CAZyme Information: MGYG000003687_01201

Basic Information

• Species: Paenibacillus polymyxa
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus polymyxa
• CAZyme ID: MGYG000003687_01201
• CAZy Family: CBM63
• CAZyme Description: Expansin-YoaJ

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
237	MGYG000003687_3|CGC6	25806.45	9.7298

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003687	5656034	Isolate	China	Asia

• Gene Location: Start: 280855; End: 281568 Strand: +

Full Sequence      

MQEKSLFRKFKTIGLTSLLSVVLFALPASAAWNDTYTGYATYTGSGYSGGALLLDPIPSD
AKITALNPTQLNYNGIKAALAGAYLEVQGPKGKTTVYVTDLYPEGPSGALDLSPNAFNLI
GNQKDGKINISWKVVKAPVSGNVSYRIKEGSSQWWAAIQVRNHKYPVLKMEVQQNGQWLN
LEKQDYNHFLGTNLGKQPLKIRITDIRGVVLNDTIPALAENGTGQAYIVKGNVQFPD

Enzyme Prediction     

No EC number prediction in MGYG000003687_01201.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM63	144	219	8.2e-39	0.9743589743589743

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4305	YoaJ	2.37e-132	18	237	13	232	Peptidoglycan-binding domain, expansin [Cell wall/membrane/envelope biogenesis].
cd22272	DPBB_EXLX1-like	2.56e-54	34	134	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	1.31e-17	36	134	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	3.39e-11	26	135	1	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.
PLN03024	PLN03024	2.08e-05	1	132	1	123	Putative EG45-like domain containing protein 1; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDA28429.1	2.82e-173	1	237	1	237
QPK59247.1	2.82e-173	1	237	1	237
QPK54157.1	2.82e-173	1	237	1	237
AUS27696.1	8.08e-173	1	237	1	237
QOH63021.1	1.15e-172	1	237	1	237

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3D30_A	3.43e-116	31	237	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	9.37e-114	31	237	2	208	Crystalstructure of a SeMet derivative of EXPA from Bacillus subtilis at 2.5 angstrom [Bacillus subtilis]
4JCW_A	4.45e-26	37	208	8	176	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	2.42e-25	37	208	8	176	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34918	6.81e-119	18	237	13	232	Expansin-YoaJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yoaJ PE=1 SV=1
Q55G31	1.23e-11	39	236	38	244	Expansin-like protein 1 OS=Dictyostelium discoideum OX=44689 GN=expl1 PE=2 SV=1
Q7KWS2	1.42e-10	9	216	2	218	Expansin-like protein 3 OS=Dictyostelium discoideum OX=44689 GN=expl3 PE=2 SV=1
Q86AV4	1.18e-09	58	221	59	225	Expansin-like protein 5 OS=Dictyostelium discoideum OX=44689 GN=expl5 PE=2 SV=1
Q55G32	4.59e-06	77	233	76	247	Expansin-like protein 6 OS=Dictyostelium discoideum OX=44689 GN=expl6 PE=2 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
0.000364	0.998907	0.000222	0.000168	0.000169	0.000160

TMHMM  Annotations     

start	end
13	32