CAZyme Information: MGYG000001473_01245

Basic Information

• Species: Anaerosalibacter massiliensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Sporanaerobacteraceae; Anaerosalibacter; Anaerosalibacter massiliensis
• CAZyme ID: MGYG000001473_01245
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
316		36468.71	10.2293

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001473	3196506	Isolate	not provided	not provided

• Gene Location: Start: 2159; End: 3109 Strand: +

Full Sequence      

MGKIIDISHHQVPSKINYKELCKQLDMAIVRVQYGSRTIDRHYKTHIAEMKRHNTPFGVY
AWVRGVSERDMQKEAQDFFNRAKDLNPSFYILDVEEKSMPDMRGGVNAYVKKLRSLTDKK
IGVYIGHHLYKSFNLDMSKFDFVWIPHYGRNDGTINSKPSFTCDLHQYTDRGRLEGYSGY
LDLNRIMNNRTIEFFTEETKKVSETSNSSKPNKVTDTFYTVKKGDNLSTIAKKYGTTVNN
LVEINNIKNPNLIYPGQKIKISGNIASKKSTIYTVKKGDNLSNISKRYNTTVNKLVKLNN
IKNPNLIYPGQKIRID

Enzyme Prediction     

No EC number prediction in MGYG000001473_01245.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	5	176	1.8e-37	0.9887005649717514
CBM50	219	262	7.2e-17	0.975
CBM50	273	315	8.2e-16	0.95

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06523	GH25_PlyB-like	2.04e-85	3	186	1	177	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.
cd00599	GH25_muramidase	2.31e-25	3	184	1	184	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.
PRK06347	PRK06347	8.67e-23	199	315	459	591	1,4-beta-N-acetylmuramoylhydrolase.
PRK06347	PRK06347	9.37e-22	196	315	382	523	1,4-beta-N-acetylmuramoylhydrolase.
cd06414	GH25_LytC-like	3.71e-19	3	184	2	188	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBP06957.1	1.61e-89	1	315	1	311
ABW19971.1	2.98e-89	4	205	2	203
QUH21063.1	1.74e-87	4	201	2	199
CCO10802.2	1.17e-86	1	287	1	301
QXN70116.1	1.28e-83	1	315	1	333

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3HMC_A	1.70e-49	1	197	4	190	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
4FF5_A	9.80e-46	4	186	54	249	Structurebasis of a novel virulence factor GHIP a glycosyl hydrolase 25 of Streptococcus pneumoniae participating in host cell invasion [Streptococcus pneumoniae]
2NW0_A	7.37e-44	24	196	21	184	ChainA, PlyB [Bacteriophage sp.],2NW0_B Chain B, PlyB [Bacteriophage sp.]
4JZ5_A	4.13e-20	1	184	22	210	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
4B8V_A	1.78e-10	219	315	44	160	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
Q49UX4	3.89e-21	187	315	54	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
Q37896	7.10e-21	190	315	139	262	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
Q6GJK9	2.87e-20	187	315	54	201	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=sle1 PE=3 SV=1
Q6GC24	7.43e-20	187	315	54	201	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MSSA476) OX=282459 GN=sle1 PE=3 SV=1
Q5HIL2	7.43e-20	187	315	54	201	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain COL) OX=93062 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
1.000078	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001473_01245.