CAZyme Information: MGYG000001700_00864

Basic Information

• Species: Citrobacter_A sedlakii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter_A; Citrobacter_A sedlakii
• CAZyme ID: MGYG000001700_00864
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1027		114785.93	6.6037

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001700	4631466	Isolate	not provided	not provided

• Gene Location: Start: 895772; End: 898855 Strand: -

Full Sequence      

MTVKIPKISYPVPSNKNGHAFPSTEELLSKLGSESSGLYLVGSQGMWHGGIHITDATIPW
CALSTDSKPENDYCREPYKGEQFIRCMADGEIVAWRVCKDYESSAIEWRGEKLFLSNSFV
LVKHYIQPGDSEESGLTFFTLYMNLAPYIAYKQKGNQSDRKVAGVQRYYSSVDDMLAGRA
AGKLNKDTPVTLGDNIVTRSRDRRQFTEVTITSETKNVAGDTLAAGTKVWTVSDRGSLKA
VASAPVPSWWAKCSPAYTTQPEGVTYCTSRTNWKYYLSSEDVLQDKKAGSLTPDFPLSYE
PGNAAQQVTRPGKKPGDAARIFSLVTLGRDKDKLKKGDRVWVVSDGDSLTPVAPSASGSE
PVFNDVYVPSEPVPVSAGDSLGHMGFYQLPEENGKRSRYQVHIECLSMDDMEKFITNPGR
AGEDAPVYLTWKTDAPLFDKSDTGITAGGRKTKSSGILTLAKVPGVDAEGNTLSSNKDAA
YYQIRPEGGWLAATSVQKVSQYALGELGFVTLNKTPESFDLIDGIKQPNNVVKGILEQLY
KAAEEEIRTTHALNKYNYKRLLALIDSNQDGHYSEQEYLQAIHNVSYRDRLYRIIAKHAS
EWFYGKDDPLWKNYLDPLTRDAPLWKTYLEAFLDKMTWMKAVSEKGVPLGPEPWHMHPVV
FLDAVSNDQKLIIFPLKVKPKNDINGVWKNYYWAASSSDSNASQAIFGRNRSGGSRKHAA
RDLYTEPSTEIVAVCDGTVKSITAYYMGTSQITIEHKTNDNRRFFARYGEVDPNSITVNV
GDKVSQGSIIAKTGLMISPETNRHPSIIAGQTVYMLHFEYYPGNESESPPNNTLDLPYRR
RNDLRDPLEILREGYENTFSENVKNGNRIDINQLQVSDEGKAFIKGWESFKSKPYNDSEG
YCTIGYGHLIARRKCEDIVLSDEFKDGITRARADELFEERLPTYVNELKSSVTVNLYQYE
FDALVSLLFNLGSLRKAPLLKSKLNSGDYAGAADEFLDITNDGTTGLVIRRRKEWGLFNN
NIYDSSH

Enzyme Prediction     

No EC number prediction in MGYG000001700_00864.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	876	1014	5.2e-34	0.9927007299270073

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	4.36e-46	880	1019	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	9.37e-26	875	1023	6	152	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16901	lyz_P1	2.31e-18	875	1014	1	135	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	1.50e-13	882	1015	10	138	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.
cd12797	M23_peptidase	1.86e-12	718	819	1	84	M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins. This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHP31272.1	0.0	1	1027	1	1027
QFU48309.1	0.0	1	1027	1	1027
QDW12774.1	0.0	1	1027	1	1027
ABX22482.1	0.0	1	1027	1	1032
AGN85714.1	0.0	5	1027	4	1016

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ET6_A	7.49e-15	876	1018	52	193	ChainA, Lysozyme [Acinetobacter baumannii]
2ANV_A	9.63e-12	874	1018	2	144	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]
7M5I_A	3.89e-08	874	1023	7	158	ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]
6H9D_A	3.10e-06	875	1018	5	146	ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9T1T5	5.13e-13	874	1018	1	143	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
Q37896	3.85e-12	874	1018	1	142	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
P09963	2.84e-11	874	1018	2	144	Endolysin OS=Salmonella phage P22 OX=10754 GN=19 PE=1 SV=1
P07540	1.28e-10	874	1019	1	143	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
P11187	1.28e-10	874	1019	1	143	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
1.000057	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001700_00864.