CAZyme Information: MGYG000001514_03396

Basic Information

• Species: Paenibacillus_A ihumii
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A ihumii
• CAZyme ID: MGYG000001514_03396
• CAZy Family: CBM50
• CAZyme Description: Cell wall-binding protein YocH

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
224	MGYG000001514_12|CGC36	23991.6	9.9842

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001514	5923787	Isolate	not provided	not provided

• Gene Location: Start: 2027695; End: 2028369 Strand: +

Full Sequence      

MLKQLRSRKWSRSIKVAVIAAGITGALSVMPAYADSVHKAKDGDTFFLLAKQYGVNLDKL
MQTNPSIEATNIYEGLSITIPGQGVQAMSAPASEVQALSTLKVLSSERVVKAWGKSFNYK
STIDVKATAYSAAASENGKWGAVDYYGNPLKLGTIAVDPKVIPMGTKVLVTGHSHPDLPK
NAFVATATDQGSAIQGNRIDIFIPASPQKVSQFGFQDLKLYVID

Enzyme Prediction     

No EC number prediction in MGYG000001514_03396.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14667	3D_containing_proteins	1.68e-28	125	223	1	90	Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues. This family contains the 3D domain, named for its 3 conserved aspartates, including similar uncharacterized proteins. These proteins contain the critical active site aspartate of mltA-like lytic transglycosylases where the 3D domain forms a larger domain with the N-terminal region. This domain is also found in conjunction with numerous other domains such as the Escherichia coli MltA, a membrane-bound lytic transglycosylase comprised of 2 domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, corresponding to the 3D domain and Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial LTs, which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond.
COG3584	3D	1.70e-16	121	222	17	109	3D (Asp-Asp-Asp) domain [Function unknown].
cd14486	3D_domain	2.16e-13	146	223	30	104	3D domain, named for 3 conserved aspartate residues, is found in mltA-like lytic transglycosylases and numerous other contexts. This family contains the 3D domain, named for its 3 conserved aspartates. It is found in conjunction with numerous other domains such as MltA (membrane-bound lytic murein transglycosylase A). These aspartates are critical active site residues of mltA-like lytic transglycosylases. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. MltA has 2 domains, separated by a large groove, where the peptidoglycan strand binds. The C-terminus has a double-psi beta barrel fold within the 3D domain, which forms the larger A domain along with the N-terminal region of Mlts, but is also found in various other domain architectures. Peptigoglycan (also known as murein) chains, the primary structural component of bacterial cells walls, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc); lytic transglycosylases (LTs) cleave this beta-1-4 bond. Typically, LTs are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, membrane-bound lytic murein transglycosylase E (MltE) is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane- bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and family 4 of bacteriophage origin. While most LTs are related members of the lysozyme-like lytic transglycosylase family, MltA represents a distinct fold and sequence conservation.
pfam06725	3D	2.81e-11	154	224	2	72	3D domain. This short presumed domain contains three conserved aspartate residues, hence the name 3D. It has been shown to be part of the catalytic double psi beta barrel domain of MltA.
cd14485	mltA_like_LT_A	1.44e-07	145	202	72	136	Domain A of MltA and related lytic transglycosylase; domain A is interrupted by domain B. Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AZK47418.1	3.51e-131	1	224	1	224
AZS15042.1	1.42e-94	2	223	1	228
AWB44823.1	5.91e-91	14	224	18	227
ACX64701.1	3.34e-89	6	224	23	243
AYB44967.1	4.73e-89	6	224	23	243

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4WLI_A	3.99e-08	125	223	16	113	StationaryPhase Survival Protein YuiC from B.subtilis [Bacillus subtilis subsp. subtilis str. 168]
4WLK_A	5.51e-08	125	223	37	134	StationaryPhase Survival Protein YuiC from B.subtilis complexed with reaction product [Bacillus subtilis subsp. subtilis str. 168],4WLK_B Stationary Phase Survival Protein YuiC from B.subtilis complexed with reaction product [Bacillus subtilis subsp. subtilis str. 168]
4WJT_A	5.59e-08	125	223	37	134	StationaryPhase Survival Protein YuiC from B.subtilis complexed with NAG [Bacillus subtilis subsp. subtilis str. 168],4WJT_B Stationary Phase Survival Protein YuiC from B.subtilis complexed with NAG [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34669	4.25e-13	2	224	47	287	Cell wall-binding protein YocH OS=Bacillus subtilis (strain 168) OX=224308 GN=yocH PE=1 SV=1
P37546	4.15e-08	125	224	317	407	Putative cell wall shaping protein YabE OS=Bacillus subtilis (strain 168) OX=224308 GN=yabE PE=2 SV=2
O32108	5.58e-07	125	223	88	185	Uncharacterized protein YuiC OS=Bacillus subtilis (strain 168) OX=224308 GN=yuiC PE=1 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
0.000324	0.998883	0.000230	0.000201	0.000182	0.000144

TMHMM  Annotations     

start	end
12	34