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Conserved domains on  [gi|333965670|gb|AEG32436|]
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Lytic transglycosylase catalytic [Thiomicrospira cyclica ALM1]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 219-380 3.59e-101

membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and MltE are periplasmic, outer membrane attached lytic transglycosylases (LTs), which cleave beta-1,4-glycosidic bonds joining N-acetylmuramic acid and N-acetylglucosamine in the cell wall peptidoglycan, yielding 1,6-anhydromuropeptides. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda


:

Pssm-ID: 381614 [Multi-domain]  Cd Length: 162  Bit Score: 296.39  E-value: 3.59e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 219 DSVRRYSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRDAHELIYKRPGTPTRNYLFVPDNNIQMGVG 298
Cdd:cd16893    1 PIVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVYRLLGGKGGLPSKSYLFDPENNIDIGTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 299 YLSILDTRYLVRVNNPQSREYCVIAGYNTGSGNVLRTFDNDRSRAFEQINRMQPQQVYQHLVRHLPFAETRRYMQKVTEF 378
Cdd:cd16893   81 YLHILQNRYLKGIKNPKSREYCAIAAYNGGAGNVLRTFSSDRKKAISKINRLSPDEVYQHLTKKLPAAETRNYLKKVLKA 160


                 ..
gi 333965670 379 QR 380
Cdd:cd16893  161 KK 162
Mltc_N super family cl13335
Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found ...
 61-205 2.24e-39

Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found associated with pfam01464. It is the N-terminal structural domain of MltC (Membrane-bound lytic murein transglycosylase C), one of the seven lytic transglycosylases found in the genome of the Gram-negative bacterium Escherichia coli. The role of the N-terminal domain is suggested to be important not as a mere structural extension of the active site beyond what is seen in other lytic transglycosylases but one that creates a peptide-binding site at position +2.


The actual alignment was detected with superfamily member pfam11873:

Pssm-ID: 432150  Cd Length: 161  Bit Score: 137.77  E-value: 2.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670   61 EIDRLVRNQLQELAsflaRKWGDEK--TASPQEFVKYSNDFETRAIVNFETRLVRVESLS--EDRALLQRAIVTTLLTPD 136
Cdd:pfam11873   7 ALDILVGQFSGNIE----KIWGKNEvlVASKKDYVKYTDNYKSRAHIDFDKGIITIETLAtkNPKAHLRNAIITTLLTPD 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333965670  137 RPDQVDLLTDQPIQGGGQPFLYRLVRDHQGQFVQFEWRATQYAQHLVTNQRQTLNSRGQpRRYFVEFAL 205
Cdd:pfam11873  83 DPSDVDLYSDKDIELSGKPFLYGQVLDQDGQPIRWEWRANRFADYLIKNKLKTRKKNGK-KVYYVSIPM 150
 
Name Accession Description Interval E-value
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 219-380 3.59e-101

membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and MltE are periplasmic, outer membrane attached lytic transglycosylases (LTs), which cleave beta-1,4-glycosidic bonds joining N-acetylmuramic acid and N-acetylglucosamine in the cell wall peptidoglycan, yielding 1,6-anhydromuropeptides. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda


Pssm-ID: 381614 [Multi-domain]  Cd Length: 162  Bit Score: 296.39  E-value: 3.59e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 219 DSVRRYSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRDAHELIYKRPGTPTRNYLFVPDNNIQMGVG 298
Cdd:cd16893    1 PIVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVYRLLGGKGGLPSKSYLFDPENNIDIGTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 299 YLSILDTRYLVRVNNPQSREYCVIAGYNTGSGNVLRTFDNDRSRAFEQINRMQPQQVYQHLVRHLPFAETRRYMQKVTEF 378
Cdd:cd16893   81 YLHILQNRYLKGIKNPKSREYCAIAAYNGGAGNVLRTFSSDRKKAISKINRLSPDEVYQHLTKKLPAAETRNYLKKVLKA 160


                 ..
gi 333965670 379 QR 380
Cdd:cd16893  161 KK 162
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
87-382 7.94e-99

