this family should not be confused with PspC itself, whose identity and function reflect regions N-terminal to the choline-binding region. See Iannelli, et al. (PMID: 11891047) for information about the different allelic forms of PspC.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNM12694.1	1.10e-189	62	355	340	633
ANO37355.1	1.37e-44	124	354	29	253
BAX31218.1	4.30e-44	124	354	46	270
BBG37459.1	4.30e-44	124	354	46	270
VGM85417.1	2.87e-43	124	354	151	375

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	1.77e-43	124	354	244	468	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	4.77e-43	124	354	244	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000019	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000223_04300.