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Conserved domains on  [gi|152929603|gb|ABS35103|]
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transglycosylase SLT domain protein [Clostridium botulinum A str. ATCC 19397]

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 ...
 22-167 4.71e-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: 248.96  E-value: 4.71e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  22 PIKYRDYIDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGEWVAEKMGMKDFNIDDLKDPETNIKMG 101
Cdd:cd16896    1 PLKYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAEWIAEKLGLEDFSEDDLYDPETNIRLG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152929603 102 CWYLNNLKEEFDGNMDLVLAAYNGGRGNVQKWLKDSEHSKDGESLHYIPFKETDKYVKKVKAIYNI 167
Cdd:cd16896   81 TWYLSYLLKEFDGNLVLALAAYNAGPGNVDKWLKDGGWSGDGKTLDQIPFPETRHYVKKVLKNYKI 146
 
Name Accession Description Interval E-value
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 22-167 4.71e-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: 248.96  E-value: 4.71e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  22 PIKYRDYIDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGEWVAEKMGMKDFNIDDLKDPETNIKMG 101
Cdd:cd16896    1 PLKYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAEWIAEKLGLEDFSEDDLYDPETNIRLG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152929603 102 CWYLNNLKEEFDGNMDLVLAAYNGGRGNVQKWLKDSEHSKDGESLHYIPFKETDKYVKKVKAIYNI 167
Cdd:cd16896   81 TWYLSYLLKEFDGNLVLALAAYNAGPGNVDKWLKDGGWSGDGKTLDQIPFPETRHYVKKVLKNYKI 146
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 21-169 1.73e-66

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: 203.30  E-value: 1.73e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  21 FPIKYRDYIDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGEWVAEKMGMKdFNIDDLKDPETNIKM 100
Cdd:COG0741   99 RPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLG-PSPDDLFDPETNIRA 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 152929603 101 GCWYLNNLKEEFDGNMDLVLAAYNGGRGNVQKWLKDSEHSkDGESlhyIPFKETDKYVKKVKAIYNIYR 169
Cdd:COG0741  178 GAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWLRRNGDR-DGEI---IPYAETRNYVKKVLANYAIYR 242
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 29-135 4.51e-32

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: 111.24  E-value: 4.51e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603   29 IDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGEWVAEKMGMKdfnIDDLKDPETNIKMGCWYLNNL 108
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPG---VDDLFDPEKNIKAGTKYLKEL 77

                          90       100
                  ....*....|....*....|....*..
gi 152929603  109 KEEFDGNMDLVLAAYNGGRGNVQKWLK 135
Cdd:pfam01464  78 YKQYGGDLWLALAAYNAGPGRVRKWIK 104
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 21-171 1.06e-25

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 102.45  E-value: 1.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  21 FPIKYRDYIDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGEWVAEKMGMKDF-NIDDLKDPETNIK 99
Cdd:PRK11619 475 FPLAWNDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFSIPGYsSSSQLLDPETNIN 554

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152929603 100 MGCWYLNNLKEEFDGNMDLVLAAYNGGRGNVQKWLKDSEHSKDG----ESlhyIPFKETDKYVKKVKAIYNIYRFL 171
Cdd:PRK11619 555 IGTSYLEYVYQQFGNNRILASAAYNAGPGRVRTWLGNSAGRIDAvafvES---IPFSETRGYVKNVLAYDAYYRYF 627
 
Name Accession Description Interval E-value
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 22-167 4.71e-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: 248.96  E-value: 4.71e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  22 PIKYRDYIDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGEWVAEKMGMKDFNIDDLKDPETNIKMG 101
Cdd:cd16896    1 PLKYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAEWIAEKLGLEDFSEDDLYDPETNIRLG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152929603 102 CWYLNNLKEEFDGNMDLVLAAYNGGRGNVQKWLKDSEHSKDGESLHYIPFKETDKYVKKVKAIYNI 167
Cdd:cd16896   81 TWYLSYLLKEFDGNLVLALAAYNAGPGNVDKWLKDGGWSGDGKTLDQIPFPETRHYVKKVLKNYKI 146
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 21-169 1.73e-66

