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Conserved domains on  [gi|1109795420|emb|SHF51151|]
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soluble lytic murein transglycosylase [Desulfofundulus australicus DSM 11792]

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 ...
77-222 2.82e-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: 252.05  E-value: 2.82e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  77 PFPYRETIFKYASSYGVDPFLVAAVIKTESNFNPRATSHRGARGLMQIMPETGSWAARELGLSHYHRDLLFDPEFNIHIG 156
Cdd:cd16896     1 PLKYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAEWIAEKLGLEDFSEDDLYDPETNIRLG 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109795420 157 TWYLADLHRTFNNDPILVLAAYNGGLGNVQKWLEQQRWTGEKSKLDQIPFAETRDFIRKVLWNYQV 222
Cdd:cd16896    81 TWYLSYLLKEFDGNLVLALAAYNAGPGNVDKWLKDGGWSGDGKTLDQIPFPETRHYVKKVLKNYKI 146
 
Name Accession Description Interval E-value
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
77-222 2.82e-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: 252.05  E-value: 2.82e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  77 PFPYRETIFKYASSYGVDPFLVAAVIKTESNFNPRATSHRGARGLMQIMPETGSWAARELGLSHYHRDLLFDPEFNIHIG 156
Cdd:cd16896     1 PLKYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAEWIAEKLGLEDFSEDDLYDPETNIRLG 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109795420 157 TWYLADLHRTFNNDPILVLAAYNGGLGNVQKWLEQQRWTGEKSKLDQIPFAETRDFIRKVLWNYQV 222
Cdd:cd16896    81 TWYLSYLLKEFDGNLVLALAAYNAGPGNVDKWLKDGGWSGDGKTLDQIPFPETRHYVKKVLKNYKI 146
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
15-225 1.75e-69

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: 213.32  E-value: 1.75e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  15 AFIAGQRKFSALSRLQAAIWSDAYLSWHLKVKKDKSFKVRLFFFVLMLLIILNLDHLGRLIYPFPYRETIFKYASSYGVD 94
Cdd:COG0741    38 AAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAIAALAAELLALAALLLRRPLPYLPLIEEAAKKYGVD 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  95 PFLVAAVIKTESNFNPRATSHRGARGLMQIMPETGSWAARELGLShYHRDLLFDPEFNIHIGTWYLADLHRTFNNDPILV 174
Cdd:COG0741   118 PALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLG-PSPDDLFDPETNIRAGAAYLRELLDRFDGDLVLA 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1109795420 175 LAAYNGGLGNVQKWLEQQRWtgekSKLDQIPFAETRDFIRKVLWNYQVYRY 225
Cdd:COG0741   197 LAAYNAGPGRVRRWLRRNGD----RDGEIIPYAETRNYVKKVLANYAIYRA 243
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
84-198 8.32e-43

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: 140.91  E-value: 8.32e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  84 IFKYASSYGVDPFLVAAVIKTESNFNPRATSHRGARGLMQIMPETGSWAARELGLShyhRDLLFDPEFNIHIGTWYLADL 163
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPG---VDDLFDPEKNIKAGTKYLKEL 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1109795420 164 HRTFNNDPILVLAAYNGGLGNVQKWLEQQRWTGEK 198
Cdd:pfam01464  78 YKQYGGDLWLALAAYNAGPGRVRKWIKNAGAKDKK 112
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
69-228 9.28e-29

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 113.62  E-value: 9.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  69 DHLGRLiYPFPYRETIFKYASSYGVDPFLVAAVIKTESNFNPRATSHRGARGLMQIMPETGSWAARELGLSHY-HRDLLF 147
Cdd:PRK11619  469 DHLEER-FPLAWNDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFSIPGYsSSSQLL 547
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420 148 DPEFNIHIGTWYLADLHRTFNNDPILVLAAYNGGLGNVQKWLEQQrwtgeKSKLD------QIPFAETRDFIRKVLwNYQ 221
Cdd:PRK11619  548 DPETNINIGTSYLEYVYQQFGNNRILASAAYNAGPGRVRTWLGNS-----AGRIDavafveSIPFSETRGYVKNVL-AYD 621

