3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases is part of the Pathway/BioSystem: 3D

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842851  78 EMTATGYTSGVESTGKSpghpeYGITYSGVKAKRdlYSTIAADLRVFPIGTILFVPDYGYGVVADKGGAIKGNRLDLYYD 157
Cdd:COG3584    1 TVTATAYTAGPECTGKG-----GGITASGTRLRP--GGVIAVDPDVIPLGTKVYIEGYGYAVAEDTGGAIKGNRIDIYMP 73

                         90
                 ....*....|
gi 446842851 158 TVKDVYsQWG 167
Cdd:COG3584   74 SVSEAL-NWG 82

3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases is part of the Pathway/BioSystem: 3D

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842851  78 EMTATGYTSGVESTGKSpghpeYGITYSGVKAKRdlYSTIAADLRVFPIGTILFVPDYGYGVVADKGGAIKGNRLDLYYD 157
Cdd:COG3584    1 TVTATAYTAGPECTGKG-----GGITASGTRLRP--GGVIAVDPDVIPLGTKVYIEGYGYAVAEDTGGAIKGNRIDIYMP 73

                         90
                 ....*....|
gi 446842851 158 TVKDVYsQWG 167
Cdd:COG3584   74 SVSEAL-NWG 82

double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and YuiC-like proteins; This family includes two subfamilies of conserved double-psi beta-barrel (DPBB) domain proteins, such as membrane-bound lytic murein transglycosylase A (MltA)-like proteins and YuiC-like proteins. MltA, also called murein hydrolase A, is a murein-degrading enzyme that may play a role in the recycling of muropeptides during cell elongation and/or cell division. It degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. Bacterial lytic transglycosylases (LTs) are classified into 4 families: family 1 includes slt70 MltC-MltF, family 2 includes MltA, family 3 includes MltB, and family 4 includes proteins of bacteriophage origin. MltA is distinct from other bacterial LTs, which are similar in structure and sequence with a lysozyme-like fold. MltA is a kidney bean-shaped monomeric protein 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 corresponds to a double-psi beta-barrel (DPBB) fold. Domain B also has a beta-barrel fold topology, but it is inserted within the linear sequence of domain A. YuiC is a Firmicute stationary phase survival (Sps) protein that closely resembles the Barwin-like endoglucanase beta barrel of MltA. It is a DPBB fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis and may be involved in substrate binding and catalysis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842851  79 MTATGYTSGVESTGKSPGhpeygITYSGVKAKRdlYSTIAADLRVFPIGTILFVPD---YGYGVVADKGGAIKGNRLDLY 155
Cdd:cd22784    1 VTVTAYTPDEEQTDGGPG-----ITASGVTLRG--YGTVAVDRDLIPLGTKVKIEGpgsGGEYVVLDRGGAIKGNRIDIY 73

                         90
                 ....*....|..
gi 446842851 156 YDTVKDVySQWG 167
Cdd:cd22784   74 FPSEKEA-KKFG 84

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.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842851  80 TATGYT---SGVESTGKSPGHPEYGITYSGVKAKRdlYSTIAADLRVFPIGTILFVPDY------GYGVVADKGGAIKGN 150
Cdd:cd14486    2 QATGYTewdDGKRPSPPDEFSFSFRLTASGRPPVP--YRTIAVDPSVIPLGSVVYIPELrglpndGVFVAEDTGGAIKGN 79

                 ....*
gi 446842851 151 RLDLY 155
Cdd:cd14486   80 HIDVY 84

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446842851 116 TIAADLRVFPIGTILFV----PDYGYG-------VVA-DKGGAIKG-NRLDLY 155
Cdd:cd14485   84 SLAVDRSLIPLGAPVWLetplPDANGGgkplrrlVIAqDTGGAIKGpVRADLF 136