CAZyme Information: MGYG000001336_02176

Basic Information

• Species: Limosilactobacillus reuteri_E
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Limosilactobacillus; Limosilactobacillus reuteri_E
• CAZyme ID: MGYG000001336_02176
• CAZy Family: GH23
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
822		90990.64	4.869

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001336	2316838	Isolate	not provided	not provided

• Gene Location: Start: 2129773; End: 2132241 Strand: +

Full Sequence      

MWPTFKPSWEKNSTYQVTFSVFNYGDPLYDELDVESSFFLDGQEYIVKNCVENFDTNTKD
ITAWHVYNEINRIYKRSDLTLNKPTDDNQNQDVSYSVEDILKAWIDGNNLGFSYEVHGNF
DKQSTSKFDSGSGKDMLSKILELWPNAIVFPNNKNIRVYSEDEFYKDNGRIIDFPHDAKS
VKTTRDSQSIINEIRCVGGKHEVQHTVYTGTGGANASGPTEPVNGDWTPVIQYAASFYGI
KPTDQQLNVLRAQIHLESGGREDAQQPGADPDGDGSGPALGLLQFKQRTFNYYCREPYTN
VKHGFDALIAFFNIPNALGQINGVTGWSPHGAPITKDKLIITPPNPWGWPFPNVGEGHFS
LGQTFGTHPQDGVGRTNGFHDGLDFGSVDHPGSEVHAVHGGKVQDIGYIAGLENYVTVVS
NDYLICYQEAFSSRSNIKVSVGQDIKTGDVIGIRDTSHVHIGITKQKNLMVALRSAWSDD
GTWLDPLQIIRDGIGGKDNNDAVGNDTTTESQEEYYFQPFIVKDQKSIDEWGEHPGPDLV
DERFQDAEAMRKYALTTLKPDPDLNLEVTLNGNEFVPEANEIVRVIAGKKYSGSYKTVGF
TLAPAKGQDNTISLNNTKTTILDYQNQRTKRLEEALDEQRQRMEGLAGSLDQQSKSLTQV
VNDKKETDKSMEAVDQNIYWMQNGQHNLVTTMTGGTASSEKYNDSPVIEVEQGALRSNEF
NLNGVSSISSRLIAKLNATDNSISATTYVEFLKSDGSSAGKSNIVYIVNNGAWQSAGTVN
IKIPAGTTKGRLVFDVSGSGKAYVSRAQVNLGYRVTDWGSLK

Enzyme Prediction     

No EC number prediction in MGYG000001336_02176.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd12797	M23_peptidase	4.90e-11	380	463	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.
pfam06605	Prophage_tail	9.30e-11	96	198	19	121	Prophage endopeptidase tail. This family is of prophage tail proteins that are probably acting as endopeptidases.
pfam18994	Prophage_tailD1	2.33e-10	4	65	19	84	Prophage endopeptidase tail N-terminal domain. This domain represents the N-terminal domain of prophage tail proteins that are probably acting as endopeptidases. This domain has a RIFT related fold.
pfam01551	Peptidase_M23	5.89e-10	378	466	1	90	Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.
pfam06605	Prophage_tail	9.66e-08	485	627	109	250	Prophage endopeptidase tail. This family is of prophage tail proteins that are probably acting as endopeptidases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEI58319.1	0.0	1	822	1	822
QDK48758.1	0.0	1	822	17	839
QLQ62892.1	0.0	1	822	17	839
AMY13353.1	0.0	1	822	17	839
QLL75900.1	0.0	1	822	17	839

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5GT1_A	8.19e-61	347	494	25	171	ChainA, Choline binding protein A [Ligilactobacillus salivarius str. Ren]

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000066	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001336_02176.