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: 203.30  E-value: 1.73e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  21 FPIKYRDYIDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGEWVAEKMGMKdFNIDDLKDPETNIKM 100
Cdd:COG0741   99 RPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLG-PSPDDLFDPETNIRA 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 152929603 101 GCWYLNNLKEEFDGNMDLVLAAYNGGRGNVQKWLKDSEHSkDGESlhyIPFKETDKYVKKVKAIYNIYR 169
Cdd:COG0741  178 GAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWLRRNGDR-DGEI---IPYAETRNYVKKVLANYAIYR 242
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 21-171 1.83e-58

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: 179.59  E-value: 1.83e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  21 FPIKYRDYIDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGEWVAEKMGMKDFNIDDLKDPETNIKM 100
Cdd:cd13401    2 YPLPYRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLPYYSPRDLFDPEYNIRL 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 152929603 101 GCWYLNNLKEEFDGNMDLVLAAYNGGRGNVQKWLKDSEHSKDGESLHYIPFKETDKYVKKVKAIYNIYRFL 171
Cdd:cd13401   82 GSAYLAELLDRFDGNPVLALAAYNAGPGRVRRWLKRRGDLDPDLWIETIPFSETRNYVKRVLENYVVYRAL 152
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 40-166 2.10e-42

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: 137.34  E-value: 2.10e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  40 PYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGEWVAEKmgmkdfNIDDLKDPETNIKMGCWYLNNLKEEFDGNMDLV 119
Cdd:cd00254    1 PALVLAVIRVESGFNPRAVSPAGARGLMQLMPGTARDLGRR------GVDDLFDPEENIRAGARYLRELLDRFGGDLELA 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 152929603 120 LAAYNGGRGNVQKWLKDsehskdgeslHYIPFKETDKYVKKVKAIYN 166
Cdd:cd00254   75 LAAYNAGPGAVDRWGGG----------EVPPYKETRNYVQRVLAYYQ 111
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 29-135 4.51e-32

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: 111.24  E-value: 4.51e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603   29 IDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGEWVAEKMGMKdfnIDDLKDPETNIKMGCWYLNNL 108
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPG---VDDLFDPEKNIKAGTKYLKEL 77

                          90       100
                  ....*....|....*....|....*..
gi 152929603  109 KEEFDGNMDLVLAAYNGGRGNVQKWLK 135
Cdd:pfam01464  78 YKQYGGDLWLALAAYNAGPGRVRKWIK 104
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 24-171 2.40e-29

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 111.31  E-value: 2.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  24 KYRDYIDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGEWvaekmgmkdFNIDDLKDPETNIKMGCW 103
Cdd:COG4623  263 PYDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPATAKE---------LGVDDRLDPEQSIRAGAK 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603 104 YLNNLKEEFDGNMD------LVLAAYNGGRGNVQK--------------WLKDSEHSKDGESLHYIPFKETDKYVKKVKA 163
Cdd:COG4623  334 YLRWLYDRFPEAIDepdrwwFALAAYNAGPGHVQDarrlakkqgldpdrWFDVEKSQPKYYDTGYARGRETVNYVPNIRA 413


                 ....*...
gi 152929603 164 IYNIYRFL 171
Cdd:COG4623  414 YYDIYKRL 421
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 27-166 1.15e-27

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: 101.48  E-value: 1.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  27 DYIDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPET-GEWVAEKMGMKD--FNIDDLKDPETNIKMGCW 103
Cdd:cd16893    1 PIVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTaGRDVYRLLGGKGglPSKSYLFDPENNIDIGTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603 104 YLNNLKEEFDGNMD-------LVLAAYNGGRGNVQKWL-KDSEHSKD-------GESLHYI----PFKETDKYVKKVKAI 164
Cdd:cd16893   81 YLHILQNRYLKGIKnpksreyCAIAAYNGGAGNVLRTFsSDRKKAISkinrlspDEVYQHLtkklPAAETRNYLKKVLKA 160


                 ..
gi 152929603 165 YN 166
Cdd:cd16893  161 KK 162
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 32-169 2.76e-26

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: 97.61  E-value: 2.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  32 YANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGewvaekmgmKDFNIDDLKDPETNIKMGCWYLNNLKEE 111
Cdd:cd13403    4 YAEKYGFDWRLLAAQAYQESRFNPNARSPAGARGLMQLMPSTA---------RELGVNDRLDPEQNIHAGAKYLRYLRDR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603 112 FDGNMD------LVLAAYNGGRGNVQ--------------KWLKDSEHSKDGESLHYIPF--------KETDKYVKKVKA 163
Cdd:cd13403   75 FPPDIDepdrlkFALAAYNAGPGHVRdarrlakkyglnpnVWFDNVEVLPLLKSPYYDPVvkygyargRETVNYVRNIRK 154


