NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|657199026|ref|WP_029314565|]
View 

MULTISPECIES: murein transglycosylase A [Aeromonas]

Protein Classification

murein transglycosylase A( domain architecture ID 11485235)

membrane-bound lytic murein transglycosylase A cleaves the beta-1,4 glycosidic linkages between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
mltA PRK11162
murein transglycosylase A; Provisional
 8-372 0e+00

murein transglycosylase A; Provisional


:

Pssm-ID: 236866 [Multi-domain]  Cd Length: 355  Bit Score: 608.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026   8 LAAAVVGLAGCAGNPEpvkvpqkkaesgcflnceipvNLGKQYLDGALPGDLVRVERVN-SRARADYSKFGPQSRMVMER 86
Cdd:PRK11162  11 TGTVLALLAGCSSKPT---------------------DRGQQYKDGKFTQPLSLVNQPNaSGKPINAGDFAEQVNQIRNS 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026  87 SGRMASRYGELYRQLSRWVANGGNPAHITQYGISLAQLGGADRMGNVLFTGYYSPVLEVRHRPDAQYKYPIYAMPNCGGR 166
Cdd:PRK11162  70 SPRLYGRYSNTYNAVQEWLLAGGDTRELRQFGIQAWQMEGVDNYGNVQFTGYYTPVIQARHTPQGEFQYPIYRMPPKRGR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 167 CPSRAEIHRGALANRGLELGYSKSLIDNFLMDVQGSGFVHYGDDDRLQYLGYSGKNGHGYVSIGRVLIDRGEVPKEQMSM 246
Cdd:PRK11162 150 LPSRAEIYAGALSGKGLELAYSNSLIDNFIMEVQGSGYVDFGDGRPLNFFAYAGKNGHAYRSIGKVLIDRGEVPKEDMSM 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 247 KAIKEWANRQPEESVKELVEQNPSYVFFERRPTNDVVGAAGIPLLPMAAVAADKTLLPMGTPILAEVPLLDKEGNWTGKH 326
Cdd:PRK11162 230 QAIREWGEKHSEAEVRELLEQNPSFVFFKPQPFAPVKGASAVPLVAMASVASDRSIIPPGTVLLAEVPLLDNNGKFTGKY 309

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 657199026 327 QLRLLIALDVGGAVKKGHLDLYHGMGEKAGVAAGHYKHFGRVWKLG 372
Cdd:PRK11162 310 ELRLMVALDVGGAIKGQHFDIYQGIGPEAGHRAGHYNHYGRVWVLK 355
 
Name Accession Description Interval E-value
mltA PRK11162
murein transglycosylase A; Provisional
 8-372 0e+00

murein transglycosylase A; Provisional


Pssm-ID: 236866 [Multi-domain]  Cd Length: 355  Bit Score: 608.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026   8 LAAAVVGLAGCAGNPEpvkvpqkkaesgcflnceipvNLGKQYLDGALPGDLVRVERVN-SRARADYSKFGPQSRMVMER 86
Cdd:PRK11162  11 TGTVLALLAGCSSKPT---------------------DRGQQYKDGKFTQPLSLVNQPNaSGKPINAGDFAEQVNQIRNS 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026  87 SGRMASRYGELYRQLSRWVANGGNPAHITQYGISLAQLGGADRMGNVLFTGYYSPVLEVRHRPDAQYKYPIYAMPNCGGR 166
Cdd:PRK11162  70 SPRLYGRYSNTYNAVQEWLLAGGDTRELRQFGIQAWQMEGVDNYGNVQFTGYYTPVIQARHTPQGEFQYPIYRMPPKRGR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 167 CPSRAEIHRGALANRGLELGYSKSLIDNFLMDVQGSGFVHYGDDDRLQYLGYSGKNGHGYVSIGRVLIDRGEVPKEQMSM 246
Cdd:PRK11162 150 LPSRAEIYAGALSGKGLELAYSNSLIDNFIMEVQGSGYVDFGDGRPLNFFAYAGKNGHAYRSIGKVLIDRGEVPKEDMSM 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 247 KAIKEWANRQPEESVKELVEQNPSYVFFERRPTNDVVGAAGIPLLPMAAVAADKTLLPMGTPILAEVPLLDKEGNWTGKH 326
Cdd:PRK11162 230 QAIREWGEKHSEAEVRELLEQNPSFVFFKPQPFAPVKGASAVPLVAMASVASDRSIIPPGTVLLAEVPLLDNNGKFTGKY 309