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 297.73  E-value: 7.94e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670  87 ASPQEFVKYSNDFETRAIVNFETRLVRVESLS--EDRALLQRAIVTTLLTPDRPDQVDLLTDQ-PIQGGGQPFLYRLVRD 163
Cdd:PRK11671  60 AGPKDYVKYTDQYQTRSHINFDDGTITIETIAgtNPAAHLRQAIIKTLLMGDDPGSIDLYSDVdDIPISKEPFLYGQVLD 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 164 HQGQFVQFEWRATQYAQHLVTNQRQTLNSRGQPRRYFVEFALSDQLDRQQQtKFADSVRRYSRTYSIRPDLIYAIMEAES 243
Cdd:PRK11671 140 NTGQPIRWEGRASNFADYLLQNKLQSRSNGLRIIYSVTINMVPNHLDKRAH-KYLPMVRKASRKYGVDESLILAIMQTES 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 244 SFNPYAMSHIPAYGLMQIVPTTAGRDahelIYKRPG---TPTRNYLFVPDNNIQMGVGYLSILDTRYLVRVNNPQSREYC 320
Cdd:PRK11671 219 SFNPYAVSRSDALGLMQVVQHTAGKD----VFRMKGksgQPSRSYLFDPANNIDTGTAYLAILQNVYLGGITNPTSRRYA 294

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333965670 321 VIAGYNTGSGNVLRTFDNDRSRAFEQINRMQPQQVYQHLVRHLPFAETRRYMQKVTEFQRKY 382
Cdd:PRK11671 295 VITAYNGGAGSVLRVFSNDKIQAANIINTMSPGDVYQTLTTRHPSAESRRYLYKVNTAQKSY 356
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 117-382 2.53e-41

Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440504 [Multi-domain]  Cd Length: 244  Bit Score: 145.52  E-value: 2.53e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 117 LSEDRALLQRAIVTTLLTPDRPDQVDLLTDQPIQGGGQPFLYRLVRDHQGQFVQFEWRATQYAQHLVTNQRQTLNSRGQP 196
Cdd:COG0741    3 AAAAAAAALALAASAAAALALALLAAAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 197 RRYFVEFALSDQLDRQQQTKFADSVRRYSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRdaheLIYK 276
Cdd:COG0741   83 AALAAELLALAALLLRRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARR----LGLK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 277 RPGTPTRNYLFVPDNNIQMGVGYLSILDTRYLvrvNNPqsreYCVIAGYNTGSGNVLRTFDNDRSRAFEQInrmqpqqvy 356
Cdd:COG0741  159 LGLGPSPDDLFDPETNIRAGAAYLRELLDRFD---GDL----VLALAAYNAGPGRVRRWLRRNGDRDGEII--------- 222

                        250       260
                 ....*....|....*....|....*.
gi 333965670 357 qhlvrhlPFAETRRYMQKVTEFQRKY 382
Cdd:COG0741  223 -------PYAETRNYVKKVLANYAIY 241
Mltc_N pfam11873
Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found ...
 61-205 2.24e-39

Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found associated with pfam01464. It is the N-terminal structural domain of MltC (Membrane-bound lytic murein transglycosylase C), one of the seven lytic transglycosylases found in the genome of the Gram-negative bacterium Escherichia coli. The role of the N-terminal domain is suggested to be important not as a mere structural extension of the active site beyond what is seen in other lytic transglycosylases but one that creates a peptide-binding site at position +2.


Pssm-ID: 432150  Cd Length: 161  Bit Score: 137.77  E-value: 2.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670   61 EIDRLVRNQLQELAsflaRKWGDEK--TASPQEFVKYSNDFETRAIVNFETRLVRVESLS--EDRALLQRAIVTTLLTPD 136
Cdd:pfam11873   7 ALDILVGQFSGNIE----KIWGKNEvlVASKKDYVKYTDNYKSRAHIDFDKGIITIETLAtkNPKAHLRNAIITTLLTPD 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333965670  137 RPDQVDLLTDQPIQGGGQPFLYRLVRDHQGQFVQFEWRATQYAQHLVTNQRQTLNSRGQpRRYFVEFAL 205
Cdd:pfam11873  83 DPSDVDLYSDKDIELSGKPFLYGQVLDQDGQPIRWEWRANRFADYLIKNKLKTRKKNGK-KVYYVSIPM 150
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 221-345 1.17e-28

Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.


