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Conserved domains on  [gi|333821531|gb|AEG14194|]
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Lytic transglycosylase catalytic [Desulfofundulus kuznetsovii DSM 6115]

Protein Classification

lytic transglycosylase domain-containing protein( domain architecture ID 13014095)

lytic transglycosylase domain-containing protein similar to lytic transglycosylase which catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 37-182 4.96e-86

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: 249.73  E-value: 4.96e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  37 PFPYRETVMEYAAGRGLDPYLVAAVIKTESNFNPRATSRRGARGLMQVMPETGTWAAKKMGLSCYHPDLLYDPEFNIRIG 116
Cdd:cd16896    1 PLKYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAEWIAEKLGLEDFSEDDLYDPETNIRLG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333821531 117 TWYLADLYRTFDRDTILALAAYNGGQGNVQKWLEQQHWTGEKSKLDQIPFAETREFVRKVLWNYQV 182
Cdd:cd16896   81 TWYLSYLLKEFDGNLVLALAAYNAGPGNVDKWLKDGGWSGDGKTLDQIPFPETRHYVKKVLKNYKI 146
 
Name Accession Description Interval E-value
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 37-182 4.96e-86

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: 249.73  E-value: 4.96e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  37 PFPYRETVMEYAAGRGLDPYLVAAVIKTESNFNPRATSRRGARGLMQVMPETGTWAAKKMGLSCYHPDLLYDPEFNIRIG 116
Cdd:cd16896    1 PLKYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAEWIAEKLGLEDFSEDDLYDPETNIRLG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333821531 117 TWYLADLYRTFDRDTILALAAYNGGQGNVQKWLEQQHWTGEKSKLDQIPFAETREFVRKVLWNYQV 182
Cdd:cd16896   81 TWYLSYLLKEFDGNLVLALAAYNAGPGNVDKWLKDGGWSGDGKTLDQIPFPETRHYVKKVLKNYKI 146
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 33-185 4.16e-67

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: 205.23  E-value: 4.16e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  33 RLIYPFPYRETVMEYAAGRGLDPYLVAAVIKTESNFNPRATSRRGARGLMQVMPETGTWAAKKMGLScYHPDLLYDPEFN 112
Cdd:COG0741   96 LLRRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLG-PSPDDLFDPETN 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333821531 113 IRIGTWYLADLYRTFDRDTILALAAYNGGQGNVQKWLEQQHWtgekSKLDQIPFAETREFVRKVLWNYQVYRY 185
Cdd:COG0741  175 IRAGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWLRRNGD----RDGEIIPYAETRNYVKKVLANYAIYRA 243
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 46-158 1.41e-39

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: 130.89  E-value: 1.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531   46 EYAAGRGLDPYLVAAVIKTESNFNPRATSRRGARGLMQVMPETGTWAAKKMGLScyhPDLLYDPEFNIRIGTWYLADLYR 125
Cdd:pfam01464   3 KAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPG---VDDLFDPEKNIKAGTKYLKELYK 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 333821531  126 TFDRDTILALAAYNGGQGNVQKWLEQQHWTGEK 158
Cdd:pfam01464  80 QYGGDLWLALAAYNAGPGRVRKWIKNAGAKDKK 112
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 29-189 5.03e-34

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 126.71  E-value: 5.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  29 DHLGRLiYPFPYRETVMEYAAGRGLDPYLVAAVIKTESNFNPRATSRRGARGLMQVMPETGTWAAKKMGLSCY-HPDLLY 107
Cdd:PRK11619 469 DHLEER-FPLAWNDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFSIPGYsSSSQLL 547

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531 108 DPEFNIRIGTWYLADLYRTFDRDTILALAAYNGGQGNVQKWLEQQhwtgeKSKLD------QIPFAETREFVRKVLwNYQ 181
Cdd:PRK11619 548 DPETNINIGTSYLEYVYQQFGNNRILASAAYNAGPGRVRTWLGNS-----AGRIDavafveSIPFSETRGYVKNVL-AYD 621


                 ....*....
gi 333821531 182 V-YRYLYGR 189
Cdd:PRK11619 622 AyYRYFMGQ 630
 
Name Accession Description Interval E-value
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 37-182 4.96e-86

