CAZyme Information: MGYG000002351_05491

Basic Information

• Species: Klebsiella_A michiganensis
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella_A; Klebsiella_A michiganensis
• CAZyme ID: MGYG000002351_05491
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
142		16071.37	6.949

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002351	6684898	Isolate	United States	North America

• Gene Location: Start: 5799766; End: 5800194 Strand: +

Full Sequence      

MSPTIPPLSLHGLEFIKRMQGLALAPYRDESGLRVIGYGHVLNDYESFPHFTREIAETLL
IVDLLQCQRELKRRLQVTLNQAQYDALVSLAFSCGAASPALDTVLTHLNHQRFADALSAW
ENICSGREQRREECAKFKTRAD

Enzyme Prediction     

No EC number prediction in MGYG000002351_05491.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	9	132	3.5e-24	0.9708029197080292

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	9.55e-30	12	137	1	135	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	1.88e-17	8	133	7	142	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16901	lyz_P1	1.30e-12	8	133	2	134	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	3.28e-08	35	128	3	98	Phage lysozyme. This family includes lambda phage lysozyme and E. coli endolysin.
cd16900	endolysin_R21-like	4.71e-08	8	133	4	136	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AID92777.1	2.49e-100	1	142	1	142
AUV89846.1	2.49e-100	1	142	1	142
AVE80185.1	2.49e-100	1	142	1	142
AUV97887.1	2.49e-100	1	142	1	142
AOV14575.1	2.49e-100	1	142	1	142

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2ANV_A	1.94e-13	8	121	4	124	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]
4EVX_A	6.74e-12	13	118	12	103	Crystalstructure of putative phage endolysin from S. enterica [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],4EVX_B Crystal structure of putative phage endolysin from S. enterica [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
6ET6_A	3.17e-06	12	132	56	187	ChainA, Lysozyme [Acinetobacter baumannii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P09963	5.38e-13	8	121	4	124	Endolysin OS=Salmonella phage P22 OX=10754 GN=19 PE=1 SV=1
Q9T1T5	2.94e-12	8	116	3	110	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
Q37896	2.64e-09	8	133	3	137	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
P07540	4.48e-08	8	114	3	111	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
P11187	4.48e-08	8	114	3	111	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 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
1.000084	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002351_05491.