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Conserved domains on  [gi|90111747|ref|NP_418809|]
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soluble lytic murein transglycosylase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

murein transglycosylase( domain architecture ID 11485431)

soluble lytic murein transglycosylase is a murein-degrading enzyme that catalyzes cleavage of glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 1-645 0e+00

lytic murein transglycosylase; Provisional


:

Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 1344.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747    1 MEKAKQVTWRLLAAGVCLLTVSSVARADSLDEQRSRYAQIKQAWDNRQMDVVEQMMPGLKDYPLYPYLEYRQITDDLMNQ 80
Cdd:PRK11619   1 MEKAKMGKWRLLAAGVCLLTVSGVARADSLDEQRQRYQQIKQAWDNRQMDVVEQLMPTLKDYPLYPYLEYRQLTQDLMNQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747   81 PAVTVTNFVRANPTLPPARTLQSRFVNELARREDWRGLLAFSPEKPGTTEAQCNYYYAKWNTGQSEEAWQGAKELWLTGK 160
Cdd:PRK11619  81 PAVQVTNFIRANPTLPPARSLQSRFVNELARREDWRGLLAFSPEKPKPVEARCNYYYAKWATGQQQEAWQGAKELWLTGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  161 SQPNACDKLFSVWRASGKQDPLAYLERIRLAMKAGNTGLVTVLAGQMPADYQTIASAIISLANNPNTVLTFARTTGATDF 240
Cdd:PRK11619 161 SLPNACDKLFSVWQQSGKQDPLAYLERIRLAMKAGNTGLVTYLAKQLPADYQTIASALIKLQNDPNTVETFARTTGPTDF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  241 TRQMAAVAFASVARQDAENARLMIPSLAQAQQLNEDQIQELRDIVAWRLMGNDVTDEQAKWRDDAIMRSQSTSLIERRVR 320
Cdd:PRK11619 241 TRQMAAVAFASVARQDAENARLMIPSLVRAQKLNEDQRQELRDIVAWRLMGNDVTDEQAKWRDDVIMRSQSTSLLERRVR 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  321 MALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLERGREAEAKEILHQLMQQRGFYPMVAAQRIGEEYELKIDKAPQ 400
Cdd:PRK11619 321 MALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLEQGRKAEAEEILRQLMQQRGFYPMVAAQRLGEEYPLKIDKAPK 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  401 nVDSALTQGPEMARVRELMYWNLDNTARSEWANLVKSKSKTEQAQLARYAFNNQWWDLSVQATIAGKLWDHLEERFPLAY 480
Cdd:PRK11619 401 -PDSALTQGPEMARVRELMYWNMDNTARSEWANLVASRSKTEQAQLARYAFNQQWWDLSVQATIAGKLWDHLEERFPLAW 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  481 NDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPGYSSPGQLLDPETNINIGTSY 560
Cdd:PRK11619 480 NDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFSIPGYSSSSQLLDPETNINIGTSY 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  561 LQYVYQQFGNNRIFSSAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGDKPTLMSATE 640
Cdd:PRK11619 560 LEYVYQQFGNNRILASAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGQKPTLLSDAE 639


                 ....*
gi 90111747  641 WGRRY 645
Cdd:PRK11619 640 WQRRY 644
 
Name Accession Description Interval E-value
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 1-645 0e+00

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 1344.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747    1 MEKAKQVTWRLLAAGVCLLTVSSVARADSLDEQRSRYAQIKQAWDNRQMDVVEQMMPGLKDYPLYPYLEYRQITDDLMNQ 80
Cdd:PRK11619   1 MEKAKMGKWRLLAAGVCLLTVSGVARADSLDEQRQRYQQIKQAWDNRQMDVVEQLMPTLKDYPLYPYLEYRQLTQDLMNQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747   81 PAVTVTNFVRANPTLPPARTLQSRFVNELARREDWRGLLAFSPEKPGTTEAQCNYYYAKWNTGQSEEAWQGAKELWLTGK 160
Cdd:PRK11619  81 PAVQVTNFIRANPTLPPARSLQSRFVNELARREDWRGLLAFSPEKPKPVEARCNYYYAKWATGQQQEAWQGAKELWLTGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  161 SQPNACDKLFSVWRASGKQDPLAYLERIRLAMKAGNTGLVTVLAGQMPADYQTIASAIISLANNPNTVLTFARTTGATDF 240
Cdd:PRK11619 161 SLPNACDKLFSVWQQSGKQDPLAYLERIRLAMKAGNTGLVTYLAKQLPADYQTIASALIKLQNDPNTVETFARTTGPTDF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  241 TRQMAAVAFASVARQDAENARLMIPSLAQAQQLNEDQIQELRDIVAWRLMGNDVTDEQAKWRDDAIMRSQSTSLIERRVR 320
Cdd:PRK11619 241 TRQMAAVAFASVARQDAENARLMIPSLVRAQKLNEDQRQELRDIVAWRLMGNDVTDEQAKWRDDVIMRSQSTSLLERRVR 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  321 MALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLERGREAEAKEILHQLMQQRGFYPMVAAQRIGEEYELKIDKAPQ 400
Cdd:PRK11619 321 MALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLEQGRKAEAEEILRQLMQQRGFYPMVAAQRLGEEYPLKIDKAPK 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  401 nVDSALTQGPEMARVRELMYWNLDNTARSEWANLVKSKSKTEQAQLARYAFNNQWWDLSVQATIAGKLWDHLEERFPLAY 480
Cdd:PRK11619 401 -PDSALTQGPEMARVRELMYWNMDNTARSEWANLVASRSKTEQAQLARYAFNQQWWDLSVQATIAGKLWDHLEERFPLAW 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  481 NDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPGYSSPGQLLDPETNINIGTSY 560
Cdd:PRK11619 480 NDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFSIPGYSSSSQLLDPETNINIGTSY 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  561 LQYVYQQFGNNRIFSSAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGDKPTLMSATE 640
Cdd:PRK11619 560 LEYVYQQFGNNRILASAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGQKPTLLSDAE 639


