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Conserved domains on  [gi|1097028230|emb|SFR56757|]
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membrane-bound lytic murein transglycosylase C [Thiomicrospira sp. ALE5]

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 2.34e-100

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: 294.47  E-value: 2.34e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 219 DSVRRHSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRDAHELIYKRPGTPTRDYLFVPDNNIQMGVG 298
Cdd:cd16893     1 PIVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVYRLLGGKGGLPSKSYLFDPENNIDIGTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 299 YLSILDTRYLVRVNNPLSREYCVIAGYNTGSGNVLRAFDNDRSRAFEQINRMQPQQVYQHLVRHLPFAETRRYMQKVTEF 378
Cdd:cd16893    81 YLHILQNRYLKGIKNPKSREYCAIAAYNGGAGNVLRTFSSDRKKAISKINRLSPDEVYQHLTKKLPAAETRNYLKKVLKA 160


                  ..
gi 1097028230 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 2.92e-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: 137.38  E-value: 2.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230  61 EIDRLVRDQLQELvsflARKWGDEK--TASPREFVKYSDDFETRAIVNFETRLVRVESLSDD--RAVLQKAIVTTLLTPD 136
Cdd:pfam11873   7 ALDILVGQFSGNI----EKIWGKNEvlVASKKDYVKYTDNYKSRAHIDFDKGIITIETLATKnpKAHLRNAIITTLLTPD 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1097028230 137 RPDQVDLLSDQPIRGSGQPFLYPLVRDHQGQIVQFEWRATQYAQHLANNQRQTLRQRGQPdRFFVEFAL 205
Cdd:pfam11873  83 DPSDVDLYSDKDIELSGKPFLYGQVLDQDGQPIRWEWRANRFADYLIKNKLKTRKKNGKK-VYYVSIPM 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 2.34e-100

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: 294.47  E-value: 2.34e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 219 DSVRRHSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRDAHELIYKRPGTPTRDYLFVPDNNIQMGVG 298
Cdd:cd16893     1 PIVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVYRLLGGKGGLPSKSYLFDPENNIDIGTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 299 YLSILDTRYLVRVNNPLSREYCVIAGYNTGSGNVLRAFDNDRSRAFEQINRMQPQQVYQHLVRHLPFAETRRYMQKVTEF 378
Cdd:cd16893    81 YLHILQNRYLKGIKNPKSREYCAIAAYNGGAGNVLRTFSSDRKKAISKINRLSPDEVYQHLTKKLPAAETRNYLKKVLKA 160


                  ..
gi 1097028230 379 QR 380
Cdd:cd16893   161 KK 162
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
87-382 1.23e-99

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 299.66  E-value: 1.23e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230  87 ASPREFVKYSDDFETRAIVNFETRLVRVESLSDD--RAVLQKAIVTTLLTPDRPDQVDLLSDQ---PIrgSGQPFLYPLV 161
Cdd:PRK11671   60 AGPKDYVKYTDQYQTRSHINFDDGTITIETIAGTnpAAHLRQAIIKTLLMGDDPGSIDLYSDVddiPI--SKEPFLYGQV 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 162 RDHQGQIVQFEWRATQYAQHLANNQRQTlRQRGQPDRFFVEFALSA-QLDRQQQtKFADSVRRHSRTYSIRPDLIYAIME 240
Cdd:PRK11671  138 LDNTGQPIRWEGRASNFADYLLQNKLQS-RSNGLRIIYSVTINMVPnHLDKRAH-KYLPMVRKASRKYGVDESLILAIMQ 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 241 AESSFNPYAMSHIPAYGLMQIVPTTAGRDahelIYKRPG---TPTRDYLFVPDNNIQMGVGYLSILDTRYLVRVNNPLSR 317
Cdd:PRK11671  216 TESSFNPYAVSRSDALGLMQVVQHTAGKD----VFRMKGksgQPSRSYLFDPANNIDTGTAYLAILQNVYLGGITNPTSR 291

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1097028230 318 EYCVIAGYNTGSGNVLRAFDNDRSRAFEQINRMQPQQVYQHLVRHLPFAETRRYMQKVTEFQRKY 382
Cdd:PRK11671  292 RYAVITAYNGGAGSVLRVFSNDKIQAANIINTMSPGDVYQTLTTRHPSAESRRYLYKVNTAQKSY 356
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 172-382 1.95e-42

