CAZyme Information: MGYG000001624_02764

Basic Information

• Species: Proteus cibarius
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Proteus; Proteus cibarius
• CAZyme ID: MGYG000001624_02764
• CAZy Family: GH24
• CAZyme Description: Lysozyme RrrD

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
156		17138.68	8.7752

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001624	3841359	MAG	China	Asia

• Gene Location: Start: 4188; End: 4658 Strand: +

Full Sequence      

MSLKQKIAALTTAGATAIALVVIAHFEGVRYEPYRDVAGVLTVCYGHTGKDIIQGKRYTQ
QECDALLQSDFINIQQQVDALIKVPLDDYTKAALYSFAFNVGTTAFARSTLLRKLNAGDR
AGACEEIKRWVYAGGKVWRGLVSRREAESALCYGNL

Enzyme Prediction     

No EC number prediction in MGYG000001624_02764.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	19	148	2.7e-51	0.9635036496350365

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd16900	endolysin_R21-like	4.90e-82	21	152	10	141	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.
cd00737	lyz_endolysin_autolysin	1.98e-58	23	151	5	134	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	2.23e-52	23	156	15	151	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16901	lyz_P1	1.41e-43	21	152	8	139	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.
pfam00959	Phage_lysozyme	1.50e-26	40	146	1	107	Phage lysozyme. This family includes lambda phage lysozyme and E. coli endolysin.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIF93726.1	6.63e-105	1	156	1	156
QGM68148.1	2.70e-104	1	156	1	156
QWV40641.1	2.70e-104	1	156	1	156
QUY07517.1	2.70e-104	1	156	1	156
QSI22805.1	2.70e-104	1	156	1	156

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4ZPU_A	4.36e-53	2	152	4	160	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	1.83e-52	2	152	4	160	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]
3HDF_A	3.21e-50	27	152	10	135	ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
6ET6_A	3.41e-24	23	151	60	192	ChainA, Lysozyme [Acinetobacter baumannii]
2ANV_A	7.40e-18	27	151	16	143	ChainA, Lysozyme [Lederbergvirus P22],2ANV_B Chain B, Lysozyme [Lederbergvirus P22],2ANX_A Chain A, Lysozyme [Lederbergvirus P22],2ANX_B Chain B, Lysozyme [Lederbergvirus P22]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O80292	4.21e-56	2	152	6	162	SAR-endolysin OS=Bacteriophage PS119 OX=83128 GN=19 PE=3 SV=1
O80288	1.31e-52	2	152	6	162	SAR-endolysin OS=Bacteriophage PS34 OX=83127 GN=19 PE=3 SV=1
P78285	1.75e-52	2	152	4	160	Lysozyme RrrD OS=Escherichia coli (strain K12) OX=83333 GN=rrrD PE=1 SV=1
P10439	1.00e-51	2	152	4	160	SAR-endolysin OS=Enterobacteria phage PA-2 OX=10738 GN=15 PE=3 SV=1
P27359	1.16e-50	2	152	4	160	SAR-endolysin OS=Enterobacteria phage P21 OX=10711 GN=R PE=1 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
0.992549	0.007402	0.000025	0.000014	0.000010	0.000023

TMHMM  Annotations     

start	end
7	29