CAZyme Information: MGYG000001705_01264

Basic Information

• Species: Citrobacter portucalensis
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter portucalensis
• CAZyme ID: MGYG000001705_01264
• CAZy Family: GH24
• CAZyme Description: Lysozyme RrrD

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
182		19815.82	8.8747

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001705	4942442	Isolate	not provided	not provided

• Gene Location: Start: 1350171; End: 1350719 Strand: +

Full Sequence      

MAMPQKLRNKLSATVVGLILAGASAPVILDQFLDEKEGNSTTAYKDGSGIWTICRGATMV
DGKPVVQGMKLSAEKCAKVNSIERDKALAWVEQNIKVPLTEPQKAGIASFCPYNIGPGKC
FPSTFYKRINAGDREGACEAIRWWIKDGGRDCRLTKGQKNGCYGQVERRDQESALACWGI
GQ

Enzyme Prediction     

EC	3.2.1.17

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	31	172	4.8e-39	0.948905109489051

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3772	RrrD	6.05e-56	19	180	1	151	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16900	endolysin_R21-like	5.93e-55	21	175	1	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.
pfam00959	Phage_lysozyme	5.51e-29	50	170	1	107	Phage lysozyme. This family includes lambda phage lysozyme and E. coli endolysin.
cd00737	lyz_endolysin_autolysin	3.51e-25	31	150	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	2.11e-15	37	175	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYY47443.1	5.65e-130	1	182	1	182
QRQ75851.1	8.03e-130	1	182	1	182
BBV35641.1	3.27e-129	1	182	1	182
BBV30628.1	3.27e-129	1	182	1	182
QFI10828.1	4.65e-129	1	182	1	182

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3HDE_A	1.21e-21	3	179	1	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	3.05e-21	3	179	1	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]
7M5I_A	4.22e-21	37	175	21	152	ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]
3HDF_A	1.70e-18	34	179	7	138	ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
6ET6_A	9.30e-15	37	175	64	192	ChainA, Lysozyme [Acinetobacter baumannii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O64362	6.07e-116	8	182	4	178	SAR-endolysin OS=Escherichia phage N15 OX=40631 GN=54 PE=3 SV=1
P68921	1.04e-109	3	180	1	175	SAR-endolysin OS=Enterobacteria phage VT2-Sa OX=97081 GN=R PE=3 SV=1
P68920	1.04e-109	3	180	1	175	SAR-endolysin OS=Escherichia phage 933W OX=10730 GN=R PE=3 SV=1
Q9ZXB7	2.01e-107	3	180	1	175	SAR-endolysin OS=Enterobacteria phage H19B OX=69932 GN=R PE=3 SV=1
P76159	7.85e-105	3	182	1	177	Probable prophage lysozyme OS=Escherichia coli (strain K12) OX=83333 GN=rrrQ 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
0.565440	0.425911	0.006767	0.000824	0.000375	0.000675

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001705_01264.