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: 148.60  E-value: 1.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 172 EWRATQYAQHLANNQRQTLRQRGQPDRFFVEFALSAQLDRQQQTKFADSVRRHSRTYSIRPDLIYAIMEAESSFNPYAMS 251
Cdd:COG0741    58 SAAAGGPALAAALAAADALAAFAAIAALAAELLALAALLLRRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVS 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 252 HIPAYGLMQIVPTTAGRdaheLIYKRPGTPTRDYLFVPDNNIQMGVGYLSILDTRYLvrvNNPlsreYCVIAGYNTGSGN 331
Cdd:COG0741   138 PAGARGLMQLMPATARR----LGLKLGLGPSPDDLFDPETNIRAGAAYLRELLDRFD---GDL----VLALAAYNAGPGR 206

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1097028230 332 VLRAFDNDRSRAFEQInrmqpqqvyqhlvrhlPFAETRRYMQKVTEFQRKY 382
Cdd:COG0741   207 VRRWLRRNGDRDGEII----------------PYAETRNYVKKVLANYAIY 241
Mltc_N pfam11873
Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found ...
 61-205 2.92e-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: 137.38  E-value: 2.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230  61 EIDRLVRDQLQELvsflARKWGDEK--TASPREFVKYSDDFETRAIVNFETRLVRVESLSDD--RAVLQKAIVTTLLTPD 136
Cdd:pfam11873   7 ALDILVGQFSGNI----EKIWGKNEvlVASKKDYVKYTDNYKSRAHIDFDKGIITIETLATKnpKAHLRNAIITTLLTPD 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1097028230 137 RPDQVDLLSDQPIRGSGQPFLYPLVRDHQGQIVQFEWRATQYAQHLANNQRQTLRQRGQPdRFFVEFAL 205
Cdd:pfam11873  83 DPSDVDLYSDKDIELSGKPFLYGQVLDQDGQPIRWEWRANRFADYLIKNKLKTRKKNGKK-VYYVSIPM 150
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 225-345 6.76e-29

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: 108.55  E-value: 6.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 225 SRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRdaheliYKRPGTPTRDYLFVPDNNIQMGVGYLSILD 304
Cdd:pfam01464   5 AQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKR------LGLRVNPGVDDLFDPEKNIKAGTKYLKELY 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1097028230 305 TRYLVRVnnplsreYCVIAGYNTGSGNVLRAFDNDRSRAFE 345
Cdd:pfam01464  79 KQYGGDL-------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 2.34e-100

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: 294.47  E-value: 2.34e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 219 DSVRRHSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRDAHELIYKRPGTPTRDYLFVPDNNIQMGVG 298
Cdd:cd16893     1 PIVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVYRLLGGKGGLPSKSYLFDPENNIDIGTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 299 YLSILDTRYLVRVNNPLSREYCVIAGYNTGSGNVLRAFDNDRSRAFEQINRMQPQQVYQHLVRHLPFAETRRYMQKVTEF 378
Cdd:cd16893    81 YLHILQNRYLKGIKNPKSREYCAIAAYNGGAGNVLRTFSSDRKKAISKINRLSPDEVYQHLTKKLPAAETRNYLKKVLKA 160


                  ..
gi 1097028230 379 QR 380
Cdd:cd16893   161 KK 162
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
87-382 1.23e-99

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 299.66  E-value: 1.23e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230  87 ASPREFVKYSDDFETRAIVNFETRLVRVESLSDD--RAVLQKAIVTTLLTPDRPDQVDLLSDQ---PIrgSGQPFLYPLV 161
Cdd:PRK11671   60 AGPKDYVKYTDQYQTRSHINFDDGTITIETIAGTnpAAHLRQAIIKTLLMGDDPGSIDLYSDVddiPI--SKEPFLYGQV 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 162 RDHQGQIVQFEWRATQYAQHLANNQRQTlRQRGQPDRFFVEFALSA-QLDRQQQtKFADSVRRHSRTYSIRPDLIYAIME 240
Cdd:PRK11671  138 LDNTGQPIRWEGRASNFADYLLQNKLQS-RSNGLRIIYSVTINMVPnHLDKRAH-KYLPMVRKASRKYGVDESLILAIMQ 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 241 AESSFNPYAMSHIPAYGLMQIVPTTAGRDahelIYKRPG---TPTRDYLFVPDNNIQMGVGYLSILDTRYLVRVNNPLSR 317
Cdd:PRK11671  216 TESSFNPYAVSRSDALGLMQVVQHTAGKD----VFRMKGksgQPSRSYLFDPANNIDTGTAYLAILQNVYLGGITNPTSR 291