                 ....*
gi 90111747  641 WGRRY 645
Cdd:PRK11619 640 WQRRY 644
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 475-627 1.44e-67

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: 217.34  E-value: 1.44e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747 475 RFPLAYNDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPgYSSPGQLLDPETNI 554
Cdd:cd13401   1 RYPLPYRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLP-YYSPRDLFDPEYNI 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111747 555 NIGTSYLQYVYQQFGNNRIFSSAAYNAGPGRVRTWLGNSaGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRY 627
Cdd:cd13401  80 RLGSAYLAELLDRFDGNPVLALAAYNAGPGRVRRWLKRR-GDLDPDLWIETIPFSETRNYVKRVLENYVVYRA 151
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 411-627 9.14e-50

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: 173.64  E-value: 9.14e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747 411 EMARVRELMYWNLDNTARSEWANLVKSKSKTEQAQLARYAFNNQWWDLSVQA----TIAGKLWDHLEERFPLAYNDLFKR 486
Cdd:COG0741  30 AAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAiaalAAELLALAALLLRRPLPYLPLIEE 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747 487 YTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPgySSPGQLLDPETNINIGTSYLQYVYQ 566
Cdd:COG0741 110 AAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLG--PSPDDLFDPETNIRAGAAYLRELLD 187

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111747 567 QFGNNRIFSSAAYNAGPGRVRTWLGNSAGRidavaFVESIPFSETRGYVKNVLAYDAYYRY 627
Cdd:COG0741 188 RFDGDLVLALAAYNAGPGRVRRWLRRNGDR-----DGEIIPYAETRNYVKKVLANYAIYRA 243
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 484-600 2.86e-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: 140.13  E-value: 2.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747   484 FKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMfsipGYSSPGQLLDPETNINIGTSYLQY 563
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLR----VNPGVDDLFDPEKNIKAGTKYLKE 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 90111747   564 VYQQFGNNRIFSSAAYNAGPGRVRTWLGNSAGRIDAV 600
Cdd:pfam01464  77 LYKQYGGDLWLALAAYNAGPGRVRKWIKNAGAKDKKL 113
 
Name Accession Description Interval E-value
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 1-645 0e+00