Pssm-ID: 396169 [Multi-domain]  Cd Length: 114  Bit Score: 107.78  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670  221 VRRYSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRdaheliYKRPGTPTRNYLFVPDNNIQMGVGYL 300
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKR------LGLRVNPGVDDLFDPEKNIKAGTKYL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 333965670  301 SILDTRYLVRVnnpqsreYCVIAGYNTGSGNVLRTFDNDRSRAFE 345
Cdd:pfam01464  75 KELYKQYGGDL-------WLALAAYNAGPGRVRKWIKNAGAKDKK 112
 
Name Accession Description Interval E-value
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 219-380 3.59e-101

membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and MltE are periplasmic, outer membrane attached lytic transglycosylases (LTs), which cleave beta-1,4-glycosidic bonds joining N-acetylmuramic acid and N-acetylglucosamine in the cell wall peptidoglycan, yielding 1,6-anhydromuropeptides. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda


Pssm-ID: 381614 [Multi-domain]  Cd Length: 162  Bit Score: 296.39  E-value: 3.59e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 219 DSVRRYSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRDAHELIYKRPGTPTRNYLFVPDNNIQMGVG 298
Cdd:cd16893    1 PIVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVYRLLGGKGGLPSKSYLFDPENNIDIGTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 299 YLSILDTRYLVRVNNPQSREYCVIAGYNTGSGNVLRTFDNDRSRAFEQINRMQPQQVYQHLVRHLPFAETRRYMQKVTEF 378
Cdd:cd16893   81 YLHILQNRYLKGIKNPKSREYCAIAAYNGGAGNVLRTFSSDRKKAISKINRLSPDEVYQHLTKKLPAAETRNYLKKVLKA 160


                 ..
gi 333965670 379 QR 380
Cdd:cd16893  161 KK 162
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
87-382 7.94e-99

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 297.73  E-value: 7.94e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670  87 ASPQEFVKYSNDFETRAIVNFETRLVRVESLS--EDRALLQRAIVTTLLTPDRPDQVDLLTDQ-PIQGGGQPFLYRLVRD 163
Cdd:PRK11671  60 AGPKDYVKYTDQYQTRSHINFDDGTITIETIAgtNPAAHLRQAIIKTLLMGDDPGSIDLYSDVdDIPISKEPFLYGQVLD 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 164 HQGQFVQFEWRATQYAQHLVTNQRQTLNSRGQPRRYFVEFALSDQLDRQQQtKFADSVRRYSRTYSIRPDLIYAIMEAES 243
Cdd:PRK11671 140 NTGQPIRWEGRASNFADYLLQNKLQSRSNGLRIIYSVTINMVPNHLDKRAH-KYLPMVRKASRKYGVDESLILAIMQTES 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 244 SFNPYAMSHIPAYGLMQIVPTTAGRDahelIYKRPG---TPTRNYLFVPDNNIQMGVGYLSILDTRYLVRVNNPQSREYC 320
Cdd:PRK11671 219 SFNPYAVSRSDALGLMQVVQHTAGKD----VFRMKGksgQPSRSYLFDPANNIDTGTAYLAILQNVYLGGITNPTSRRYA 294

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333965670 321 VIAGYNTGSGNVLRTFDNDRSRAFEQINRMQPQQVYQHLVRHLPFAETRRYMQKVTEFQRKY 382
Cdd:PRK11671 295 VITAYNGGAGSVLRVFSNDKIQAANIINTMSPGDVYQTLTTRHPSAESRRYLYKVNTAQKSY 356
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 117-382 2.53e-41

Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440504 [Multi-domain]  Cd Length: 244  Bit Score: 145.52  E-value: 2.53e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 117 LSEDRALLQRAIVTTLLTPDRPDQVDLLTDQPIQGGGQPFLYRLVRDHQGQFVQFEWRATQYAQHLVTNQRQTLNSRGQP 196
Cdd:COG0741    3 AAAAAAAALALAASAAAALALALLAAAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 197 RRYFVEFALSDQLDRQQQTKFADSVRRYSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRdaheLIYK 276
Cdd:COG0741   83 AALAAELLALAALLLRRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARR----LGLK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 277 RPGTPTRNYLFVPDNNIQMGVGYLSILDTRYLvrvNNPqsreYCVIAGYNTGSGNVLRTFDNDRSRAFEQInrmqpqqvy 356
Cdd:COG0741  159 LGLGPSPDDLFDPETNIRAGAAYLRELLDRFD---GDL----VLALAAYNAGPGRVRRWLRRNGDRDGEII--------- 222

                        250       260
                 ....*....|....*....|....*.
gi 333965670 357 qhlvrhlPFAETRRYMQKVTEFQRKY 382
Cdd:COG0741  223 -------PYAETRNYVKKVLANYAIY 241
Mltc_N pfam11873
Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found ...
 61-205 2.24e-39

Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found associated with pfam01464. It is the N-terminal structural domain of MltC (Membrane-bound lytic murein transglycosylase C), one of the seven lytic transglycosylases found in the genome of the Gram-negative bacterium Escherichia coli. The role of the N-terminal domain is suggested to be important not as a mere structural extension of the active site beyond what is seen in other lytic transglycosylases but one that creates a peptide-binding site at position +2.