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1097028230 318 EYCVIAGYNTGSGNVLRAFDNDRSRAFEQINRMQPQQVYQHLVRHLPFAETRRYMQKVTEFQRKY 382
Cdd:PRK11671  292 RYAVITAYNGGAGSVLRVFSNDKIQAANIINTMSPGDVYQTLTTRHPSAESRRYLYKVNTAQKSY 356
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 172-382 1.95e-42

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: 148.60  E-value: 1.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 172 EWRATQYAQHLANNQRQTLRQRGQPDRFFVEFALSAQLDRQQQTKFADSVRRHSRTYSIRPDLIYAIMEAESSFNPYAMS 251
Cdd:COG0741    58 SAAAGGPALAAALAAADALAAFAAIAALAAELLALAALLLRRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVS 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 252 HIPAYGLMQIVPTTAGRdaheLIYKRPGTPTRDYLFVPDNNIQMGVGYLSILDTRYLvrvNNPlsreYCVIAGYNTGSGN 331
Cdd:COG0741   138 PAGARGLMQLMPATARR----LGLKLGLGPSPDDLFDPETNIRAGAAYLRELLDRFD---GDL----VLALAAYNAGPGR 206

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1097028230 332 VLRAFDNDRSRAFEQInrmqpqqvyqhlvrhlPFAETRRYMQKVTEFQRKY 382
Cdd:COG0741   207 VRRWLRRNGDRDGEII----------------PYAETRNYVKKVLANYAIY 241
Mltc_N pfam11873
Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found ...
 61-205 2.92e-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: 137.38  E-value: 2.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230  61 EIDRLVRDQLQELvsflARKWGDEK--TASPREFVKYSDDFETRAIVNFETRLVRVESLSDD--RAVLQKAIVTTLLTPD 136
Cdd:pfam11873   7 ALDILVGQFSGNI----EKIWGKNEvlVASKKDYVKYTDNYKSRAHIDFDKGIITIETLATKnpKAHLRNAIITTLLTPD 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1097028230 137 RPDQVDLLSDQPIRGSGQPFLYPLVRDHQGQIVQFEWRATQYAQHLANNQRQTLRQRGQPdRFFVEFAL 205
Cdd:pfam11873  83 DPSDVDLYSDKDIELSGKPFLYGQVLDQDGQPIRWEWRANRFADYLIKNKLKTRKKNGKK-VYYVSIPM 150
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 216-381 1.02e-32

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: 119.54  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 216 KFADSVRRHSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAgrdahELIYKRPGTP--TRDYLFVPDNNI 293
Cdd:cd16896     3 KYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETA-----EWIAEKLGLEdfSEDDLYDPETNI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 294 QMGVGYLSILDTRYlvrvnnpLSREYCVIAGYNTGSGNVLR-AFDNDRSRAFEQINRMqpqqvyqhlvrhlPFAETRRYM 372
Cdd:cd16896    78 RLGTWYLSYLLKEF-------DGNLVLALAAYNAGPGNVDKwLKDGGWSGDGKTLDQI-------------PFPETRHYV 137


                  ....*....
gi 1097028230 373 QKVTEFQRK 381
Cdd:cd16896   138 KKVLKNYKI 146
emtA PRK15470
membrane-bound lytic murein transglycosylase EmtA;
228-375 5.52e-32

membrane-bound lytic murein transglycosylase EmtA;


