CAZyme Information: MGYG000003593_02151

Basic Information

• Species: Enterocloster sp900770345
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Enterocloster; Enterocloster sp900770345
• CAZyme ID: MGYG000003593_02151
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
558	MGYG000003593_198|CGC1	59069.41	4.6964

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003593	4467273	MAG	Fiji	Oceania

• Gene Location: Start: 42907; End: 44583 Strand: +

Full Sequence      

MKINRKKCGKCAAHRMLKKCRILALAGVIGAGTLSSSVAAWAAGPGDGDSVYTSEGGPGA
AGAAAAGAASQTGNTAGPGGPGAVGSQTGQDSGSSQNQNSQSQSSQAAAQTDPNAWKKIN
GVYRMSDGTAINNVLKRGIDVSRWQGDINWSQVAADDVSFVMLGTRSKGAVDPYFHTNIQ
KASAAGIQVGVYIYSLATTVSMAEEEADFVLDLIHDYPVSYPVAFDMEDSAQGALSKEEL
AAIANAFCRKISDAGYYPIIYANDNWLANKLDMSLMNYPVWVARYSARPDYANPVMWQAT
STGSVNGISGNVDIDFQYKDFSSVIPANTWRTVKGQRYYYSNYAKLRNGWAQDGDSWYYM
GSDGLASKGWILESGKHYFLDETTGKMVTGWLSENGKWYYLDGSGALATGWINDGGTWYY
SDSQGIMQTGWLDEGGSRYFLRGSGAMATGWRQMDGAWYYFEGSGSMARGMIQVNGVSYY
LDPATGKMAADTQVTVDGTVYVADGSGALSLSVQETGTADGESQTAVPAGPGMSSQTAVQ
SGPGESGQAAGVLIVPVQ

Enzyme Prediction     

No EC number prediction in MGYG000003593_02151.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	139	308	2.1e-47	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	6.74e-82	136	318	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.
NF033838	PspC_subgroup_1	1.06e-52	326	521	484	673	pneumococcal surface protein PspC, choline-binding form. The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
NF033930	pneumo_PspA	1.26e-52	326	512	441	624	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.
COG5263	COG5263	5.50e-40	338	505	142	310	Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism].
cd00599	GH25_muramidase	5.22e-38	137	315	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQR03194.1	5.18e-146	15	525	6	489
ANU47907.1	5.18e-146	15	525	6	489
QRP37172.1	2.32e-142	15	389	6	353
ASN98018.1	2.32e-142	15	389	6	353
QIX91481.1	2.47e-142	15	389	6	353

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	5.24e-17	137	315	21	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	3.06e-16	137	315	21	205	X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
2WW5_A	6.23e-14	136	318	269	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	1.46e-13	136	318	269	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
5A6S_A	2.58e-13	135	325	21	209	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
P76421	1.22e-14	138	315	69	252	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	1.64e-14	138	315	69	252	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	1.64e-14	138	315	69	252	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P26836	3.93e-13	127	315	2	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	1.17e-09	137	315	2	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000398	0.998745	0.000259	0.000220	0.000198	0.000162

TMHMM  Annotations     

start	end
21	43