Pssm-ID: 432150  Cd Length: 161  Bit Score: 137.77  E-value: 2.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670   61 EIDRLVRNQLQELAsflaRKWGDEK--TASPQEFVKYSNDFETRAIVNFETRLVRVESLS--EDRALLQRAIVTTLLTPD 136
Cdd:pfam11873   7 ALDILVGQFSGNIE----KIWGKNEvlVASKKDYVKYTDNYKSRAHIDFDKGIITIETLAtkNPKAHLRNAIITTLLTPD 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333965670  137 RPDQVDLLTDQPIQGGGQPFLYRLVRDHQGQFVQFEWRATQYAQHLVTNQRQTLNSRGQpRRYFVEFAL 205
Cdd:pfam11873  83 DPSDVDLYSDKDIELSGKPFLYGQVLDQDGQPIRWEWRANRFADYLIKNKLKTRKKNGK-KVYYVSIPM 150
emtA PRK15470
membrane-bound lytic murein transglycosylase EmtA;
228-375 3.44e-34

membrane-bound lytic murein transglycosylase EmtA;


Pssm-ID: 185367 [Multi-domain]  Cd Length: 203  Bit Score: 125.46  E-value: 3.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 228 YSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRDahelIYKR---PGTPTRNYLFVPDNNIQMGVGYLSILD 304
Cdd:PRK15470  50 WGVDPQLITAIIAIESGGNPNAVSKSNAIGLMQLKASTSGRD----VYRRmgwSGEPTTSELKNPERNISMGAAYLNILE 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333965670 305 TRYLVRVNNPQSREYCVIAGYNTGSGNVLRTFDNDRSRAFEQINRMQPQQVYQHLVRHLPFAETRRYMQKV 375
Cdd:PRK15470 126 TGPLAGIEDPKVLQYALVVSYANGAGALLRTFSSDRKKAISKINDLDADEFLEHVARNHPAPQAPRYIYKL 196
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 216-381 1.44e-33

uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized lytic transglycosylase (LT) with a conserved sequence pattern suggesting similarity to the Slt70, a 70kda soluble lytic transglycosylase which also has an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381617 [Multi-domain]  Cd Length: 146  Bit Score: 121.85  E-value: 1.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 216 KFADSVRRYSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAgrdahELIYKRPGTP--TRNYLFVPDNNI 293
Cdd:cd16896    3 KYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETA-----EWIAEKLGLEdfSEDDLYDPETNI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 294 QMGVGYLSILDTRYlvrvnnpQSREYCVIAGYNTGSGNVLR-TFDNDRSRAFEQINRMqpqqvyqhlvrhlPFAETRRYM 372
Cdd:cd16896   78 RLGTWYLSYLLKEF-------DGNLVLALAAYNAGPGNVDKwLKDGGWSGDGKTLDQI-------------PFPETRHYV 137


                 ....*....
gi 333965670 373 QKVTEFQRK 381
Cdd:cd16896  138 KKVLKNYKI 146
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 217-382 8.23e-30

70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381604 [Multi-domain]  Cd Length: 152  Bit Score: 112.18  E-value: 8.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 217 FADSVRRYSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRDAHELiyKRPGTPTRNyLFVPDNNIQMG 296
Cdd:cd13401    6 YRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVAKKL--GLPYYSPRD-LFDPEYNIRLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 297 VGYLSILDTRYlvrvnnPQSREYcVIAGYNTGSGNV---LRTFDNDRSRAF-EQInrmqpqqvyqhlvrhlPFAETRRYM 372
Cdd:cd13401   83 SAYLAELLDRF------DGNPVL-ALAAYNAGPGRVrrwLKRRGDLDPDLWiETI----------------PFSETRNYV 139

                        170
                 ....*....|
gi 333965670 373 QKVTEFQRKY 382
Cdd:cd13401  140 KRVLENYVVY 149
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 221-345 1.17e-28

Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.