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: 249.73  E-value: 4.96e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  37 PFPYRETVMEYAAGRGLDPYLVAAVIKTESNFNPRATSRRGARGLMQVMPETGTWAAKKMGLSCYHPDLLYDPEFNIRIG 116
Cdd:cd16896    1 PLKYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAEWIAEKLGLEDFSEDDLYDPETNIRLG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333821531 117 TWYLADLYRTFDRDTILALAAYNGGQGNVQKWLEQQHWTGEKSKLDQIPFAETREFVRKVLWNYQV 182
Cdd:cd16896   81 TWYLSYLLKEFDGNLVLALAAYNAGPGNVDKWLKDGGWSGDGKTLDQIPFPETRHYVKKVLKNYKI 146
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 36-186 2.74e-69

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: 207.33  E-value: 2.74e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  36 YPFPYRETVMEYAAGRGLDPYLVAAVIKTESNFNPRATSRRGARGLMQVMPETGTWAAKKMGLSCYHPDLLYDPEFNIRI 115
Cdd:cd13401    2 YPLPYRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLPYYSPRDLFDPEYNIRL 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333821531 116 GTWYLADLYRTFDRDTILALAAYNGGQGNVQKWLEQqhwTGEKSKLD---QIPFAETREFVRKVLWNYQVYRYL 186
Cdd:cd13401   82 GSAYLAELLDRFDGNPVLALAAYNAGPGRVRRWLKR---RGDLDPDLwieTIPFSETRNYVKRVLENYVVYRAL 152
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 33-185 4.16e-67

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: 205.23  E-value: 4.16e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  33 RLIYPFPYRETVMEYAAGRGLDPYLVAAVIKTESNFNPRATSRRGARGLMQVMPETGTWAAKKMGLScYHPDLLYDPEFN 112
Cdd:COG0741   96 LLRRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLG-PSPDDLFDPETN 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333821531 113 IRIGTWYLADLYRTFDRDTILALAAYNGGQGNVQKWLEQQHWtgekSKLDQIPFAETREFVRKVLWNYQVYRY 185
Cdd:COG0741  175 IRAGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWLRRNGD----RDGEIIPYAETRNYVKKVLANYAIYRA 243
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 55-181 3.13e-48

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: 152.75  E-value: 3.13e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  55 PYLVAAVIKTESNFNPRATSRRGARGLMQVMPETGTWAAKKmglscyHPDLLYDPEFNIRIGTWYLADLYRTFDRDTILA 134
Cdd:cd00254    1 PALVLAVIRVESGFNPRAVSPAGARGLMQLMPGTARDLGRR------GVDDLFDPEENIRAGARYLRELLDRFGGDLELA 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 333821531 135 LAAYNGGQGNVQKWLEQQHwtgekskldqIPFAETREFVRKVLWNYQ 181
Cdd:cd00254   75 LAAYNAGPGAVDRWGGGEV----------PPYKETRNYVQRVLAYYQ 111
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 46-158 1.41e-39

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: 130.89  E-value: 1.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531   46 EYAAGRGLDPYLVAAVIKTESNFNPRATSRRGARGLMQVMPETGTWAAKKMGLScyhPDLLYDPEFNIRIGTWYLADLYR 125
Cdd:pfam01464   3 KAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPG---VDDLFDPEKNIKAGTKYLKELYK 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 333821531  126 TFDRDTILALAAYNGGQGNVQKWLEQQHWTGEK 158
Cdd:pfam01464  80 QYGGDLWLALAAYNAGPGRVRKWIKNAGAKDKK 112
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 29-189 5.03e-34

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 126.71  E-value: 5.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  29 DHLGRLiYPFPYRETVMEYAAGRGLDPYLVAAVIKTESNFNPRATSRRGARGLMQVMPETGTWAAKKMGLSCY-HPDLLY 107
Cdd:PRK11619 469 DHLEER-FPLAWNDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFSIPGYsSSSQLL 547

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531 108 DPEFNIRIGTWYLADLYRTFDRDTILALAAYNGGQGNVQKWLEQQhwtgeKSKLD------QIPFAETREFVRKVLwNYQ 181
Cdd:PRK11619 548 DPETNINIGTSYLEYVYQQFGNNRILASAAYNAGPGRVRTWLGNS-----AGRIDavafveSIPFSETRGYVKNVL-AYD 621


                 ....*....
gi 333821531 182 V-YRYLYGR 189
Cdd:PRK11619 622 AyYRYFMGQ 630
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 42-181 5.28e-34

