CAZyme Information: MGYG000004876_00514

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides
• CAZyme ID: MGYG000004876_00514
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
514		56869.39	5.6977

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004876	4781463	MAG	China	Asia

• Gene Location: Start: 97608; End: 99152 Strand: +

Full Sequence      

MSKNQEYAERYAEYSMEQMRRYGIPASVTLAQGILESSNGQSRLALNENNHFGIKATPEW
IAQGGRYGLYTDDKPNEKFCSYDNVGDSYEHHSRFLKENGRYARCFTLAPDDYKGWTLAL
EQAGYATGGHYAASLQQIIERNGLQEYDRQVMREMEAQGKQFGVEENPLRESENAKEYSF
PVEREEFLFITSPFGMRQDPIDGTKRMHTGIDIRCKSDAVLATEKGGKVISVNGKGNTPG
GKSVTVEYVRENGSKVQCTYMHLGDIAVKVGDTVQAGQRLGTSGNTGTRTTGEHLHFGVR
QIHADGTQRDIDPAAYLAKIAQKGNIRQQALHNGNDLLAKYRDAESVKENQPLSPDAWMK
KLLSSEDSGVGMSGCNDPIVEMAMTAFTSLMLLAAQIDNRNEEEQRAAISAAMDSRRIDL
KSLVTGMKACELVIGENGRATLRADNGSVEVSHELTSAELSRLSATLNNDTLSEETKRLR
VAGVLNTVLLSETASRNFEQGMSEQQGQTENLKR

Enzyme Prediction     

No EC number prediction in MGYG000004876_00514.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH73	13	144	2.2e-31	0.9765625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
NF038016	sporang_Gsm	5.90e-28	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.
COG1705	FlgJ	8.25e-28	20	149	59	189	Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility].
COG0739	NlpD	5.61e-27	171	329	127	276	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
cd12797	M23_peptidase	1.83e-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.
pfam01832	Glucosaminidase	3.72e-22	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUR43544.1	9.70e-307	2	514	3	515
QCQ31411.1	9.70e-307	2	514	3	515
QDM08698.1	9.70e-307	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	1.47e-11	190	312	13	133	Identificationand structural characterization of LytU [Staphylococcus aureus],5KQC_A Identification and structural characterization of LytU [Staphylococcus aureus]
6JMX_A	1.20e-08	189	319	130	248	ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni]
5DN5_A	4.39e-08	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]
4QP5_A	5.48e-08	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]
5DN4_A	5.73e-08	23	141	22	147	Structureof the glycoside hydrolase domain from Salmonella typhimurium FlgJ [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O32083	4.20e-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	2.35e-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	1.32e-06	23	141	171	296	Peptidoglycan hydrolase FlgJ OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=flgJ PE=1 SV=1
P10547	3.72e-06	194	317	265	382	Lysostaphin OS=Staphylococcus simulans OX=1286 GN=lss PE=1 SV=2

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
1.000038	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004876_00514.