Pssm-ID: 396169 [Multi-domain]  Cd Length: 114  Bit Score: 107.78  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670  221 VRRYSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRdaheliYKRPGTPTRNYLFVPDNNIQMGVGYL 300
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKR------LGLRVNPGVDDLFDPEKNIKAGTKYL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 333965670  301 SILDTRYLVRVnnpqsreYCVIAGYNTGSGNVLRTFDNDRSRAFE 345
Cdd:pfam01464  75 KELYKQYGGDL-------WLALAAYNAGPGRVRKWIKNAGAKDKK 112
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 232-375 1.11e-21

lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble membrane-bound LTs in bacteria and LTs in bacteriophage lambda. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381594 [Multi-domain]  Cd Length: 111  Bit Score: 88.81  E-value: 1.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 232 PDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAgrdaheliyKRPGTPTRNYLFVPDNNIQMGVGYLSILDTRYLVRV 311
Cdd:cd00254    1 PALVLAVIRVESGFNPRAVSPAGARGLMQLMPGTA---------RDLGRRGVDDLFDPEENIRAGARYLRELLDRFGGDL 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333965670 312 nnpqsreYCVIAGYNTGSGNVlrtfdnDRSRAFEQInrmqpqqvyqhlvrhlPFAETRRYMQKV 375
Cdd:cd00254   72 -------ELALAAYNAGPGAV------DRWGGGEVP----------------PYKETRNYVQRV 106
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 221-334 4.28e-15

membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily includes membrane-bound lytic murein transglycosylase F (MltF, murein lyase F) that degrades murein glycan strands. It is responsible for catalyzing the release of 1,6-anhydromuropeptides from peptidoglycan. Lytic transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do goose-type lysozymes. However, in addition, it also makes a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381606 [Multi-domain]  Cd Length: 161  Bit Score: 72.18  E-value: 4.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 221 VRRYSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAgrdaheliyKRPGTPTRnylFVPDNNIQMGVGYL 300
Cdd:cd13403    1 FKKYAEKYGFDWRLLAAQAYQESRFNPNARSPAGARGLMQLMPSTA---------RELGVNDR---LDPEQNIHAGAKYL 68

                         90       100       110
                 ....*....|....*....|....*....|....
gi 333965670 301 SILDTRYLvRVNNPQSREYCVIAGYNTGSGNVLR 334
Cdd:cd13403   69 RYLRDRFP-PDIDEPDRLKFALAAYNAGPGHVRD 101
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 197-334 1.40e-12

Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 68.55  E-value: 1.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 197 RRYF--VEFALSDQLDRQQQT--KFADSVRRYSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAgrdahe 272
Cdd:COG4623  240 ERYFghVKRDTRAFLRRIEGRlpPYDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPATA------ 313

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333965670 273 liyKRPGTPTRnylFVPDNNIQMGVGYLSILDTRYLVRVNNPQsREYCVIAGYNTGSGNVLR 334
Cdd:COG4623  314 ---KELGVDDR---LDPEQSIRAGAKYLRWLYDRFPEAIDEPD-RWWFALAAYNAGPGHVQD 368
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 219-375 1.85e-10

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 62.39  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 219 DSVRRYSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRDAHEliYKRPGTPTRNYLFVPDNNIQMGVG 298
Cdd:PRK11619 481 DEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKM--FSIPGYSSSSQLLDPETNINIGTS 558

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 299 YLSILDTRYlvrvnnPQSREYCViAGYNTGSGNVLRTFDNDRSR----AFeqinrmqpqqvyqhlVRHLPFAETRRYMQK 374
Cdd:PRK11619 559 YLEYVYQQF------GNNRILAS-AAYNAGPGRVRTWLGNSAGRidavAF---------------VESIPFSETRGYVKN 616


                 .
gi 333965670 375 V 375
Cdd:PRK11619 617 V 617
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 232-374 8.77e-07

Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381615 [Multi-domain]  Cd Length: 129  Bit Score: 47.51  E-value: 8.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 232 PDLIYaIMEAESSFNPYAMSHIPAYGLMQIVPTTAgrdaheliykrpgtptRNYLFVPDNNIqmgvgylsilDTR----- 306
Cdd:cd16894    8 EELKY-LALVESGFNPDAVSSAGAAGLWQFMPATA----------------REYGLRVDSWV----------DERrdpek 60

