CAZyme Information: MGYG000001525_03327

Basic Information

• Species: Paenibacillus_A rubinfantis
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A rubinfantis
• CAZyme ID: MGYG000001525_03327
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
213		23378.39	7.2749

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001525	5369528	Isolate	not provided	not provided

• Gene Location: Start: 1110493; End: 1111134 Strand: -

Full Sequence      

MEIHFIDGAGQSFVLPVNPEEITISRSKGVETVNIASLGEYDFPAGERVKEIAFSSFFPA
DYDPGYCNYQDLPDPQEAMNRITTMMNSKSPVRLIITDTAVNVLVTIAAHNSTFRGGEPG
DVYFDLSARTWREMKVHAQTGASGAASTTQSTRPDTKKPAKTYVVKSGDTLSKIAKLELG
DSSKWQQIYSANQKTIGKDPNRIKPGQKLVMPQ

Enzyme Prediction     

No EC number prediction in MGYG000001525_03327.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK11198	PRK11198	3.18e-15	150	213	85	147	LysM domain/BON superfamily protein; Provisional
COG1652	XkdP	1.82e-14	5	213	58	263	Nucleoid-associated protein YgaU, contains BON and LysM domains [Function unknown].
cd00118	LysM	5.36e-11	161	210	1	44	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.
pfam01476	LysM	2.29e-08	163	212	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.
smart00257	LysM	2.33e-08	162	210	1	43	Lysin motif.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AZS14242.1	1.60e-114	1	212	1	210
AZS15369.1	4.44e-104	1	212	1	215
QPK51779.1	4.42e-94	1	211	1	212
QPK56865.1	4.42e-94	1	211	1	212
AUS25384.1	8.90e-94	1	211	1	212

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5FIM_A	1.37e-06	132	213	67	148	Thestructure of Kbp.K from E. coli [Escherichia coli],7PVC_A Chain A, Potassium binding protein Kbp [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P54335	1.61e-31	15	213	19	219	Phage-like element PBSX protein XkdP OS=Bacillus subtilis (strain 168) OX=224308 GN=xkdP PE=4 SV=2
P45932	4.92e-30	15	213	19	219	Uncharacterized protein YqbP OS=Bacillus subtilis (strain 168) OX=224308 GN=yqbP PE=4 SV=1
P0ADE6	6.69e-06	132	213	67	148	Potassium binding protein Kbp OS=Escherichia coli (strain K12) OX=83333 GN=kbp PE=1 SV=2
P0ADE7	6.69e-06	132	213	67	148	Potassium binding protein Kbp OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=kbp PE=3 SV=2

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
1.000058	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001525_03327.