CAZyme Information: MGYG000001659_00064

Basic Information

• Species: Paraprevotella sp900760455
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; Paraprevotella sp900760455
• CAZyme ID: MGYG000001659_00064
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
514		56781.26	5.5491

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001659	3410285	MAG	United States	North America

• Gene Location: Start: 69942; End: 71486 Strand: -

Full Sequence      

MSKNQEYAERYAEYSIEQMRRYGIPASVTLAQGILESSNGQSRLALNENNHFGIKATPEW
IAQGGRYGLYTDDKPNEKFCSYDSVGDSYEHHSRFLKENGRYARCFTLAPDDYKGWTLAL
EQAGYATGGHYAASLQQIIERNGLQEYDRQVMREMEAQGKQFGVEENPLRESENAKEYSF
PVEREEFLFITSPFGMRQDPIDGTKRMHTGIDIRCKSDAVLATEKGGKVIAVNGKGNTPG
GKSVTVEYVRENGSKVQCTYMHLGDIAVKVGDTVQAGQRLGTSGNTGTRTTGEHLHFSVR
QIHADGTQRDIDPAAYLAEIAQKGNIRQQALHNGNDLLAKYRDAESVKENQPLSPDAWMK
KLLSSEDSGVGMSGCNDPIVEMAMTAFTSLMLLAAQIDNRNAEEQRAAISAAMDSRRIDL
KSLVTGMKACELVIGENGRATLRADNGSVEVSHELTSAELSRLSATLNNDTLSEETKRLR
VAGVLNTVLLSETASRNFEQGMSEQQGQTENLKR

Enzyme Prediction     

No EC number prediction in MGYG000001659_00064.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH73	12	144	5.2e-32	0.984375

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1705	FlgJ	2.52e-28	2	149	41	189	Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility].
NF038016	sporang_Gsm	1.54e-27	4	148	160	312	sporangiospore maturation cell wall hydrolase GsmA. The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.
COG0739	NlpD	1.68e-25	171	329	127	276	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01832	Glucosaminidase	7.04e-23	12	92	1	77	Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase. This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyze peptidoglycan.
cd12797	M23_peptidase	1.94e-22	208	299	1	85	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
QUR43544.1	3.94e-306	2	514	3	515
QCQ31411.1	3.94e-306	2	514	3	515
QDM08698.1	3.94e-306	2	514	3	515
QCQ49986.1	1.86e-304	2	514	3	515
QLK81501.1	1.53e-303	2	514	3	515

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KQB_A	5.07e-11	190	320	13	135	Identificationand structural characterization of LytU [Staphylococcus aureus],5KQC_A Identification and structural characterization of LytU [Staphylococcus aureus]
5DN5_A	6.99e-09	23	141	22	147	Structureof a C-terminally truncated glycoside hydrolase domain from Salmonella typhimurium FlgJ [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],5DN5_B Structure of a C-terminally truncated glycoside hydrolase domain from Salmonella typhimurium FlgJ [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],5DN5_C Structure of a C-terminally truncated glycoside hydrolase domain from Salmonella typhimurium FlgJ [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
5DN4_A	9.22e-09	23	141	22	147	Structureof the glycoside hydrolase domain from Salmonella typhimurium FlgJ [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
5J1L_A	7.75e-08	185	300	42	152	Crystalstructure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1L_C Crystal structure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1M_A Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695],5J1M_C Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695]
4QP5_A	1.02e-07	194	317	19	136	Catalyticdomain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the presence of phosphate [Staphylococcus simulans bv. staphylolyticus],4QP5_B Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the presence of phosphate [Staphylococcus simulans bv. staphylolyticus],4QPB_A Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the absence of phosphate [Staphylococcus simulans],4QPB_B Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the absence of phosphate [Staphylococcus simulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O32083	1.30e-09	21	148	65	198	Exo-glucosaminidase LytG OS=Bacillus subtilis (strain 168) OX=224308 GN=lytG PE=1 SV=1
Q8K9M4	6.58e-09	190	342	272	415	Uncharacterized metalloprotease BUsg_310 OS=Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) OX=198804 GN=BUsg_310 PE=3 SV=1
P44693	4.12e-08	180	347	321	472	Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
P15931	2.35e-07	23	141	171	296	Peptidoglycan hydrolase FlgJ OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=flgJ PE=1 SV=1
P58231	1.73e-06	23	141	168	293	Peptidoglycan hydrolase FlgJ OS=Escherichia coli O157:H7 OX=83334 GN=flgJ 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
1.000036	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001659_00064.