                 ....*.
gi 152929603 164 IYNIYR 169
Cdd:cd13403  155 YYDAYK 160
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 21-171 1.06e-25

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 102.45  E-value: 1.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  21 FPIKYRDYIDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGEWVAEKMGMKDF-NIDDLKDPETNIK 99
Cdd:PRK11619 475 FPLAWNDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFSIPGYsSSSQLLDPETNIN 554

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152929603 100 MGCWYLNNLKEEFDGNMDLVLAAYNGGRGNVQKWLKDSEHSKDG----ESlhyIPFKETDKYVKKVKAIYNIYRFL 171
Cdd:PRK11619 555 IGTSYLEYVYQQFGNNRILASAAYNAGPGRVRTWLGNSAGRIDAvafvES---IPFSETRGYVKNVLAYDAYYRYF 627
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 50-164 2.09e-18

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: 76.40  E-value: 2.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  50 ESNFKKDAASKKNAQGLMQITPETgewvAEKMGMK-DFNIDDLKDPETNIKMGCWYLNNLKEEFdGNMDLVLAAYNGGRG 128
Cdd:cd16894   17 ESGFNPDAVSSAGAAGLWQFMPAT----AREYGLRvDSWVDERRDPEKSTRAAARYLKDLYKRF-GDWLLALAAYNAGEG 91

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 152929603 129 NVQKWLKDSEHSKDGESLH-YIPfKETDKYVKKVKAI 164
Cdd:cd16894   92 RVRRAIKRAGTDKWEDYYRlYLP-AETRRYVPKFLAA 127
emtA PRK15470
membrane-bound lytic murein transglycosylase EmtA;
38-109 3.41e-11

membrane-bound lytic murein transglycosylase EmtA;


Pssm-ID: 185367 [Multi-domain]  Cd Length: 203  Bit Score: 59.21  E-value: 3.41e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 152929603  38 LDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPET-GEWVAEKMGMK-DFNIDDLKDPETNIKMGCWYLNNLK 109
Cdd:PRK15470  52 VDPQLITAIIAIESGGNPNAVSKSNAIGLMQLKASTsGRDVYRRMGWSgEPTTSELKNPERNISMGAAYLNILE 125
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 38-129 6.21e-11

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: 56.55  E-value: 6.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  38 LDPYFVAAVIKTESNFKKDA-ASKKNAQGLMQITPETGEWVAekmgmKDFNID---DLKDPETNIKMGCWYLN----NLK 109
Cdd:cd13399    3 VPPGILAAILGVESGFGPNAgGSPAGAQGIAQFMPSTWKAYG-----VDGNGDgkaDPFNPEDAIASAANYLCrhgwDLN 77

                         90       100
                 ....*....|....*....|
gi 152929603 110 EEFDGNMDLVLAAYNGGRGN 129
Cdd:cd13399   78 AFLGEDNFLALAAYNAGPGA 97
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
24-130 8.21e-10

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 56.21  E-value: 8.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  24 KYRDYIDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPET-GEWVAEKMGM-----KDFniddLKDPETN 97
Cdd:PRK11671 191 KYLPMVRKASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHTaGKDVFRMKGKsgqpsRSY----LFDPANN 266

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 152929603  98 IKMGCWYLNNLKEEFDGNMD-------LVLAAYNGGRGNV 130
Cdd:PRK11671 267 IDTGTAYLAILQNVYLGGITnptsrryAVITAYNGGAGSV 306
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 50-169 1.44e-09

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 55.90  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  50 ESNFKKDAASKKNAQGLMQITPETGEwvaeKMGMK-DFNIDDLKDPETNIKMGCWYLNNLKEEFDGNMDLVLAAYNGGRG 128
Cdd:PRK10783 128 ESAFDPHATSGANAAGIWQIIPSTGR----NYGLKqTRWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEG 203

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 152929603 129 NVQKWLKDSE---HSKDGESLHyIPfKETDKYVKKVKAIYNIYR 169
Cdd:PRK10783 204 RVMKAIKANKakgKPTDFWSLS-LP-RETKIYVPKMLALSDILK 245
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
24-131 1.55e-09