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 657199026 327 QLRLLIALDVGGAVKKGHLDLYHGMGEKAGVAAGHYKHFGRVWKLG 372
Cdd:PRK11162 310 ELRLMVALDVGGAIKGQHFDIYQGIGPEAGHRAGHYNHYGRVWVLK 355
MltA COG2821
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];
7-380 2.91e-117

Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442069 [Multi-domain]  Cd Length: 388  Bit Score: 345.71  E-value: 2.91e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026   7 WLAAAVVGLAGCAGNPEPVKVPQKKAESgcflnceIPVNLGkqyldgALPG-------DLVRVERVNSRAradyskfgPQ 79
Cdd:COG2821    5 LLLLALLLLAACATQPPPPGAAAPDARL-------QPVSFS------DLPGwadddlaAALPAFRRSCRR--------LA 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026  80 SRMVMERSGRMASRYGELYRQLSRW-VANGGNPAHITQYGISLAQLGGADRMGNVLFTGYYSPVLEVRHRPDAQYKYPIY 158
Cdd:COG2821   64 RRPAASAYGITAADWRAACAAARQLpAADPAAARAFFEREFQPYQVVGPDGGGNGLFTGYYEPELEGSRTRTAEYRYPLY 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 159 AMPNC---------------------GGR---CPSRAEIHRGALANRGLELGYSKSLIDNFLMDVQGSGFVHYgDDDRLQ 214
Cdd:COG2821  144 RRPPDlvtvdlgsfelkgkrlrgrleGGRlvpYPTRAEIEAGALAGRGLELAWVDDPVDAFFLQIQGSGRVRL-PDGSLI 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 215 YLGYSGKNGHGYVSIGRVLIDRGEVPKEQMSMKAIKEWANRQPEEsVKELVEQNPSYVFFERRPTND--VVGAAGIPLLP 292
Cdd:COG2821  223 RVGYAGKNGHPYTSIGRLLIDRGELPLEQMSMQAIRAWLRANPEE-LRELLNQNPSYVFFRELPGPDagPLGALGVPLTP 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 293 MAAVAADKTLLPMGTPILAEVPLLDKegNWTGKHQLRLLIALDVGGAVKK-GHLDLYHGMGEKAGVAAGHYKHFGRVWKL 371
Cdd:COG2821  302 GRSIAVDPSLIPLGAPVWLETTLPDA--NFSGKPLRRLMIAQDTGGAIKGaVRADLFWGTGDEAGERAGRMKHPGRLWVL 379


                 ....*....
gi 657199026 372 GLHHGPTAA 380
Cdd:COG2821  380 LPKGAAPPL 388
MltA smart00925
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
 142-274 8.86e-63

MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein degrading transglycosylase enzyme. This domain may be involved in peptidoglycan binding.


Pssm-ID: 214916  Cd Length: 153  Bit Score: 198.17  E-value: 8.86e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026   142 VLEVRHRPDAQYKYPIYAMPNC-----------------GGR----CPSRAEIHRGALANRGLELGYSKSLIDNFLMDVQ 200
Cdd:smart00925   1 VLEGSRTRTGRYRYPLYRRPDDlvvvdlfdpelkgkrlrGGGklvpYPTRAEIEDGALDGRGLELAWVDDPVDLFFLQIQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657199026   201 GSGFVHYgDDDRLQYLGYSGKNGHGYVSIGRVLIDRGEVPKEQMSMKAIKEWANRQPEEsVKELVEQNPSYVFF 274
Cdd:smart00925  81 GSGRVRL-PDGRLIRVGYAGKNGHPYRSIGRLLIDRGEIPKEEASMQAIRAWLRANPER-VDELLNRNPSYVFF 152
mlta_B cd14668
Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a ...
 143-277 8.85e-51

Domain B insert of mltA_like lytic transglycosylases; 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.


