dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Bacillus sonorensis

Lineage

Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus sonorensis

CAZyme ID

MGYG000000227_02562

CAZy Family

CBM63

CAZyme Description

Expansin-YoaJ

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
232	MGYG000000227_4\|CGC3	25641.69	9.9673

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000227	4782975	Isolate	China	Asia

Gene Location

Start: 392508; End: 393206 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000000227_02562.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CBM63	139	214	1e-39	0.9743589743589743

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4305	YoaJ	9.69e-147	1	232	1	232	Peptidoglycan-binding domain, expansin [Cell wall/membrane/envelope biogenesis].
cd22272	DPBB_EXLX1-like	3.39e-60	29	129	1	101	N-terminal double-psi beta-barrel fold domain of bacterial expansins similar to Bacillus subtilis EXLX1. This subfamily is composed of bacterial expansins including Bacillus subtilis EXLX1, also called expansin-YoaJ. Similar to plant expansins, EXLX1 contains an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. It strongly binds to crystalline cellulose via D2, and weakly binds soluble cellooligosaccharides. Bacterial expansins, which are present in some plant pathogens, have the ability to loosen plant cell walls, but with weaker activity compared to plant expansins. They may have a role in plant-bacterial interactions. This model represents the N-terminal domain of EXLX1 and similar bacterial expansins, which adopts a double-psi beta-barrel (DPBB) fold.
cd22191	DPBB_RlpA_EXP_N-like	3.97e-18	31	129	1	94	double-psi beta-barrel fold of RlpA, N-terminal domain of expansins, and similar domains. The double-psi beta-barrel (DPBB) fold is found in a divergent group of proteins, including endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A), EG45-like domain containing proteins, kiwellins, Streptomyces papain inhibitor (SPI), and the N-terminal domain of plant and bacterial expansins. RlpA may work in tandem with amidases to degrade peptidoglycan (PG) in the division septum and lateral wall to facilitate daughter cell separation. An EG45-like domain containing protein from Arabidopsis thaliana, called plant natriuretic peptide A (AtPNP-A), functions in cell volume regulation. Kiwellin proteins comprise a widespread family of plant-defense proteins that target pathogenic bacterial/fungal effectors that down-regulate plant defense responses. SPI is a stress protein produced under hyperthermal stress conditions that serves as a glutamine and lysine donor substrate for microbial transglutaminase (MTG, EC 2.3.2.13) from Streptomycetes. Some expansin family proteins display cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs.
cd22271	DPBB_EXP_N-like	2.83e-11	35	130	13	115	N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains. The plant expansin family consists of four subfamilies, alpha-expansin (EXPA), beta-expansin (EXPB), expansin-like A (EXLA), and expansin-like B (EXLB). EXPA and EXPB display cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. EXPA proteins function more efficiently on dicotyledonous cell walls, whereas EXPB proteins exhibit specificity for the cell walls of monocotyledons. Expansins also affect environmental stress responses. Expansin family proteins contain an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. This family also includes GH45 endoglucanases from mollusks. This model represents the N-terminal domain of expansins and similar proteins, which adopts a double-psi beta-barrel (DPBB) fold.
cd22269	DPBB_EG45-like	3.72e-05	86	125	62	102	double-psi beta-barrel fold of EG45-like domain-containing proteins. This family contains plant EG45-like domain-containing proteins which show sequence similarity to expansins, and similar proteins. Citrus jambhiri EG45-like domain-containing protein was identified as a protein associated with citrus blight (CB), and is also called blight-associated protein p12 (CjBAp12) or plant natriuretic peptide (PNP). CjBAp12 does not display cell wall loosening activity of expansins. Arabidopsis thaliana EG45-like domain-containing protein 2, also called plant natriuretic peptide A (AtPNP-A), is a systemically mobile natriuretic peptide immunoanalog, recognized by antibodies against vertebrate atrial natriuretic peptides (ANPs), that functions in cell volume regulation. Thus, it has an important and systemic role in plant growth and homeostasis. Due to their similarity to the N-terminal domain of expansin and to endolytic peptidoglycan transglycosylase RlpA, EG45-like domain-containing proteins may adopt a double-psi beta-barrel fold.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASB88842.1	3.71e-171	1	232	1	232
ATH92043.1	1.56e-163	1	232	1	232
SCA86346.1	3.15e-163	1	232	1	232
QAT65683.1	3.15e-163	1	232	1	232
QHZ47299.1	1.09e-156	1	232	1	231

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3D30_A	2.80e-139	26	232	2	208	Structureof an expansin like protein from Bacillus Subtilis at 1.9A resolution [Bacillus subtilis],4FER_A Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with cellohexaose [Bacillus subtilis subsp. subtilis str. 168],4FER_B Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with cellohexaose [Bacillus subtilis subsp. subtilis str. 168],4FFT_A Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with mixed-linkage glucan [Bacillus subtilis subsp. subtilis str. 168],4FFT_B Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with mixed-linkage glucan [Bacillus subtilis subsp. subtilis str. 168],4FG2_A Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with cellotetraose [Bacillus subtilis subsp. subtilis str. 168],4FG2_B Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with cellotetraose [Bacillus subtilis subsp. subtilis str. 168],4FG4_A Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with hemithiocellodextrin [Bacillus subtilis subsp. subtilis str. 168],4FG4_B Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with hemithiocellodextrin [Bacillus subtilis subsp. subtilis str. 168]
2BH0_A	2.11e-134	26	232	2	208	Crystalstructure of a SeMet derivative of EXPA from Bacillus subtilis at 2.5 angstrom [Bacillus subtilis]
4JCW_A	6.63e-28	34	206	10	179	Crystalstructure of Clavibacter michiganensis expansin in complex with cellopentaose [Clavibacter michiganensis subsp. michiganensis NCPPB 382],4JCW_B Crystal structure of Clavibacter michiganensis expansin in complex with cellopentaose [Clavibacter michiganensis subsp. michiganensis NCPPB 382],4JJO_A crystal structure of apo-clavibacter Michiganensis expansin [Clavibacter michiganensis]
4JS7_A	3.63e-27	34	206	10	179	Crystalstructure of D78N mutant apo form of clavibacter michiganensis expansin [Clavibacter michiganensis subsp. michiganensis NCPPB 382],4L48_A Crystal structure of d78n mutant clavibacter michiganensis expansin in complex with cellohexaose [Clavibacter michiganensis subsp. michiganensis NCPPB 382],4L48_C Crystal structure of d78n mutant clavibacter michiganensis expansin in complex with cellohexaose [Clavibacter michiganensis subsp. michiganensis NCPPB 382]