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: 118.05  E-value: 5.28e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  42 ETVMEYAAGRGLDPYLVAAVIKTESNFNPRATSRRGARGLMQVMPET-GTWAAKKMGLS--CYHPDLLYDPEFNIRIGTW 118
Cdd:cd16893    1 PIVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTaGRDVYRLLGGKggLPSKSYLFDPENNIDIGTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531 119 YLADLYRTFDRDTI-------LALAAYNGGQGNVQKwleqqHWTGEKSK-LDQI----------------PFAETREFVR 174
Cdd:cd16893   81 YLHILQNRYLKGIKnpksreyCAIAAYNGGAGNVLR-----TFSSDRKKaISKInrlspdevyqhltkklPAAETRNYLK 155


                 ....*..
gi 333821531 175 KVLWNYQ 181
Cdd:cd16893  156 KVLKAKK 162
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 39-186 7.63e-33

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 121.32  E-value: 7.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  39 PYRETVMEYAAGRGLDPYLVAAVIKTESNFNPRATSRRGARGLMQVMPETgtwaAKKMGLscyhpDLLYDPEFNIRIGTW 118
Cdd:COG4623  263 PYDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPAT----AKELGV-----DDRLDPEQSIRAGAK 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531 119 YLADLYRTFDR------DTILALAAYNGGQGNVQK--------------WLEQQHWTGEKSKLDQIPFAETREFVRKVLW 178
Cdd:COG4623  334 YLRWLYDRFPEaidepdRWWFALAAYNAGPGHVQDarrlakkqgldpdrWFDVEKSQPKYYDTGYARGRETVNYVPNIRA 413


                 ....*...
gi 333821531 179 NYQVYRYL 186
Cdd:COG4623  414 YYDIYKRL 421
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 46-185 4.91e-28

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: 102.61  E-value: 4.91e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  46 EYAAGRGLDPYLVAAVIKTESNFNPRATSRRGARGLMQVMPETgtwaAKKMGLScyhpDlLYDPEFNIRIGTWYLADLYR 125
Cdd:cd13403    3 KYAEKYGFDWRLLAAQAYQESRFNPNARSPAGARGLMQLMPST----ARELGVN----D-RLDPEQNIHAGAKYLRYLRD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531 126 TFDRD------TILALAAYNGGQGNVQKW--LEQQH------WTGEKSKL----DQIPFA----------ETREFVRKVL 177
Cdd:cd13403   74 RFPPDidepdrLKFALAAYNAGPGHVRDArrLAKKYglnpnvWFDNVEVLpllkSPYYDPvvkygyargrETVNYVRNIR 153


                 ....*...
gi 333821531 178 WNYQVYRY 185
Cdd:cd13403  154 KYYDAYKQ 161
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 56-177 5.06e-21

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: 83.72  E-value: 5.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  56 YLvaAVIktESNFNPRATSRRGARGLMQVMPETgtwaAKKMGLSCYHP-DLLYDPEFNIRIGTWYLADLYRTFDrDTILA 134
Cdd:cd16894   12 YL--ALV--ESGFNPDAVSSAGAAGLWQFMPAT----AREYGLRVDSWvDERRDPEKSTRAAARYLKDLYKRFG-DWLLA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 333821531 135 LAAYNGGQGNVQKWLEQQHWTG-EKSKLDQIPfAETREFVRKVL 177
Cdd:cd16894   83 LAAYNAGEGRVRRAIKRAGTDKwEDYYRLYLP-AETRRYVPKFL 125
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
48-145 6.85e-16

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 74.32  E-value: 6.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  48 AAGR-GLDPYLVAAVIKTESNFNPRATSRRGARGLMQVMPETGTWAAKKMGLSCYHPD--LLYDPEFNIRIGTWYLADLy 124
Cdd:PRK11671 199 ASRKyGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHTAGKDVFRMKGKSGQPSrsYLFDPANNIDTGTAYLAIL- 277

                         90       100       110
                 ....*....|....*....|....*....|...
gi 333821531 125 rtfdRDTILA------------LAAYNGGQGNV 145
Cdd:PRK11671 278 ----QNVYLGgitnptsrryavITAYNGGAGSV 306
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
40-146 2.40e-14

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 70.29  E-value: 2.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  40 YRETVMEYAagRGLDPYLVAAVIKTESNFNPRATSRRGARGLMQVMPETgtwaAKKMGLScyhpDLLyDPEFNIRIGTWY 119
Cdd:PRK10859 290 YQPLFEKYA--GELDWRLLAAIAYQESHWNPQATSPTGVRGLMMLTRNT----AQSMGVT----DRL-DPEQSIRGGARY 358