Pssm-ID: 270616  Cd Length: 159  Bit Score: 167.32  E-value: 8.85e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 143 LEVRHRPDAQYKYPIYAMPN------------------CGGRC--------PSRAEIHRGALANRGLELGYSKSLIDNFL 196
Cdd:cd14668    1 LEGSRTPTAEYRYPLYGRPPdlvtvdlgefypelkgkrLRGRVeggrlvpyYTRAEIEAGALLGRGLELAWLDDPVDAFF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 197 MDVQGSGFVHYgDDDRLQYLGYSGKNGHGYVSIGRVLIDRGEVPKEQMSMKAIKEWANRQPEEsVKELVEQNPSYVFFER 276
Cdd:cd14668   81 LQIQGSGRLRL-PDGSVVRVGYAGKNGHPYRSIGRVLIDRGELPKEQMSMQAIRAWLRANPER-ARELLNENPSYVFFRE 158


                 .
gi 657199026 277 R 277
Cdd:cd14668  159 L 159
MltA pfam03562
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
 134-274 1.36e-50

MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein degrading transglycosylase enzyme. This domain may be involved in peptidoglycan binding.


Pssm-ID: 460973 [Multi-domain]  Cd Length: 231  Bit Score: 169.28  E-value: 1.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026  134 LFTGYYSPVLEVRHRPDAQYKYPIYAMP------------NCGGRC------------PSRAEIHR-GALANRGLELGYS 188
Cdd:pfam03562  67 LFTGYYEPELEGSRTRTAEYRYPLYRRPpdlvtvdlgffpLKGKRLrgrlvggwlvpyPTRAEIEGkGALSGRGLELAWL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026  189 KSLIDNFLMDVQGSGFVHYgDDDRLQYLGYSGKNGHGYVSIGRVLIDRGEVPKEQMSMKAIKEWANRQPEEsVKELVEQN 268
Cdd:pfam03562 147 RDPVDAFFLQIQGSGRLRL-PDGSVVRVGYAGQNGHPYTSIGRELIDRGELPLEQASMQGIRAWLRANPEE-LDELLNRN 224


                  ....*.
gi 657199026  269 PSYVFF 274
Cdd:pfam03562 225 PSYVFF 230
 
Name Accession Description Interval E-value
mltA PRK11162
murein transglycosylase A; Provisional
 8-372 0e+00

murein transglycosylase A; Provisional


Pssm-ID: 236866 [Multi-domain]  Cd Length: 355  Bit Score: 608.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026   8 LAAAVVGLAGCAGNPEpvkvpqkkaesgcflnceipvNLGKQYLDGALPGDLVRVERVN-SRARADYSKFGPQSRMVMER 86
Cdd:PRK11162  11 TGTVLALLAGCSSKPT---------------------DRGQQYKDGKFTQPLSLVNQPNaSGKPINAGDFAEQVNQIRNS 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026  87 SGRMASRYGELYRQLSRWVANGGNPAHITQYGISLAQLGGADRMGNVLFTGYYSPVLEVRHRPDAQYKYPIYAMPNCGGR 166
Cdd:PRK11162  70 SPRLYGRYSNTYNAVQEWLLAGGDTRELRQFGIQAWQMEGVDNYGNVQFTGYYTPVIQARHTPQGEFQYPIYRMPPKRGR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 167 CPSRAEIHRGALANRGLELGYSKSLIDNFLMDVQGSGFVHYGDDDRLQYLGYSGKNGHGYVSIGRVLIDRGEVPKEQMSM 246
Cdd:PRK11162 150 LPSRAEIYAGALSGKGLELAYSNSLIDNFIMEVQGSGYVDFGDGRPLNFFAYAGKNGHAYRSIGKVLIDRGEVPKEDMSM 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 247 KAIKEWANRQPEESVKELVEQNPSYVFFERRPTNDVVGAAGIPLLPMAAVAADKTLLPMGTPILAEVPLLDKEGNWTGKH 326
Cdd:PRK11162 230 QAIREWGEKHSEAEVRELLEQNPSFVFFKPQPFAPVKGASAVPLVAMASVASDRSIIPPGTVLLAEVPLLDNNGKFTGKY 309

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 657199026 327 QLRLLIALDVGGAVKKGHLDLYHGMGEKAGVAAGHYKHFGRVWKLG 372
Cdd:PRK11162 310 ELRLMVALDVGGAIKGQHFDIYQGIGPEAGHRAGHYNHYGRVWVLK 355
MltA COG2821
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];
7-380 2.91e-117

Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442069 [Multi-domain]  Cd Length: 388  Bit Score: 345.71  E-value: 2.91e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026   7 WLAAAVVGLAGCAGNPEPVKVPQKKAESgcflnceIPVNLGkqyldgALPG-------DLVRVERVNSRAradyskfgPQ 79
Cdd:COG2821    5 LLLLALLLLAACATQPPPPGAAAPDARL-------QPVSFS------DLPGwadddlaAALPAFRRSCRR--------LA 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026  80 SRMVMERSGRMASRYGELYRQLSRW-VANGGNPAHITQYGISLAQLGGADRMGNVLFTGYYSPVLEVRHRPDAQYKYPIY 158
Cdd:COG2821   64 RRPAASAYGITAADWRAACAAARQLpAADPAAARAFFEREFQPYQVVGPDGGGNGLFTGYYEPELEGSRTRTAEYRYPLY 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 159 AMPNC---------------------GGR---CPSRAEIHRGALANRGLELGYSKSLIDNFLMDVQGSGFVHYgDDDRLQ 214
Cdd:COG2821  144 RRPPDlvtvdlgsfelkgkrlrgrleGGRlvpYPTRAEIEAGALAGRGLELAWVDDPVDAFFLQIQGSGRVRL-PDGSLI 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 215 YLGYSGKNGHGYVSIGRVLIDRGEVPKEQMSMKAIKEWANRQPEEsVKELVEQNPSYVFFERRPTND--VVGAAGIPLLP 292
Cdd:COG2821  223 RVGYAGKNGHPYTSIGRLLIDRGELPLEQMSMQAIRAWLRANPEE-LRELLNQNPSYVFFRELPGPDagPLGALGVPLTP 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 293 MAAVAADKTLLPMGTPILAEVPLLDKegNWTGKHQLRLLIALDVGGAVKK-GHLDLYHGMGEKAGVAAGHYKHFGRVWKL 371
Cdd:COG2821  302 GRSIAVDPSLIPLGAPVWLETTLPDA--NFSGKPLRRLMIAQDTGGAIKGaVRADLFWGTGDEAGERAGRMKHPGRLWVL 379


                 ....*....
gi 657199026 372 GLHHGPTAA 380
Cdd:COG2821  380 LPKGAAPPL 388
MltA smart00925
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
 142-274 8.86e-63

MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein degrading transglycosylase enzyme. This domain may be involved in peptidoglycan binding.


Pssm-ID: 214916  Cd Length: 153  Bit Score: 198.17  E-value: 8.86e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026   142 VLEVRHRPDAQYKYPIYAMPNC-----------------GGR----CPSRAEIHRGALANRGLELGYSKSLIDNFLMDVQ 200
Cdd:smart00925   1 VLEGSRTRTGRYRYPLYRRPDDlvvvdlfdpelkgkrlrGGGklvpYPTRAEIEDGALDGRGLELAWVDDPVDLFFLQIQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657199026   201 GSGFVHYgDDDRLQYLGYSGKNGHGYVSIGRVLIDRGEVPKEQMSMKAIKEWANRQPEEsVKELVEQNPSYVFF 274
Cdd:smart00925  81 GSGRVRL-PDGRLIRVGYAGKNGHPYRSIGRLLIDRGEIPKEEASMQAIRAWLRANPER-VDELLNRNPSYVFF 152
mlta_B cd14668
Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a ...
 143-277 8.85e-51

Domain B insert of mltA_like lytic transglycosylases; 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.


Pssm-ID: 270616  Cd Length: 159  Bit Score: 167.32  E-value: 8.85e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 143 LEVRHRPDAQYKYPIYAMPN------------------CGGRC--------PSRAEIHRGALANRGLELGYSKSLIDNFL 196
Cdd:cd14668    1 LEGSRTPTAEYRYPLYGRPPdlvtvdlgefypelkgkrLRGRVeggrlvpyYTRAEIEAGALLGRGLELAWLDDPVDAFF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 197 MDVQGSGFVHYgDDDRLQYLGYSGKNGHGYVSIGRVLIDRGEVPKEQMSMKAIKEWANRQPEEsVKELVEQNPSYVFFER 276
Cdd:cd14668   81 LQIQGSGRLRL-PDGSVVRVGYAGKNGHPYRSIGRVLIDRGELPKEQMSMQAIRAWLRANPER-ARELLNENPSYVFFRE 158


                 .
gi 657199026 277 R 277
Cdd:cd14668  159 L 159
MltA pfam03562
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
 134-274 1.36e-50

MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein degrading transglycosylase enzyme. This domain may be involved in peptidoglycan binding.