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 1344.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747    1 MEKAKQVTWRLLAAGVCLLTVSSVARADSLDEQRSRYAQIKQAWDNRQMDVVEQMMPGLKDYPLYPYLEYRQITDDLMNQ 80
Cdd:PRK11619   1 MEKAKMGKWRLLAAGVCLLTVSGVARADSLDEQRQRYQQIKQAWDNRQMDVVEQLMPTLKDYPLYPYLEYRQLTQDLMNQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747   81 PAVTVTNFVRANPTLPPARTLQSRFVNELARREDWRGLLAFSPEKPGTTEAQCNYYYAKWNTGQSEEAWQGAKELWLTGK 160
Cdd:PRK11619  81 PAVQVTNFIRANPTLPPARSLQSRFVNELARREDWRGLLAFSPEKPKPVEARCNYYYAKWATGQQQEAWQGAKELWLTGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  161 SQPNACDKLFSVWRASGKQDPLAYLERIRLAMKAGNTGLVTVLAGQMPADYQTIASAIISLANNPNTVLTFARTTGATDF 240
Cdd:PRK11619 161 SLPNACDKLFSVWQQSGKQDPLAYLERIRLAMKAGNTGLVTYLAKQLPADYQTIASALIKLQNDPNTVETFARTTGPTDF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  241 TRQMAAVAFASVARQDAENARLMIPSLAQAQQLNEDQIQELRDIVAWRLMGNDVTDEQAKWRDDAIMRSQSTSLIERRVR 320
Cdd:PRK11619 241 TRQMAAVAFASVARQDAENARLMIPSLVRAQKLNEDQRQELRDIVAWRLMGNDVTDEQAKWRDDVIMRSQSTSLLERRVR 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  321 MALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLERGREAEAKEILHQLMQQRGFYPMVAAQRIGEEYELKIDKAPQ 400
Cdd:PRK11619 321 MALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLEQGRKAEAEEILRQLMQQRGFYPMVAAQRLGEEYPLKIDKAPK 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  401 nVDSALTQGPEMARVRELMYWNLDNTARSEWANLVKSKSKTEQAQLARYAFNNQWWDLSVQATIAGKLWDHLEERFPLAY 480
Cdd:PRK11619 401 -PDSALTQGPEMARVRELMYWNMDNTARSEWANLVASRSKTEQAQLARYAFNQQWWDLSVQATIAGKLWDHLEERFPLAW 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  481 NDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPGYSSPGQLLDPETNINIGTSY 560
Cdd:PRK11619 480 NDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFSIPGYSSSSQLLDPETNINIGTSY 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  561 LQYVYQQFGNNRIFSSAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGDKPTLMSATE 640
Cdd:PRK11619 560 LEYVYQQFGNNRILASAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGQKPTLLSDAE 639


                 ....*
gi 90111747  641 WGRRY 645
Cdd:PRK11619 640 WQRRY 644
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 475-627 1.44e-67

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: 217.34  E-value: 1.44e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747 475 RFPLAYNDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPgYSSPGQLLDPETNI 554
Cdd:cd13401   1 RYPLPYRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLP-YYSPRDLFDPEYNI 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111747 555 NIGTSYLQYVYQQFGNNRIFSSAAYNAGPGRVRTWLGNSaGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRY 627
Cdd:cd13401  80 RLGSAYLAELLDRFDGNPVLALAAYNAGPGRVRRWLKRR-GDLDPDLWIETIPFSETRNYVKRVLENYVVYRA 151
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 411-627 9.14e-50

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: 173.64  E-value: 9.14e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747 411 EMARVRELMYWNLDNTARSEWANLVKSKSKTEQAQLARYAFNNQWWDLSVQA----TIAGKLWDHLEERFPLAYNDLFKR 486
Cdd:COG0741  30 AAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAiaalAAELLALAALLLRRPLPYLPLIEE 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747 487 YTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPgySSPGQLLDPETNINIGTSYLQYVYQ 566
Cdd:COG0741 110 AAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLG--PSPDDLFDPETNIRAGAAYLRELLD 187

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111747 567 QFGNNRIFSSAAYNAGPGRVRTWLGNSAGRidavaFVESIPFSETRGYVKNVLAYDAYYRY 627
Cdd:COG0741 188 RFDGDLVLALAAYNAGPGRVRRWLRRNGDR-----DGEIIPYAETRNYVKKVLANYAIYRA 243
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 477-621 9.35e-42

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: 148.04  E-value: 9.35e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747 477 PLAYNDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPGYSsPGQLLDPETNINI 556
Cdd:cd16896   1 PLKYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAEWIAEKLGLEDFS-EDDLYDPETNIRL 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111747 557 GTSYLQYVYQQFGNNRIFSSAAYNAGPGRVRTWLGNSAGRIDAVAfVESIPFSETRGYVKNVLAY 621
Cdd:cd16896  80 GTWYLSYLLKEFDGNLVLALAAYNAGPGNVDKWLKDGGWSGDGKT-LDQIPFPETRHYVKKVLKN 143
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 484-600 2.86e-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: 140.13  E-value: 2.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747   484 FKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMfsipGYSSPGQLLDPETNINIGTSYLQY 563
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLR----VNPGVDDLFDPEKNIKAGTKYLKE 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 90111747   564 VYQQFGNNRIFSSAAYNAGPGRVRTWLGNSAGRIDAV 600
Cdd:pfam01464  77 LYKQYGGDLWLALAAYNAGPGRVRKWIKNAGAKDKKL 113
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 499-621 2.71e-36

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: 131.57  E-value: 2.71e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747 499 MAIARQESAWNPKVKSPVGASGLMQIMPGTATHtvkmfsiPGYSSPGQLLDPETNINIGTSYLQYVYQQFGNNRIFSSAA 578
Cdd:cd00254   5 LAVIRVESGFNPRAVSPAGARGLMQLMPGTARD-------LGRRGVDDLFDPEENIRAGARYLRELLDRFGGDLELALAA 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 90111747 579 YNAGPGRVRTWLGNsagridavafvESIPFSETRGYVKNVLAY 621
Cdd:cd00254  78 YNAGPGAVDRWGGG-----------EVPPYKETRNYVQRVLAY 109
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 471-627 2.11e-26