                         90       100       110
                 ....*....|....*....|....*....|....
gi 333821531 120 LADLYRTFDrDTI-------LALAAYNGGQGNVQ 146
Cdd:PRK10859 359 LQDLMERLP-ESIpeperiwFALAAYNIGYGHML 391
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 52-141 5.15e-14

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: 64.86  E-value: 5.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  52 GLDPYLVAAVIKTESNFNPRATSRRGAR----GLMQV----MPETgtwaaKKMGLScyHPDLLYDPEFNIRIGTWYLADL 123
Cdd:cd13400    2 GVPPRLLRAIAKVESGFNPNAINRNKNGsydiGLMQInsiwLPEL-----ARYGIT--REELLNDPCTNIYVGAWILARN 74

                         90
                 ....*....|....*...
gi 333821531 124 YRTFdRDTILALAAYNGG 141
Cdd:cd13400   75 IKRY-GNTWKAVGAYNSG 91
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 52-144 1.24e-13

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: 63.87  E-value: 1.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  52 GLDPYLVAAVIKTESNFNPRA-TSRRGARGLMQVMPetGTWAAKKMGLSCYHPDLLYDPE--------FNIRIGtWYLAD 122
Cdd:cd13399    2 GVPPGILAAILGVESGFGPNAgGSPAGAQGIAQFMP--STWKAYGVDGNGDGKADPFNPEdaiasaanYLCRHG-WDLNA 78

                         90       100
                 ....*....|....*....|..
gi 333821531 123 LYrtfDRDTILALAAYNGGQGN 144
Cdd:cd13399   79 FL---GEDNFLALAAYNAGPGA 97
PHA00368 PHA00368
internal virion protein D
 37-143 9.70e-12

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 62.88  E-value: 9.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531   37 PFPYRETVMEYAAGRGLDPYLVAAVIKTESNFNPRATSRRGARGLMQVMPETGtwaaKKMGLSCYHPDlLYDPEFNIRIG 116
Cdd:PHA00368    8 PSEYDGLFQKAADAHGVSYDLLRKVGWDESRFNPTAKSPTGPKGLMQFTKATA----KALGLIVDDDD-RLDPELAIDAG 82

                          90       100
                  ....*....|....*....|....*..
gi 333821531  117 TWYLADLYRTFDRDTILALAAYNGGQG 143
Cdd:PHA00368   83 ARYLADLVGKYDGDELKAALAYNQGEG 109
emtA PRK15470
membrane-bound lytic murein transglycosylase EmtA;
12-187 2.55e-10

membrane-bound lytic murein transglycosylase EmtA;


Pssm-ID: 185367 [Multi-domain]  Cd Length: 203  Bit Score: 57.28  E-value: 2.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  12 KVRLFFFILSLLAILNIDH------------LGRLIYPFPYRETVmeyAAGRGLDPYLVAAVIKTESNFNPRATSRRGAR 79
Cdd:PRK15470   2 KLRWFAFLIVLLAGCSSKHdytnppwnakvpVQRAMQWMPISQKA---GAAWGVDPQLITAIIAIESGGNPNAVSKSNAI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  80 GLMQVMPET-GTWAAKKMGLSCyHPDL--LYDPEFNIRIGTWYLADL----YRTFDRDTILALA---AYNGGQGNVQKWL 149
Cdd:PRK15470  79 GLMQLKASTsGRDVYRRMGWSG-EPTTseLKNPERNISMGAAYLNILetgpLAGIEDPKVLQYAlvvSYANGAGALLRTF 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 333821531 150 EqqhwTGEKSKLDQIPFAETREFVRKVLWNY---QVYRYLY 187
Cdd:PRK15470 158 S----SDRKKAISKINDLDADEFLEHVARNHpapQAPRYIY 194
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 65-147 9.81e-10

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 56.67  E-value: 9.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  65 ESNFNPRATSRRGARGLMQVMPETGtwaaKKMGLScyhPDLLYDPEFNIRIGTWYLAD----LYRTFDRDTILALAAYNG 140
Cdd:PRK10783 128 ESAFDPHATSGANAAGIWQIIPSTG----RNYGLK---QTRWYDARRDVVASTTAALDmmqrLNKMFDGDWLLTVAAYNS 200


