CAZyme Information: MGYG000001018_01411

Basic Information

• Species: Mediterraneibacter sp900751785
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter sp900751785
• CAZyme ID: MGYG000001018_01411
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
322		34793.96	4.6041

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001018	2841260	MAG	Sweden	Europe

• Gene Location: Start: 2525; End: 3493 Strand: -

Full Sequence      

MSIKGLDVSKFQGEVDWERVKAAGYQFAMLRAGYGFNTVDEQFRRNASECNRIGLPIGAY
WFCYAVSPETASQEADGCINTISGYKLEYPVCYDIEQASADYAAGQGVKLTPSLARQLVQ
SFCGRLEANGYFAMFYSNKNFLDTYLGTDLSARYALWYARYTDTFDGTDCGMWQYTSQGS
VPGISGNVDLDLSYVDYPSVIRNAGLNHLTGTAPSPSPIPPQEYITYVIQSGDTLSGIAA
RFGTTVSALAALNNISDPDKIYAGATLRVPETGSGTKTYTIRPGDTLSGIAVKFGTTVST
LAALNGIADPDRIYAGTTIKIP

Enzyme Prediction     

No EC number prediction in MGYG000001018_01411.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	7	184	6.3e-47	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	7.07e-87	3	194	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	3.26e-43	4	192	1	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.
cd06413	GH25_muramidase_1	1.71e-34	3	190	3	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.
pfam01183	Glyco_hydro_25	1.02e-28	7	184	2	180	Glycosyl hydrolases family 25.
COG3757	Acm	3.37e-27	1	191	61	251	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHB23957.1	3.22e-137	1	272	1	268
QEI31463.1	3.22e-137	1	272	1	268
QRT30197.1	3.22e-137	1	272	1	268
QYX27151.1	1.33e-128	1	321	1	325
QEK16471.1	2.09e-120	1	321	1	325

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	1.79e-13	3	189	5	198	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2WAG_A	2.26e-12	3	194	16	207	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
5A6S_A	3.88e-12	4	195	23	201	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
5JCD_A	1.18e-10	227	322	85	192	Crystalstructure of OsCEBiP [Oryza sativa Japonica Group],5JCD_B Crystal structure of OsCEBiP [Oryza sativa Japonica Group],5JCD_C Crystal structure of OsCEBiP [Oryza sativa Japonica Group]
4B8V_A	2.53e-10	225	322	42	161	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
P07540	3.46e-15	203	321	143	257	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
Q49UX4	5.64e-15	226	321	87	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
P11187	6.49e-15	227	321	163	257	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
P34020	1.58e-13	3	191	1	178	Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1
Q37896	1.85e-12	226	321	164	262	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 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
1.000046	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001018_01411.