CAZyme Information: MGYG000000248_00827

Basic Information

• Species: Weissella cibaria
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Weissella; Weissella cibaria
• CAZyme ID: MGYG000000248_00827
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
276		27765.66	4.511

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000248	2506217	Isolate	China	Asia

• Gene Location: Start: 225900; End: 226730 Strand: +

Full Sequence      

MEKVSVNKSIKGMALTTAAVAAAVLPFMHTNAASADDSAKGWRSKTVDEVRTTVKDAGRV
YVVQSGDTLSTIAAATDRSVDDIAKQNDITNANMIEVGQKLDLVSEAPATSVAASVAPSE
ASLAPAASSVAPASSVASQASSASSEAPVATSAATSTAPVATVSPASADATLNALNALRA
SAGLPQLVWDDGLAASATARAASMSQTGVDQAHYSGAVANEVVAAGFGAGQDVISAWFNE
TNMTGVPNGHHDWEMNGSFTRVGFGYVNGWIVGHAE

Enzyme Prediction     

No EC number prediction in MGYG000000248_00827.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00118	LysM	4.92e-12	59	101	1	43	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.
smart00257	LysM	8.47e-11	61	103	2	44	Lysin motif.
pfam00188	CAP	4.88e-10	172	269	1	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.
cd05379	CAP_bacterial	1.05e-09	168	269	1	108	Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain proteins. Little is known about bacterial and archaeal members of the CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain family. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Studies of eukaryotic proteins show that CAP domains have several functions, including the binding of cholesterol, lipids and heparan sulfate. This group includes Borrelia burgdorferi outer surface protein BB0689, which does not bind to cholesterol, lipids, or heparan sulfate, and whose function is unknown.
pfam01476	LysM	1.17e-09	61	101	1	40	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMU89145.1	1.58e-162	1	276	1	276
AWF96336.1	1.58e-162	1	276	1	276
ASS52118.1	4.51e-162	1	276	1	276
APS26953.1	4.51e-162	1	276	1	276
APU62350.1	4.51e-162	1	276	1	276

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000403	0.998771	0.000202	0.000235	0.000188	0.000156

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000248_00827.