Pssm-ID: 460973 [Multi-domain]  Cd Length: 231  Bit Score: 169.28  E-value: 1.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026  134 LFTGYYSPVLEVRHRPDAQYKYPIYAMP------------NCGGRC------------PSRAEIHR-GALANRGLELGYS 188
Cdd:pfam03562  67 LFTGYYEPELEGSRTRTAEYRYPLYRRPpdlvtvdlgffpLKGKRLrgrlvggwlvpyPTRAEIEGkGALSGRGLELAWL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026  189 KSLIDNFLMDVQGSGFVHYgDDDRLQYLGYSGKNGHGYVSIGRVLIDRGEVPKEQMSMKAIKEWANRQPEEsVKELVEQN 268
Cdd:pfam03562 147 RDPVDAFFLQIQGSGRLRL-PDGSVVRVGYAGQNGHPYTSIGRELIDRGELPLEQASMQGIRAWLRANPEE-LDELLNRN 224


                  ....*.
gi 657199026  269 PSYVFF 274
Cdd:pfam03562 225 PSYVFF 230
mltA_B_like cd14472
Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a ...
 143-277 2.11e-44

Domain B insert of mltA_like lytic transglycosylases; 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.


Pssm-ID: 270615  Cd Length: 134  Bit Score: 150.20  E-value: 2.11e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 143 LEVRHRPDAQYKYPIYAMPNCGGRCPSRAEIHRGALAnRGLELGYSKSLIDNFLMDVQGSGFVHYGDDDRLQYLGYSGKN 222
Cdd:cd14472    1 IQARHTRQGEFQYPIYRIPPKRGRLSSRAEIYAGALS-DKYILAYSNSLVDNFIADVQGSGYIDFGDGSPLNFFSYAGKN 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 657199026 223 GHGYVSIGRVLIDRGEVPKEQMSMKAIKEWANRQPEESVKELVEQNPSYVFFERR 277
Cdd:cd14472   80 GHAYRSIGKVLIDRGEVKKEDISSQAIRHWGETHSEAEVRELLEQNPSFVFFKPQ 134
mltA_like_LT_A cd14485
Domain A of MltA and related lytic transglycosylase; domain A is interrupted by domain B; ...
 287-371 3.03e-27

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.


Pssm-ID: 270618 [Multi-domain]  Cd Length: 159  Bit Score: 105.41  E-value: 3.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 287 GIPLLPMAAVAADKTLLPMGTPILAEVPLLDkeGNWTGKHQLRLLIALDVGGAVK-KGHLDLYHGMGEKAGVAAGHYKHF 365
Cdd:cd14485   76 GVPLTPGRSLAVDRSLIPLGAPVWLETPLPD--ANGGGKPLRRLVIAQDTGGAIKgPVRADLFWGSGDEAGELAGRMKHP 153


                 ....*.
gi 657199026 366 GRVWKL 371
Cdd:cd14485  154 GRLWVL 159
DPBB_MltA-like cd22785
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
 282-371 1.80e-25

double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and similar 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. This model corresponds to the DPBB fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis. It is involved in substrate binding and catalysis.


Pssm-ID: 439262 [Multi-domain]  Cd Length: 97  Bit Score: 98.87  E-value: 1.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 282 VVGAAGIPLLPMAAVAADKTLLPMGTPILAEVPLLDKegNWTGKHQLRLLIALDVGGAVKKGHLDLYHGMGEKAGVAAGH 361
Cdd:cd22785   10 PRGALGVPLTPFRSVAVDPSVIPLGSVVYIPALDGVK--LPDGEPHDGLFIAQDTGGAIKGKHIDVFTGSGDEAGELAGK 87

                         90
                 ....*....|
gi 657199026 362 YKHFGRVWKL 371
Cdd:cd22785   88 LNHTGRVYVL 97
3D pfam06725
3D domain; This short presumed domain contains three conserved aspartate residues, hence the ...
 294-371 6.57e-20

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.