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333965670 307 -------YLVRVNNPQSREYCVIAGYNTGSGNVLRtfdndrsrafeQINRMQPQQVYQHLVRHLPfAETRRYMQK 374
Cdd:cd16894   61 straaarYLKDLYKRFGDWLLALAAYNAGEGRVRR-----------AIKRAGTDKWEDYYRLYLP-AETRRYVPK 123
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 228-261 1.31e-06

Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like protein, similar to Escherichia coli invasion protein IagB. IagB is encoded within a pathogenicity island in Salmonella enterica and has been shown to degrade polymeric peptidoglycan. IagB-like invasion proteins are implicated in the invasion of eukaryotic host cells by bacteria. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Members of this family resemble the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381603 [Multi-domain]  Cd Length: 109  Bit Score: 46.75  E-value: 1.31e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 333965670 228 YSIRPDLIYAIMEAESSFNPYAMSHIP----AYGLMQI 261
Cdd:cd13400    1 YGVPPRLLRAIAKVESGFNPNAINRNKngsyDIGLMQI 38
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 228-335 1.93e-06

Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic transglycosylase Slt35 and Pseudomonas aeruginosa Sltb1. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381602 [Multi-domain]  Cd Length: 108  Bit Score: 46.15  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 228 YSIRPDLIYAIMEAESSFNPYA-MSHIPAYGLMQIVPTTA---GRDAheliykrPGTPtRNYLFVPDNNIQMGVGYLSIL 303
Cdd:cd13399    1 YGVPPGILAAILGVESGFGPNAgGSPAGAQGIAQFMPSTWkayGVDG-------NGDG-KADPFNPEDAIASAANYLCRH 72

                         90       100       110
                 ....*....|....*....|....*....|..
gi 333965670 304 DTRYLVRVNNPQSReycVIAGYNTGSGNVLRT 335
Cdd:cd13399   73 GWDLNAFLGEDNFL---ALAAYNAGPGAYANA 101
PRK15328 PRK15328
type III secretion system invasion protein IagB;
214-307 2.72e-06

type III secretion system invasion protein IagB;


Pssm-ID: 185228 [Multi-domain]  Cd Length: 160  Bit Score: 46.78  E-value: 2.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 214 QTKFADSVRRYSRTYSIRPDLIYAIMEAESSFNPYAMSH----IPAYGLMQIvpttagRDAHELIYKRPGTPTRNYLFVP 289
Cdd:PRK15328  15 NTAWADCWLQAEKMFNIESELLYAIAQQESAMKPGAIGHnrdgSTDLGLMQI------NSFHMKRLKKMGISEKQLLQDP 88

                         90
                 ....*....|....*...
gi 333965670 290 DNNIQMGVGYLSILDTRY 307
Cdd:PRK15328  89 CISVIVGASILSDMMKIY 106
GEWL cd01021
Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; ...
 208-338 1.76e-04

Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; GEWL) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). Mammals have two lysozymes. This family corresponds to human and mouse lysozyme G-like protein 2.


Pssm-ID: 381601 [Multi-domain]  Cd Length: 174  Bit Score: 41.82  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 208 QLDRQQQTKFADSVRRYSRTYSIRPDLIYAIMEAESSF-----NPYAMSHIPAYGLMQIvpttaGRDAHELiykrPGTPT 282
Cdd:cd01021   28 ETDLNRLNKYKDCIKQVGKKLCIDPALIAAIISRESRAgaaldKNGWGDHGNGFGLMQV-----DKRYHPP----KGAWD 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 333965670 283 RnylfvpDNNIQMGVGYLsiLDTRYLVRVNNPQ-SREYCV---IAGYNTGSGNVlRTFDN 338
Cdd:cd01021   99 S------EEHIEQATGIL--IDFIKTVQRKHPSwSPEQQLkggIAAYNAGVGNV-QSYAG 149
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 242-268 4.49e-03

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 38.95  E-value: 4.49e-03
                         10        20
                 ....*....|....*....|....*..
gi 333965670 242 ESSFNPYAMSHIPAYGLMQIVPTTaGR 268
Cdd:PRK10783 128 ESAFDPHATSGANAAGIWQIIPST-GR 153
 
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.
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