                  ....*...
gi 1109795420 222 V-YRYLYG 228
Cdd:PRK11619  622 AyYRYFMG 629
 
Name Accession Description Interval E-value
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
77-222 2.82e-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: 252.05  E-value: 2.82e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  77 PFPYRETIFKYASSYGVDPFLVAAVIKTESNFNPRATSHRGARGLMQIMPETGSWAARELGLSHYHRDLLFDPEFNIHIG 156
Cdd:cd16896     1 PLKYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAEWIAEKLGLEDFSEDDLYDPETNIRLG 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109795420 157 TWYLADLHRTFNNDPILVLAAYNGGLGNVQKWLEQQRWTGEKSKLDQIPFAETRDFIRKVLWNYQV 222
Cdd:cd16896    81 TWYLSYLLKEFDGNLVLALAAYNAGPGNVDKWLKDGGWSGDGKTLDQIPFPETRHYVKKVLKNYKI 146
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
76-226 6.68e-71

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: 213.49  E-value: 6.68e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  76 YPFPYRETIFKYASSYGVDPFLVAAVIKTESNFNPRATSHRGARGLMQIMPETGSWAARELGLSHYHRDLLFDPEFNIHI 155
Cdd:cd13401     2 YPLPYRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLPYYSPRDLFDPEYNIRL 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109795420 156 GTWYLADLHRTFNNDPILVLAAYNGGLGNVQKWLEQqrwTGEKSKLD---QIPFAETRDFIRKVLWNYQVYRYL 226
Cdd:cd13401    82 GSAYLAELLDRFDGNPVLALAAYNAGPGRVRRWLKR---RGDLDPDLwieTIPFSETRNYVKRVLENYVVYRAL 152
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
15-225 1.75e-69

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: 213.32  E-value: 1.75e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  15 AFIAGQRKFSALSRLQAAIWSDAYLSWHLKVKKDKSFKVRLFFFVLMLLIILNLDHLGRLIYPFPYRETIFKYASSYGVD 94
Cdd:COG0741    38 AAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAIAALAAELLALAALLLRRPLPYLPLIEEAAKKYGVD 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  95 PFLVAAVIKTESNFNPRATSHRGARGLMQIMPETGSWAARELGLShYHRDLLFDPEFNIHIGTWYLADLHRTFNNDPILV 174
Cdd:COG0741   118 PALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLG-PSPDDLFDPETNIRAGAAYLRELLDRFDGDLVLA 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1109795420 175 LAAYNGGLGNVQKWLEQQRWtgekSKLDQIPFAETRDFIRKVLWNYQVYRY 225
Cdd:COG0741   197 LAAYNAGPGRVRRWLRRNGD----RDGEIIPYAETRNYVKKVLANYAIYRA 243
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
95-221 2.46e-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: 154.68  E-value: 2.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  95 PFLVAAVIKTESNFNPRATSHRGARGLMQIMPETGSWAARElglshyHRDLLFDPEFNIHIGTWYLADLHRTFNNDPILV 174
Cdd:cd00254     1 PALVLAVIRVESGFNPRAVSPAGARGLMQLMPGTARDLGRR------GVDDLFDPEENIRAGARYLRELLDRFGGDLELA 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1109795420 175 LAAYNGGLGNVQKWLEQQRwtgekskldqIPFAETRDFIRKVLWNYQ 221
Cdd:cd00254    75 LAAYNAGPGAVDRWGGGEV----------PPYKETRNYVQRVLAYYQ 111
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
84-198 8.32e-43

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: 140.91  E-value: 8.32e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  84 IFKYASSYGVDPFLVAAVIKTESNFNPRATSHRGARGLMQIMPETGSWAARELGLShyhRDLLFDPEFNIHIGTWYLADL 163
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPG---VDDLFDPEKNIKAGTKYLKEL 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1109795420 164 HRTFNNDPILVLAAYNGGLGNVQKWLEQQRWTGEK 198
Cdd:pfam01464  78 YKQYGGDLWLALAAYNAGPGRVRKWIKNAGAKDKK 112
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
86-221 4.29e-36

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: 124.98  E-value: 4.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  86 KYASSYGVDPFLVAAVIKTESNFNPRATSHRGARGLMQIMPET-GSWAARELGLS--HYHRDLLFDPEFNIHIGTWYLAD 162
Cdd:cd16893     5 KYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTaGRDVYRLLGGKggLPSKSYLFDPENNIDIGTAYLHI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420 163 L-HRTFN--NDPI----LVLAAYNGGLGNVQKWLeqqrwTGEKSK-LDQI----------------PFAETRDFIRKVLW 218
Cdd:cd16893    85 LqNRYLKgiKNPKsreyCAIAAYNGGAGNVLRTF-----SSDRKKaISKInrlspdevyqhltkklPAAETRNYLKKVLK 159