Pssm-ID: 185367 [Multi-domain]  Cd Length: 203  Bit Score: 119.68  E-value: 5.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 228 YSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRDahelIYKR---PGTPTRDYLFVPDNNIQMGVGYLSILD 304
Cdd:PRK15470   50 WGVDPQLITAIIAIESGGNPNAVSKSNAIGLMQLKASTSGRD----VYRRmgwSGEPTTSELKNPERNISMGAAYLNILE 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1097028230 305 TRYLVRVNNPLSREYCVIAGYNTGSGNVLRAFDNDRSRAFEQINRMQPQQVYQHLVRHLPFAETRRYMQKV 375
Cdd:PRK15470  126 TGPLAGIEDPKVLQYALVVSYANGAGALLRTFSSDRKKAISKINDLDADEFLEHVARNHPAPQAPRYIYKL 196
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 217-382 1.75e-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: 114.11  E-value: 1.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 217 FADSVRRHSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRDAHELiyKRPGTPTRDyLFVPDNNIQMG 296
Cdd:cd13401     6 YRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVAKKL--GLPYYSPRD-LFDPEYNIRLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 297 VGYLSILDTRYlvrVNNPLsreyCVIAGYNTGSGNV---LRAFDNDRSRAF-EQInrmqpqqvyqhlvrhlPFAETRRYM 372
Cdd:cd13401    83 SAYLAELLDRF---DGNPV----LALAAYNAGPGRVrrwLKRRGDLDPDLWiETI----------------PFSETRNYV 139

                         170
                  ....*....|
gi 1097028230 373 QKVTEFQRKY 382
Cdd:cd13401   140 KRVLENYVVY 149
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 225-345 6.76e-29

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: 108.55  E-value: 6.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 225 SRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRdaheliYKRPGTPTRDYLFVPDNNIQMGVGYLSILD 304
Cdd:pfam01464   5 AQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKR------LGLRVNPGVDDLFDPEKNIKAGTKYLKELY 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1097028230 305 TRYLVRVnnplsreYCVIAGYNTGSGNVLRAFDNDRSRAFE 345
Cdd:pfam01464  79 KQYGGDL-------WLALAAYNAGPGRVRKWIKNAGAKDKK 112
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 232-375 7.34e-23

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: 92.28  E-value: 7.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 232 PDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAgrdaheliyKRPGTPTRDYLFVPDNNIQMGVGYLSILDTRYLVRV 311
Cdd:cd00254     1 PALVLAVIRVESGFNPRAVSPAGARGLMQLMPGTA---------RDLGRRGVDDLFDPEENIRAGARYLRELLDRFGGDL 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1097028230 312 nnplsreYCVIAGYNTGSGNVLRAFDNdrsrafeqinrmqpqqvyqhlvRHLPFAETRRYMQKV 375
Cdd:cd00254    72 -------ELALAAYNAGPGAVDRWGGG----------------------EVPPYKETRNYVQRV 106
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 221-335 2.33e-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: 72.95  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 221 VRRHSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAgrdaheliyKRPGTPTRdylFVPDNNIQMGVGYL 300
Cdd:cd13403     1 FKKYAEKYGFDWRLLAAQAYQESRFNPNARSPAGARGLMQLMPSTA---------RELGVNDR---LDPEQNIHAGAKYL 68

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1097028230 301 SILDTRYlVRVNNPLSREYCVIAGYNTGSGNVLRA 335
Cdd:cd13403    69 RYLRDRF-PPDIDEPDRLKFALAAYNAGPGHVRDA 102
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 216-335 3.78e-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: 67.39  E-value: 3.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 216 KFADSVRRHSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAgrdaheliyKRPGTPTRdylFVPDNNIQM 295
Cdd:COG4623   263 PYDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPATA---------KELGVDDR---LDPEQSIRA 330

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1097028230 296 GVGYLSILDTRYLVRVNNPlSREYCVIAGYNTGSGNVLRA 335
Cdd:COG4623   331 GAKYLRWLYDRFPEAIDEP-DRWWFALAAYNAGPGHVQDA 369
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 219-375 1.23e-09

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 59.69  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 219 DSVRRHSRTYSIRPDLIYAIMEAESSFNPYAMSHIPAYGLMQIVPTTAGRDAHEliYKRPGTPTRDYLFVPDNNIQMGVG 298
Cdd:PRK11619  481 DEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKM--FSIPGYSSSSQLLDPETNINIGTS 558

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 299 YLSILDTRYlvRVNNPLSReycviAGYNTGSGNVLRAFDNDRSR----AFeqinrmqpqqvyqhlVRHLPFAETRRYMQK 374
Cdd:PRK11619  559 YLEYVYQQF--GNNRILAS-----AAYNAGPGRVRTWLGNSAGRidavAF---------------VESIPFSETRGYVKN 616