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 55.65  E-value: 1.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  24 KYRDYIDMYANEhkLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETgewvAEKMGmkdfnIDDLKDPETNIKMGCW 103
Cdd:PRK10859 289 KYQPLFEKYAGE--LDWRLLAAIAYQESHWNPQATSPTGVRGLMMLTRNT----AQSMG-----VTDRLDPEQSIRGGAR 357

                         90       100       110
                 ....*....|....*....|....*....|....
gi 152929603 104 YLNNLKEEFDGNMD------LVLAAYNGGRGNVQ 131
Cdd:PRK10859 358 YLQDLMERLPESIPeperiwFALAAYNIGYGHML 391
PHA00658 PHA00658
putative lysin
 55-166 2.47e-09

putative lysin


Pssm-ID: 106967 [Multi-domain]  Cd Length: 720  Bit Score: 55.21  E-value: 2.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  55 KDAASKKNAQGLMQITPETGEWVAEKMGMKDFNIDDLKDPETNIKMGCWYLNNLKEEFDGNMDLVLAAYNGGRGNVQKWL 134
Cdd:PHA00658 322 KPLTSPKGAVGIAQVMPDTAPEAAKLAGLPWDENRYRNDAAYNRALGMAYFQKQLRDFGGDLPKAYAAYNAGPGALQSAL 401

                         90       100       110
                 ....*....|....*....|....*....|..
gi 152929603 135 KDsehSKDGESLHYIPfKETDKYVKKVKAIYN 166
Cdd:PHA00658 402 KD---AKDGNWLALLP-KETQDYVVKNMQAYN 429
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 36-166 1.02e-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: 47.91  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  36 HKLDPYFVAAVIKTESNFKKDAASK-KNAQ---GLMQI-TpetgEWVAEKMGMKDFNIDDLKDPETNIKMGCWYL-NNLK 109
Cdd:cd13400    1 YGVPPRLLRAIAKVESGFNPNAINRnKNGSydiGLMQInS----IWLPELARYGITREELLNDPCTNIYVGAWILaRNIK 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 152929603 110 EEfdGNMDLVLAAYNGGRGNVQkwlkdsehskdgeslhyipfketDKYVKKVKAIYN 166
Cdd:cd13400   77 RY--GNTWKAVGAYNSGTPKKN-----------------------DKYARKVYRIYR 108
PHA00368 PHA00368
internal virion protein D
 22-128 1.33e-07

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 50.16  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603   22 PIKYRDYIDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGEwvaeKMGMKdFNIDDLKDPETNIKMG 101
Cdd:PHA00368    8 PSEYDGLFQKAADAHGVSYDLLRKVGWDESRFNPTAKSPTGPKGLMQFTKATAK----ALGLI-VDDDDRLDPELAIDAG 82

                          90       100
                  ....*....|....*....|....*..
gi 152929603  102 CWYLNNLKEEFDGNMDLVLAAYNGGRG 128
Cdd:PHA00368   83 ARYLADLVGKYDGDELKAALAYNQGEG 109
GEWL cd01021
Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; ...
 24-133 9.86e-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: 40.66  E-value: 9.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152929603  24 KYRDYIDMYANEHKLDPYFVAAVIKTESNF-----KKDAASKKNAQGLMQI-----TPEtGEWvaekmgmkdfniddlkD 93
Cdd:cd01021   36 KYKDCIKQVGKKLCIDPALIAAIISRESRAgaaldKNGWGDHGNGFGLMQVdkryhPPK-GAW----------------D 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 152929603  94 PETNIKM--GCW--YLNNLKEEFDG-----NMDLVLAAYNGGRGNVQKW 133
Cdd:cd01021   99 SEEHIEQatGILidFIKTVQRKHPSwspeqQLKGGIAAYNAGVGNVQSY 147
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 42-104 6.38e-03

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: 33.54  E-value: 6.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 152929603  42 FVAAVIKTESNFKKDAA--SKKNAQGLMQITPETGEwvaekmGMKDFNIDDLKDPETNIKMGCWY 104
Cdd:cd00442    1 VLAAIIGQESGGNKPANagSGSGAAGLFQFMPGTWK------AYGKNSSSDLNDPEASIEAAAKY 59
 
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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