CAZyme Information: MGYG000000096_01067

Basic Information

• Species: Leuconostoc pseudomesenteroides
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Leuconostoc; Leuconostoc pseudomesenteroides
• CAZyme ID: MGYG000000096_01067
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
383		38195.56	4.6547

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000096	2296803	Isolate	Canada	North America

• Gene Location: Start: 363550; End: 364701 Strand: +

Full Sequence      

MSNNIKKTLLATAAGAAAVVGGHAAASANTVEVKSGDTLSAIAAANNTTVAELAKNNNIS
NENLILAGTSLEVSTSTQSVSGLSSDGSSYTVQSGDTLSKIAEKTGVSVSTLTSLNGVSN
QNLILTGQELSLKTATSAASSAATVATVAASSVASTASSAAVDTSNLKYIAAADTNNDGF
MSLSEYNTYVANGGSTTSSAATTTTSAATSSSASSEAITYIAAADTNKDGYMTMAEYNAY
KANGGSTATTTTQTATAQTTQTSTSTSASTSTGSTTADATINAWNAMRAKMGLNPIRISS
ALTAQAQGRAQAIATSSNWFGTHASSGTPEVVANGFGAGASVINAWYYETGMVNGGHTAF
IINPNFTEAGVGYYNGWIVINAQ

Enzyme Prediction     

No EC number prediction in MGYG000000096_01067.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10783	mltD	4.35e-12	27	132	342	446	membrane-bound lytic murein transglycosylase D; Provisional
pfam01476	LysM	9.43e-11	90	133	1	43	LysM domain. The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
cd00118	LysM	1.41e-10	89	132	2	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
pfam00188	CAP	1.90e-10	285	376	5	105	Cysteine-rich secretory protein family. This is a large family of cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins (CAP) that are found in a wide range of organisms, including prokaryotes and non-vertebrate eukaryotes, The nine subfamilies of the mammalian CAP 'super'family include: the human glioma pathogenesis-related 1 (GLIPR1), Golgi associated pathogenesis related-1 (GAPR1) proteins, peptidase inhibitor 15 (PI15), peptidase inhibitor 16 (PI16), cysteine-rich secretory proteins (CRISPs), CRISP LCCL domain containing 1 (CRISPLD1), CRISP LCCL domain containing 2 (CRISPLD2), mannose receptor like and the R3H domain containing like proteins. Members are most often secreted and have an extracellular endocrine or paracrine function and are involved in processes including the regulation of extracellular matrix and branching morphogenesis, potentially as either proteases or protease inhibitors; in ion channel regulation in fertility; as tumor suppressor or pro-oncogenic genes in tissues including the prostate; and in cell-cell adhesion during fertilisation. The overall protein structural conservation within the CAP 'super'family results in fundamentally similar functions for the CAP domain in all members, yet the diversity outside of this core region dramatically alters the target specificity and, thus, the biological consequences. The Ca++-chelating function would fit with the various signalling processes (e.g. the CRISP proteins) that members of this family are involved in, and also the sequence and structural evidence of a conserved pocket containing two histidines and a glutamate. It also may explain how the cysteine-rich venom protein helothermine blocks the Ca++ transporting ryanodine receptors.
cd00118	LysM	4.71e-10	30	73	2	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQB27187.1	3.59e-172	1	383	1	381
QEA41112.1	3.59e-172	1	383	1	381
QSB51658.1	1.56e-171	1	383	1	383
QQB01765.1	5.60e-163	1	383	1	386
API71422.1	9.55e-124	1	383	1	436

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2MKX_A	7.62e-06	90	133	7	49	Solutionstructure of LysM the peptidoglycan binding domain of autolysin AtlA from Enterococcus faecalis [Enterococcus faecalis V583]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q49UX4	4.08e-12	27	141	25	138	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1
P37710	1.65e-08	33	144	569	686	Autolysin OS=Enterococcus faecalis (strain ATCC 700802 / V583) OX=226185 GN=EF_0799 PE=1 SV=2
O34669	9.02e-08	5	142	1	131	Cell wall-binding protein YocH OS=Bacillus subtilis (strain 168) OX=224308 GN=yocH PE=1 SV=1
P11187	1.75e-07	32	132	164	257	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
P07540	1.75e-07	32	132	164	257	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000362	0.998929	0.000177	0.000177	0.000166	0.000146

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000096_01067.