                  ...
gi 1109795420 219 NYQ 221
Cdd:cd16893   160 AKK 162
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
84-225 4.57e-32

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: 114.55  E-value: 4.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  84 IFKYASSYGVDPFLVAAVIKTESNFNPRATSHRGARGLMQIMPETgswaARELGLSHyhrdlLFDPEFNIHIGTWYLADL 163
Cdd:cd13403     1 FKKYAEKYGFDWRLLAAQAYQESRFNPNARSPAGARGLMQLMPST----ARELGVND-----RLDPEQNIHAGAKYLRYL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420 164 HRTFNNDP------ILVLAAYNGGLGNVQKW--------LEQQRWTGEKSKL----DQIPFA----------ETRDFIRK 215
Cdd:cd13403    72 RDRFPPDIdepdrlKFALAAYNAGPGHVRDArrlakkygLNPNVWFDNVEVLpllkSPYYDPvvkygyargrETVNYVRN 151
                         170
                  ....*....|
gi 1109795420 216 VLWNYQVYRY 225
Cdd:cd13403   152 IRKYYDAYKQ 161
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
79-226 1.39e-31

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 119.78  E-value: 1.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  79 PYRETIFKYASSYGVDPFLVAAVIKTESNFNPRATSHRGARGLMQIMPETgswaARELGLshyhrDLLFDPEFNIHIGTW 158
Cdd:COG4623   263 PYDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPAT----AKELGV-----DDRLDPEQSIRAGAK 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420 159 YLADLHRTFNNDPI------LVLAAYNGGLGNVQK--------------WLEQQRWTGEKSKLDQIPFAETRDFIRKVLW 218
Cdd:COG4623   334 YLRWLYDRFPEAIDepdrwwFALAAYNAGPGHVQDarrlakkqgldpdrWFDVEKSQPKYYDTGYARGRETVNYVPNIRA 413

                  ....*...
gi 1109795420 219 NYQVYRYL 226
Cdd:COG4623   414 YYDIYKRL 421
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
69-228 9.28e-29

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 113.62  E-value: 9.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  69 DHLGRLiYPFPYRETIFKYASSYGVDPFLVAAVIKTESNFNPRATSHRGARGLMQIMPETGSWAARELGLSHY-HRDLLF 147
Cdd:PRK11619  469 DHLEER-FPLAWNDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFSIPGYsSSSQLL 547
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420 148 DPEFNIHIGTWYLADLHRTFNNDPILVLAAYNGGLGNVQKWLEQQrwtgeKSKLD------QIPFAETRDFIRKVLwNYQ 221
Cdd:PRK11619  548 DPETNINIGTSYLEYVYQQFGNNRILASAAYNAGPGRVRTWLGNS-----AGRIDavafveSIPFSETRGYVKNVL-AYD 621

                  ....*...
gi 1109795420 222 V-YRYLYG 228
Cdd:PRK11619  622 AyYRYFMG 629
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
105-217 2.98e-22

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: 88.34  E-value: 2.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420 105 ESNFNPRATSHRGARGLMQIMPETgswaARELGLS-HYHRDLLFDPEFNIHIGTWYLADLHRTFnNDPILVLAAYNGGLG 183
Cdd:cd16894    17 ESGFNPDAVSSAGAAGLWQFMPAT----AREYGLRvDSWVDERRDPEKSTRAAARYLKDLYKRF-GDWLLALAAYNAGEG 91
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1109795420 184 NVQKWLEQQRWTG-EKSKLDQIPfAETRDFIRKVL 217
Cdd:cd16894    92 RVRRAIKRAGTDKwEDYYRLYLP-AETRRYVPKFL 125
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
86-185 1.18e-19

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 86.26  E-value: 1.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  86 KYASSYGVDPFLVAAVIKTESNFNPRATSHRGARGLMQIMPETgswAAREL----GLS-HYHRDLLFDPEFNIHIGTWYL 160
Cdd:PRK11671  198 KASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHT---AGKDVfrmkGKSgQPSRSYLFDPANNIDTGTAYL 274
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1109795420 161 ADLHRTF---NNDPI----LVLAAYNGGLGNV 185
Cdd:PRK11671  275 AILQNVYlggITNPTsrryAVITAYNGGAGSV 306
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
91-184 2.99e-18