                  .
gi 1097028230 375 V 375
Cdd:PRK11619  617 V 617
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 232-374 3.44e-08

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: 51.75  E-value: 3.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 232 PDLIYaIMEAESSFNPYAMSHIPAYGLMQIVPTTAgrdaheliykrpgtptRDYLFVPDNNIqmgvgylsilDTR----- 306
Cdd:cd16894     8 EELKY-LALVESGFNPDAVSSAGAAGLWQFMPATA----------------REYGLRVDSWV----------DERrdpek 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1097028230 307 -------YLVRVNNPLSREYCVIAGYNTGSGNVLRAFDNDRSRAFEQINRMqpqqvyqhlvrHLPfAETRRYMQK 374
Cdd:cd16894    61 straaarYLKDLYKRFGDWLLALAAYNAGEGRVRRAIKRAGTDKWEDYYRL-----------YLP-AETRRYVPK 123
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 228-301 3.84e-07

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: 48.29  E-value: 3.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 228 YSIRPDLIYAIMEAESSFNPYAMSHIP----AYGLMQI----VPTTAgrdaheliyKRPGTPTRDyLFVPDNNIQMGVGY 299
Cdd:cd13400     1 YGVPPRLLRAIAKVESGFNPNAINRNKngsyDIGLMQInsiwLPELA---------RYGITREEL-LNDPCTNIYVGAWI 70


                  ..
gi 1097028230 300 LS 301
Cdd:cd13400    71 LA 72
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 228-335 5.71e-07

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: 47.69  E-value: 5.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 228 YSIRPDLIYAIMEAESSFNPYA-MSHIPAYGLMQIVPTTA---GRDAheliykrPGTPTRDYLFVPDNNIQMGvGYLSIL 303
Cdd:cd13399     1 YGVPPGILAAILGVESGFGPNAgGSPAGAQGIAQFMPSTWkayGVDG-------NGDGKADPFNPEDAIASAA-NYLCRH 72

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1097028230 304 DTRYLVRVNNPLSReycVIAGYNTGSGNVLRA 335
Cdd:cd13399    73 GWDLNAFLGEDNFL---ALAAYNAGPGAYANA 101
PRK15328 PRK15328
type III secretion system invasion protein IagB;
214-307 2.82e-06

type III secretion system invasion protein IagB;


Pssm-ID: 185228 [Multi-domain]  Cd Length: 160  Bit Score: 46.78  E-value: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 214 QTKFADSVRRHSRTYSIRPDLIYAIMEAESSFNPYAMSH----IPAYGLMQIvpttagRDAHELIYKRPGTPTRDYLFVP 289
Cdd:PRK15328   15 NTAWADCWLQAEKMFNIESELLYAIAQQESAMKPGAIGHnrdgSTDLGLMQI------NSFHMKRLKKMGISEKQLLQDP 88

                          90
                  ....*....|....*...
gi 1097028230 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; ...
 207-332 1.96e-05

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: 44.51  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 207 AQLDRQQQTKFADSVRRHSRTYSIRPDLIYAIMEAESSF-----NPYAMSHIPAYGLMQIvpttaGRDAHELiykrPGTP 281
Cdd:cd01021    27 AETDLNRLNKYKDCIKQVGKKLCIDPALIAAIISRESRAgaaldKNGWGDHGNGFGLMQV-----DKRYHPP----KGAW 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1097028230 282 -TRDylfvpdnNIQMGVGYLsiLDTRYLVRVNNP-LSREYCV---IAGYNTGSGNV 332
Cdd:cd01021    98 dSEE-------HIEQATGIL--IDFIKTVQRKHPsWSPEQQLkggIAAYNAGVGNV 144
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 242-342 1.54e-03

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 40.49  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097028230 242 ESSFNPYAMSHIPAYGLMQIVPTTaGRDaHELiykrpgTPTRDYlfvpDNNIQMGVGYLSILDTryLVRVNNPLSREYCV 321
Cdd:PRK10783  128 ESAFDPHATSGANAAGIWQIIPST-GRN-YGL------KQTRWY----DARRDVVASTTAALDM--MQRLNKMFDGDWLL 193

                          90       100
                  ....*....|....*....|..
gi 1097028230 322 -IAGYNTGSGNVLRAFDNDRSR 342
Cdd:PRK10783  194 tVAAYNSGEGRVMKAIKANKAK 215
 
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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