CAZyme Information: MGYG000000269_01959

Basic Information

• Species: Faecalibacillus sp003480255
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Faecalibacillus; Faecalibacillus sp003480255
• CAZyme ID: MGYG000000269_01959
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
607		69357.79	5.7206

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000269	2159883	Isolate	China	Asia

• Gene Location: Start: 26384; End: 28207 Strand: -

Full Sequence      

MPTWTEKNGQDDITWPKISVVNKGNNLYEATYTVKTKDHKNETGKYNTHVYVYNKDNEVA
VKTLEITVNDTATPKISNVKVENETRKGYTVTCDIQSDSKITKVEMPTWTEKNGQDDLIW
HKAEVKDNGDGTYKATCEIKTSDHNGESGKYITHIYATNTGKTGVYVKDDIVIKNSKPVI
KSATLLTKDSESYTLEIVAEDDSKVSKVYVPTWTEKNGQDDVIWHEAQFESGKWKCTINR
KDHYYQYGNYVSHVYAYDNDNEISDGYVYGSTLISEPDDDLPHISDVYISDKNDDGYTIT
CKVTSKFNVTKVSFPTWTYTNGQDDLVWHQASYIGNNQYSFRILRSYHNYEFGTYITHIY
AYDNVGNVSALVLDYNEIKNTTVRQGWAYMNGQKYFFDNNGNIAGNMPSKKVIDVSSYNG
VIDWETVKRYGDVDGVIIRIASHPNGHYIDDPQFANNLAGCRRYNIPFGVYIYDYANENA
GAYSEAQVVVDILRKYGVSPSELSYPVYFDLERPQLSTSQAVQNSQVFISRMNQYGYTAQ
LYSYRSMLQGVLNHPYILQNMSWMAAYTNTMGWTNPYYHGKFGWQYTSKGSIPGINGNVD
ISCWFNV

Enzyme Prediction     

No EC number prediction in MGYG000000269_01959.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	413	595	1.3e-35	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.45e-60	410	605	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	4.48e-29	411	600	1	182	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	2.44e-19	413	595	1	180	Glycosyl hydrolases family 25.
cd06523	GH25_PlyB-like	2.44e-18	411	602	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.
pfam08481	GBS_Bsp-like	2.50e-18	79	167	1	86	GBS Bsp-like repeat. This domain is found as a repeat in a number of Streptococcus proteins including some hypothetical proteins and Bsp. Bsp is a protein of group B Streptococcus (GBS) which might control cell morphology.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQV05342.1	7.96e-254	1	607	1098	1701
QPS13527.1	8.65e-218	1	607	1063	1662
QMW73215.1	8.65e-218	1	607	1063	1662
QQY27665.1	4.25e-191	2	607	1102	1712
BCL58958.1	1.67e-67	381	606	64	287

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	6.41e-49	386	605	245	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	1.69e-48	386	605	245	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
3HMC_A	6.25e-06	412	602	7	177	Endolysinfrom Bacillus anthracis [Bacillus anthracis]

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
1.000041	0.000007	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000269_01959.