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: 76.96  E-value: 2.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  91 YGVDPFLVAAVIKTESNFNPRA-TSHRGARGLMQIMPETgsWAARELGLSHYHRDLLFDPEFNIHIGTWYLA----DLHR 165
Cdd:cd13399     1 YGVPPGILAAILGVESGFGPNAgGSPAGAQGIAQFMPST--WKAYGVDGNGDGKADPFNPEDAIASAANYLCrhgwDLNA 78
                          90
                  ....*....|....*....
gi 1109795420 166 TFNNDPILVLAAYNGGLGN 184
Cdd:cd13399    79 FLGEDNFLALAAYNAGPGA 97
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
91-162 5.01e-15

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: 68.71  E-value: 5.01e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109795420  91 YGVDPFLVAAVIKTESNFNPRATSHRGAR----GLMQImpetGSWAARELGLSHYHR-DLLFDPEFNIHIGTWYLAD 162
Cdd:cd13400     1 YGVPPRLLRAIAKVESGFNPNAINRNKNGsydiGLMQI----NSIWLPELARYGITReELLNDPCTNIYVGAWILAR 73
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
80-186 2.54e-11

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 62.58  E-value: 2.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  80 YRETIFKYASsyGVDPFLVAAVIKTESNFNPRATSHRGARGLMQIMPETgswaARELGLShyhrDLLfDPEFNIHIGTWY 159
Cdd:PRK10859  290 YQPLFEKYAG--ELDWRLLAAIAYQESHWNPQATSPTGVRGLMMLTRNT----AQSMGVT----DRL-DPEQSIRGGARY 358
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1109795420 160 LADLHRTF-----NNDPI-LVLAAYNGGLGNVQ 186
Cdd:PRK10859  359 LQDLMERLpesipEPERIwFALAAYNIGYGHML 391
PHA00368 PHA00368
internal virion protein D
77-186 5.18e-11

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 62.11  E-value: 5.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420   77 PFPYRETIFKYASSYGVDPFLVAAVIKTESNFNPRATSHRGARGLMQIMPETGswaaRELGLSHYHRDLLfDPEFNIHIG 156
Cdd:PHA00368     8 PSEYDGLFQKAADAHGVSYDLLRKVGWDESRFNPTAKSPTGPKGLMQFTKATA----KALGLIVDDDDRL-DPELAIDAG 82
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1109795420  157 TWYLADLHRTFNNDPILVLAAYNGG---LGNVQ 186
Cdd:PHA00368    83 ARYLADLVGKYDGDELKAALAYNQGegrLGAPQ 115
emtA PRK15470
membrane-bound lytic murein transglycosylase EmtA;
86-227 5.93e-11

membrane-bound lytic murein transglycosylase EmtA;


Pssm-ID: 185367 [Multi-domain]  Cd Length: 203  Bit Score: 59.98  E-value: 5.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  86 KYASSYGVDPFLVAAVIKTESNFNPRATSHRGARGLMQIMPET-GSWAARELGLS-HYHRDLLFDPEFNIHIGTWYLADL 163
Cdd:PRK15470   45 KAGAAWGVDPQLITAIIAIESGGNPNAVSKSNAIGLMQLKASTsGRDVYRRMGWSgEPTTSELKNPERNISMGAAYLNIL 124
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109795420 164 HR---TFNNDPIL----VLAAYNGGLGNVQKWLEQQRwtgeKSKLDQIPFAETRDFIRKVLWNY---QVYRYLY 227
Cdd:PRK15470  125 ETgplAGIEDPKVlqyaLVVSYANGAGALLRTFSSDR----KKAISKINDLDADEFLEHVARNHpapQAPRYIY 194
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
105-187 1.10e-08

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 54.74  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420 105 ESNFNPRATSHRGARGLMQIMPETGswaaRELGLSHyhrDLLFDPEFNIHIGTWYLAD----LHRTFNNDPILVLAAYNG 180
Cdd:PRK10783  128 ESAFDPHATSGANAAGIWQIIPSTG----RNYGLKQ---TRWYDARRDVVASTTAALDmmqrLNKMFDGDWLLTVAAYNS 200

                  ....*..
gi 1109795420 181 GLGNVQK 187
Cdd:PRK10783  201 GEGRVMK 207
PHA00658 PHA00658
putative lysin
113-223 2.48e-07

putative lysin


Pssm-ID: 106967 [Multi-domain]  Cd Length: 720  Bit Score: 50.98  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420 113 TSHRGARGLMQIMPETGSWAARELGLSHYHRDLLFDPEFNIHIGTWYLADLHRTFNNDPILVLAAYNGGLGNVQKWLEQQ 192
Cdd:PHA00658  325 TSPKGAVGIAQVMPDTAPEAAKLAGLPWDENRYRNDAAYNRALGMAYFQKQLRDFGGDLPKAYAAYNAGPGALQSALKDA 404
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1109795420 193 RwtgEKSKLDQIPfAETRDFIRKvlwNYQVY 223
Cdd:PHA00658  405 K---DGNWLALLP-KETQDYVVK---NMQAY 428
PRK15328 PRK15328
type III secretion system invasion protein IagB;
54-182 1.51e-05

type III secretion system invasion protein IagB;