                 ....*..
gi 333821531 141 GQGNVQK 147
Cdd:PRK10783 201 GEGRVMK 207
PHA00658 PHA00658
putative lysin
 73-189 7.33e-09

putative lysin


Pssm-ID: 106967 [Multi-domain]  Cd Length: 720  Bit Score: 54.44  E-value: 7.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  73 TSRRGARGLMQVMPETGTWAAKKMGLSCYHPDLLYDPEFNIRIGTWYLADLYRTFDRDTILALAAYNGGQGNVQKWLEQQ 152
Cdd:PHA00658 325 TSPKGAVGIAQVMPDTAPEAAKLAGLPWDENRYRNDAAYNRALGMAYFQKQLRDFGGDLPKAYAAYNAGPGALQSALKDA 404

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 333821531 153 HwtgEKSKLDQIPfAETREFVRKvlwNYQVYRYLYGR 189
Cdd:PHA00658 405 K---DGNWLALLP-KETQDYVVK---NMQAYNAGQGR 434
LT_TF-like cd13402
lytic transglycosylase-like domain of tail fiber-like proteins and similar domains; These tail ...
 61-143 4.68e-07

lytic transglycosylase-like domain of tail fiber-like proteins and similar domains; These tail fiber-like proteins are multi-domain proteins that include a lytic transglycosylase (LT) domain. Members of the LT family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, and the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL). 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: 381605 [Multi-domain]  Cd Length: 117  Bit Score: 46.42  E-value: 4.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  61 VIKTESNFNPRAT------SRRG--ARGLMQVMPetGTWAAKKMGlscYHPDlLYDPEFNIRIGTWYLADLYrtfdrDTI 132
Cdd:cd13402    7 QIQTESGGNPNAInnwdsnAKAGhpSKGLMQVIP--PTFAAYAPP---GHGN-ILNPLDNILAAINYAKARY-----GSG 75

                         90
                 ....*....|.
gi 333821531 133 LALAAYNGGQG 143
Cdd:cd13402   76 FALAAGGGGGG 86
SLT COG3953
SLT domain protein [Mobilome: prophages, transposons];
58-141 8.18e-07

SLT domain protein [Mobilome: prophages, transposons];


Pssm-ID: 443153 [Multi-domain]  Cd Length: 325  Bit Score: 48.17  E-value: 8.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  58 VAAVIKTESNFNPRAT------SRRG--ARGLMQVMPetGTWAA-KKMGlscyHPDlLYDPEFNIRIGTWYLADLYRTFD 128
Cdd:COG3953  236 ILRIIQHESGGNPNAInlwdsnAAAGtpSKGLMQVIP--PTFNAyKLPG----HGN-IYNPVDNILAGINYAKSRYGSSD 308

                         90
                 ....*....|...
gi 333821531 129 RDTILALAAYNGG 141
Cdd:COG3953  309 NVPGLASLGQGGG 321
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 59-119 1.19e-04

lysozyme-like domains; This family contains several members, including soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, chitosanases, and pesticin. Typical members are involved in the hydrolysis of beta-1,4- linked polysaccharides.


Pssm-ID: 381596 [Multi-domain]  Cd Length: 59  Bit Score: 38.54  E-value: 1.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333821531  59 AAVIKTESNFNP--RATSRRGARGLMQVMPetGTWAAkkMGLSCyhPDLLYDPEFNIRIGTWY 119
Cdd:cd00442    3 AAIIGQESGGNKpaNAGSGSGAAGLFQFMP--GTWKA--YGKNS--SSDLNDPEASIEAAAKY 59
PRK15328 PRK15328
type III secretion system invasion protein IagB;
53-141 3.23e-04

type III secretion system invasion protein IagB;


Pssm-ID: 185228 [Multi-domain]  Cd Length: 160  Bit Score: 39.46  E-value: 3.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333821531  53 LDPYLVAAVIKTESNFNPRAT--SRRGAR--GLMQV----MPETgtwaaKKMGLSCYHpdLLYDPEFNIRIGTWYLADLY 124
Cdd:PRK15328  31 IESELLYAIAQQESAMKPGAIghNRDGSTdlGLMQInsfhMKRL-----KKMGISEKQ--LLQDPCISVIVGASILSDMM 103

                         90
                 ....*....|....*..
gi 333821531 125 RTFDRdTILALAAYNGG 141
Cdd:PRK15328 104 KIYGY-SWEAVGAYNAG 119
 
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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