CAZyme Information: MGYG000002441_01856

Basic Information

• Species: Rubneribacter badeniensis
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Eggerthellaceae; Rubneribacter; Rubneribacter badeniensis
• CAZyme ID: MGYG000002441_01856
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
305	MGYG000002441_57|CGC1	32528.18	4.2738

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002441	3364395	Isolate	Germany	Europe

• Gene Location: Start: 11402; End: 12319 Strand: -

Full Sequence      

MRRPTKRTPPPRGASRPAARARTSASTLPRAATRAAAIVGIAALICLLAVLGRCGTFAAD
ESASAPYASPYDWTALERTADRLAYVEDGEVRSQLGVDVSEHQGAIDWQAVAADGIDFAF
VRVGNRGYTEGALYADARYAENLDGAEAAGLAVGAYFFSQATNADEAREEADFVVDLLAG
RSLALPVVFDHEPVSDGAGRANDLDRQTLADCMATFCERLEAAGYDTMVYGNRSDMARFC
AIDGTQAAAERLDEALGHRPVWFAEYDAAVPNAQFDFAIWQYTNDCSVVGISTAVDLDLL
LPAAP

Enzyme Prediction     

No EC number prediction in MGYG000002441_01856.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	97	291	1.6e-42	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	2.34e-70	96	299	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	1.23e-34	96	299	2	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.
pfam01183	Glyco_hydro_25	9.01e-29	97	291	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	6.91e-27	96	298	2	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	1.13e-26	96	297	5	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACV56468.1	1.18e-120	33	304	6	265
APO31195.1	1.18e-120	33	304	6	265
QOS67704.1	3.06e-119	30	302	3	266
BAK43831.1	1.11e-94	70	299	3	220
QTU85263.1	1.05e-71	54	299	2	239

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A6S_A	3.46e-08	129	300	52	201	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	5.34e-08	96	298	11	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 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
0.640305	0.279372	0.076830	0.000893	0.001204	0.001385

TMHMM  Annotations     

start	end
30	52