CAZyme Information: MGYG000001497_01218

Basic Information

• Species: Clostridium_F niameyense
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_F; Clostridium_F niameyense
• CAZyme ID: MGYG000001497_01218
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
312	MGYG000001497_6|CGC8	34562.45	8.6002

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001497	2542824	Isolate	not provided	not provided

• Gene Location: Start: 1043004; End: 1043942 Strand: +

Full Sequence      

MGLVSKECIDFVKKFEGFYPKPYYDIVGVKTLGYGMTGKEIEGLSSVTEAQASTMLENLL
NNKYAAPIKRDLDNRGISLKQNEFDALVSMAYNVGVGGVLDSTLYRNICNGVRDKSTITS
NFEMWSMAGGKQVYGLLRRRREEAAMFFGDGNVATDNSTGGSYYNVKEVQEMLIKIGYPC
GNYGADGSWGNSTKAAVECFQRDCNLKVDGWVGGDTYRKIKEEYNKKLAINKEVKQKVKE
EYDMDKIILYYGDMDALSALLVGQKNSCPVMKESDFEKSGLKAKKVIRIGGPNGDATGKD
RFKTFKAAANLV

Enzyme Prediction     

No EC number prediction in MGYG000001497_01218.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	4	143	2e-36	0.9927007299270073

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	1.11e-43	8	148	1	136	endolysin and autolysin. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
COG3772	RrrD	2.05e-29	1	150	4	150	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16901	lyz_P1	2.58e-23	4	146	2	138	P1 lysozyme Lyz-like proteins. Enterobacteria phage P1 lysozyme Lyz is secreted to the Escherichia coli periplasm where it is membrane bound and inactive. Activation involves the release from the membrane, an intramolecular thiol-disulfide isomerization and extensive structural rearrangement of the N-terminal region. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
cd16900	endolysin_R21-like	9.59e-21	11	146	11	140	endolysin R21-like proteins. Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
pfam01471	PG_binding_1	7.18e-12	165	220	4	57	Putative peptidoglycan binding domain. This domain is composed of three alpha helices. This domain is found at the N or C-terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QXE20011.1	8.28e-73	3	168	4	169
AUM96824.1	9.08e-73	1	138	1	138
AVQ42412.1	9.08e-73	1	138	1	138
AVQ38952.1	9.08e-73	1	138	1	138
AIY79897.1	4.14e-66	3	153	108	261

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ET6_A	2.81e-17	5	147	53	193	ChainA, Lysozyme [Acinetobacter baumannii]
3HDF_A	8.81e-13	16	143	10	131	ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
4ZPU_A	1.33e-12	16	143	35	156	Thestructure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_B The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_C The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_D The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12]
3HDE_A	1.50e-12	16	143	35	156	ChainA, Lysozyme [Enterobacteria phage P21],3HDE_B Chain B, Lysozyme [Enterobacteria phage P21],3HDE_C Chain C, Lysozyme [Enterobacteria phage P21],3HDE_D Chain D, Lysozyme [Enterobacteria phage P21]
7M5I_A	2.55e-12	4	147	9	153	ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P11187	6.85e-17	4	177	3	168	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
P07540	2.44e-16	4	177	3	168	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
Q37896	8.43e-15	4	147	3	142	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
O80292	5.23e-14	16	143	37	158	SAR-endolysin OS=Bacteriophage PS119 OX=83128 GN=19 PE=3 SV=1
O80288	9.25e-13	16	143	37	158	SAR-endolysin OS=Bacteriophage PS34 OX=83127 GN=19 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
1.000069	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001497_01218.