Pssm-ID: 399598 [Multi-domain]  Cd Length: 72  Bit Score: 82.64  E-value: 6.57e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657199026  294 AAVAADKTLLPMGTPILAEVPLldkegnwTGKHQLRLLIALDVGGAVKKGHLDLYHGMGEKAGVAAGHYKHFGRVWKL 371
Cdd:pfam06725   1 RSIAVDPSVIPLGTPVYVEGPL-------GGKPVYRLAIAQDTGGAIKGNRIDLYFGTGDEAGNLAGLYRKTGRVYIL 71
mlta_related_B cd14669
putative domain B insert of mltA_type lytic transglycosylases; Escherichia coli MltA is a ...
 143-276 3.94e-12

putative domain B insert of mltA_type lytic transglycosylases; 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.


Pssm-ID: 270617  Cd Length: 128  Bit Score: 62.82  E-value: 3.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 143 LEVRHRPDAQYKYPIYAMP-NCGGRCPSRAEIHRGALANRGLeLGYSKSLIDNFLMDVQGSGFVHYgDDDRLQYLGYSGK 221
Cdd:cd14669    3 IGSRTYPGGAFLYPVYGNPgDMIVPYYTRAEIERGALWEAKV-IAYVKDPTDLYLMQLQGSGKVKL-PDGTVFRIAYAEQ 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 657199026 222 NGHGYVSIGRVL----IDRGEVPKEQMSMKAIKEWANRqpeesvkelveqNPSYVFFER 276
Cdd:cd14669   81 NGRPFLPPVASAkgslTPSEAANCIALNPPEVAAFAIS------------DPSYVFFRK 127
3D_domain cd14486
3D domain, named for 3 conserved aspartate residues, is found in mltA-like lytic ...
 284-356 1.11e-08

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.


Pssm-ID: 270619 [Multi-domain]  Cd Length: 104  Bit Score: 52.38  E-value: 1.11e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657199026 284 GAAGIPLLPMAAVAADKTLLPMGTPILAEVPLLDKEGNWtgkhqlrlLIALDVGGAVKKGHLDLYHGMGEKAG 356
Cdd:cd14486   28 TASGRPPVPYRTIAVDPSVIPLGSVVYIPELRGLPNDGV--------FVAEDTGGAIKGNHIDVYTGDGPDAR 92
DPBB_MltA_YuiC-like cd22784
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
 281-355 5.06e-07

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.


Pssm-ID: 439261 [Multi-domain]  Cd Length: 92  Bit Score: 47.26  E-value: 5.06e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657199026 281 DVVGAAGIPLLPMAAVAADKTLLPMGTPILAEVPLLDKEGnwtgkhqlrllIALDVGGAVKKGHLDLYHGMGEKA 355
Cdd:cd22784   17 PGITASGVTLRGYGTVAVDRDLIPLGTKVKIEGPGSGGEY-----------VVLDRGGAIKGNRIDIYFPSEKEA 80
3D_containing_proteins cd14667
Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; ...
 285-367 2.20e-04

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.


Pssm-ID: 270620 [Multi-domain]  Cd Length: 90  Bit Score: 39.81  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199026 285 AAGIPLLPMAAVAADKTLLPMGTPILAEVplldkegnwtgkhqLRLLIALDVGGAVKKGHLDLYHGMGEKAgvaaghyKH 364
Cdd:cd14667   21 ASGGLPVGGGTIAVDPSVIPLGTKVYIEG--------------YGVYVVEDTGGAIKGNRIDIYMDSHAEA-------LA 79


                 ...
gi 657199026 365 FGR 367
Cdd:cd14667   80 FGR 82
COG3584 COG3584
3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D ...
 285-348 1.54e-03

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


Pssm-ID: 442803 [Multi-domain]  Cd Length: 92  Bit Score: 37.39  E-value: 1.54e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657199026 285 AAGIPLLPMAAVAADKTLLPMGTPILAEvplldkeGNWTGkhqlrllIALDVGGAVKKGHLDLY 348
Cdd:COG3584   22 ASGTRLRPGGVIAVDPDVIPLGTKVYIE-------GYGYA-------VAEDTGGAIKGNRIDIY 71
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH