CAZyme Information: MGYG000001393_01880

Basic Information

• Species: Hafnia paralvei
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Hafnia; Hafnia paralvei
• CAZyme ID: MGYG000001393_01880
• CAZy Family: GH24
• CAZyme Description: Lysozyme RrrD

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
175		19230.2	9.3041

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001393	4880992	Isolate	not provided	not provided

• Gene Location: Start: 8456; End: 8983 Strand: -

Full Sequence      

MGTKTKLSAAVLALILGGATADKILDQFLDEKEGVRTIAYQDGRGIWSICRGLTRIEGKP
VTQGLKLSYSQCKRYDALERDKAIAWVRRNVTVPLSEPAIAGIASFCPYNIGPAKCFPST
FYKKLNAGDRIGACAEIKRWIFDGGRDCRIKANNCAGQPVRRGQESELTCWGIDQ

Enzyme Prediction     

EC	3.2.1.17

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	26	164	2.3e-31	0.948905109489051

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3772	RrrD	1.06e-43	15	174	1	152	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16900	endolysin_R21-like	1.46e-43	17	170	1	142	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	1.12e-23	27	146	3	119	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.
cd16901	lyz_P1	6.48e-16	33	168	14	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.
pfam00959	Phage_lysozyme	2.10e-15	46	162	1	106	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
QQE41734.1	2.33e-130	1	175	1	175
QQE41783.1	3.06e-126	1	175	1	175
QIP56296.1	4.18e-124	1	175	1	175
AMH20069.1	2.50e-123	1	175	1	176
QDW32871.1	2.20e-92	4	175	5	176

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3HDE_A	1.38e-17	7	172	5	163	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]
4ZPU_A	1.72e-17	7	172	5	163	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]
3HDF_A	2.16e-17	30	172	7	138	ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
7M5I_A	3.43e-17	33	140	21	126	ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]
6ET6_A	1.58e-12	7	146	38	177	ChainA, Lysozyme [Acinetobacter baumannii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P68920	1.69e-88	7	175	9	177	SAR-endolysin OS=Escherichia phage 933W OX=10730 GN=R PE=3 SV=1
P68921	1.69e-88	7	175	9	177	SAR-endolysin OS=Enterobacteria phage VT2-Sa OX=97081 GN=R PE=3 SV=1
P76159	1.96e-87	1	175	1	177	Probable prophage lysozyme OS=Escherichia coli (strain K12) OX=83333 GN=rrrQ PE=3 SV=1
O64362	1.94e-85	1	175	1	178	SAR-endolysin OS=Escherichia phage N15 OX=40631 GN=54 PE=3 SV=1
Q9ZXB7	3.78e-85	7	175	9	177	SAR-endolysin OS=Enterobacteria phage H19B OX=69932 GN=R PE=3 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
0.000316	0.999088	0.000151	0.000146	0.000134	0.000131

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001393_01880.