Pssm-ID: 185228 [Multi-domain]  Cd Length: 160  Bit Score: 43.70  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  54 RLFFFVLMLLIIlnldhlgrliyPFPYRETIFKYASSYGVDPFLVAAVIKTESNFNPRAT--SHRGAR--GLMQI----M 125
Cdd:PRK15328    3 YFFIIVIWLLSI-----------NTAWADCWLQAEKMFNIESELLYAIAQQESAMKPGAIghNRDGSTdlGLMQInsfhM 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1109795420 126 PETgswaaRELGLSHYHrdLLFDPEFNIHIGTWYLADLHRTFNNDPILVlAAYNGGL 182
Cdd:PRK15328   72 KRL-----KKMGISEKQ--LLQDPCISVIVGASILSDMMKIYGYSWEAV-GAYNAGT 120
SLT COG3953
SLT domain protein [Mobilome: prophages, transposons];
87-181 1.03e-04

SLT domain protein [Mobilome: prophages, transposons];


Pssm-ID: 443153 [Multi-domain]  Cd Length: 325  Bit Score: 42.39  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  87 YASSYGVDPflVAAVIKTESNFNPRAT------SHRG--ARGLMQIMPETgsWAArelglshYHR---DLLFDPEFNIHI 155
Cdd:COG3953   227 PVSEAWVDG--ILRIIQHESGGNPNAInlwdsnAAAGtpSKGLMQVIPPT--FNA-------YKLpghGNIYNPVDNILA 295
                          90       100
                  ....*....|....*....|....*.
gi 1109795420 156 GTWYLADLHRTFNNDPILVLAAYNGG 181
Cdd:COG3953   296 GINYAKSRYGSSDNVPGLASLGQGGG 321
LT_TF-like cd13402
lytic transglycosylase-like domain of tail fiber-like proteins and similar domains; These tail ...
101-183 2.80e-04

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: 39.49  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420 101 VIKTESNFNPRAT------SHRG--ARGLMQIMPET-GSWAARelglshYHRDlLFDPEFNIHIGTWYLadLHRtfnNDP 171
Cdd:cd13402     7 QIQTESGGNPNAInnwdsnAKAGhpSKGLMQVIPPTfAAYAPP------GHGN-ILNPLDNILAAINYA--KAR---YGS 74
                          90
                  ....*....|..
gi 1109795420 172 ILVLAAYNGGLG 183
Cdd:cd13402    75 GFALAAGGGGGG 86
CwlT-like cd16891
CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall ...
80-200 8.55e-04

CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall hydrolase containing an N-terminal lysozyme domain and a C-terminal NlpC/P60 endopeptidase domain (gamma-d-D-glutamyl-L-diamino acid endopeptidase), and has been implicated in the spread of transposons. 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: 381612 [Multi-domain]  Cd Length: 151  Bit Score: 38.74  E-value: 8.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109795420  80 YRETIFKYASSYGVDPF--LVAAVIKTESnfnpratshrGARG--LMQimpetgswAARELGLShyhRDLLFDPEFNIHI 155
Cdd:cd16891     1 YRPLVEKEAKKYGIPEYvpLILAIIMQES----------GGKGpdIMQ--------SSESAGLP---PNTITDPEESIEQ 59
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1109795420 156 GTWYLADL---HRTFNNDPILVLAAYNGGLGNVQKWLE-QQRWTGEKSK 200
Cdd:cd16891    60 GVKYFADVlkkAKGKGVDIWTAVQAYNFGGGYIDYVAKnGGKYTLELAK 108
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
99-159 9.78e-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: 36.62  E-value: 9.78e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109795420  99 AAVIKTESNFNP--RATSHRGARGLMQIMPETgswaARELGLshYHRDLLFDPEFNIHIGTWY 159
Cdd:cd00442     3 AAIIGQESGGNKpaNAGSGSGAAGLFQFMPGT----WKAYGK--NSSSDLNDPEASIEAAAKY 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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