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 112.08  E-value: 2.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747 471 HLEERFPlAYNDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTAthtvKMFSIPgysspgQLLDP 550
Cdd:COG4623 256 RIEGRLP-PYDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPATA----KELGVD------DRLDP 324

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747 551 ETNINIGTSYLQYVYQQFGN-----NRI-FSSAAYNAGPGRVR--------------TWLGN--SAGRIDAVAFVESipf 608
Cdd:COG4623 325 EQSIRAGAKYLRWLYDRFPEaidepDRWwFALAAYNAGPGHVQdarrlakkqgldpdRWFDVekSQPKYYDTGYARG--- 401

                       170       180
                ....*....|....*....|
gi 90111747 609 SETRGYVKNVLA-YDAYYRY 627
Cdd:COG4623 402 RETVNYVPNIRAyYDIYKRL 421
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 499-624 3.56e-24

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: 99.15  E-value: 3.56e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747 499 MAIARQESAWNPKVKSPVGASGLMQIMPGTAthtvKMFSIpgysspGQLLDPETNINIGTSYLQYVYQQF-----GNNRI 573
Cdd:cd13403  16 AAQAYQESRFNPNARSPAGARGLMQLMPSTA----RELGV------NDRLDPEQNIHAGAKYLRYLRDRFppdidEPDRL 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111747 574 -FSSAAYNAGPGRVR--------------TWLGN-------SAGRIDAVAFVESIPFSETRGYVKNVLA-YDAY 624
Cdd:cd13403  86 kFALAAYNAGPGHVRdarrlakkyglnpnVWFDNvevlpllKSPYYDPVVKYGYARGRETVNYVRNIRKyYDAY 159
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 493-621 4.72e-24

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: 98.79  E-value: 4.72e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747 493 IPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTV--KMFSIPGYSSPGQLLDPETNINIGTSY---LQYVYQQ 567
Cdd:cd16893  12 VDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVyrLLGGKGGLPSKSYLFDPENNIDIGTAYlhiLQNRYLK 91

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111747 568 FGNN---RIFSS-AAYNAGPGRV-RTWLGN---SAGRI---DAVAFVESI----PFSETRGYVKNVLAY 621
Cdd:cd16893  92 GIKNpksREYCAiAAYNGGAGNVlRTFSSDrkkAISKInrlSPDEVYQHLtkklPAAETRNYLKKVLKA 160
SLT_L pfam14718
Soluble lytic murein transglycosylase L domain; Soluble lytic murein transglycosylase (SLT) ...
 408-472 4.15e-22

Soluble lytic murein transglycosylase L domain; Soluble lytic murein transglycosylase (SLT) consists of three domains, an N-terminal U domain, an L domain (linker domain) and a C-terminal domain (C). The L domain may be involved in the interaction of the enzyme with peptidoglycan.


Pssm-ID: 434154 [Multi-domain]  Cd Length: 68  Bit Score: 89.97  E-value: 4.15e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111747   408 QGPEMARVRELMYWNLDNTARSEWANLVKSKSKTEQAQLARYAFNNQWWDLSVQATIAGKLWDHL 472
Cdd:pfam14718   4 QLPALARIRELLALGRDAEARREWRHLLARLDKEQQLALARLALDWGWHDLAIQATIQAKLWDDL 68
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 501-621 7.34e-14

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: 68.70  E-value: 7.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747 501 IARQESAWNPKVKSPVGASGLMQIMPGTAthtvKMFSIPGYSSPGQLLDPETNINIGTSYLQYVYQQFGNNRIfSSAAYN 580
Cdd:cd16894  13 LALVESGFNPDAVSSAGAAGLWQFMPATA----REYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRFGDWLL-ALAAYN 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 90111747 581 AGPGRVRTWLGNSAGRIDAVAFVESIPFsETRGYVKNVLAY 621
Cdd:cd16894  88 AGEGRVRRAIKRAGTDKWEDYYRLYLPA-ETRRYVPKFLAA 127
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
423-586 1.91e-10

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 62.76  E-value: 1.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  423 LDNTA---RSEW-AN-----LVKSKSKTEQAQLaryafnNQWWDLSVQaTIAgklwDHLEERfplAYNDL-FKRYTSGKE 492
Cdd:PRK11671 138 LDNTGqpiRWEGrASnfadyLLQNKLQSRSNGL------RIIYSVTIN-MVP----NHLDKR---AHKYLpMVRKASRKY 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  493 -IPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTV-KMFSIPGYSSPGQLLDPETNINIGTSY---LQYVYQQ 567
Cdd:PRK11671 204 gVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHTAGKDVfRMKGKSGQPSRSYLFDPANNIDTGTAYlaiLQNVYLG 283

                        170       180
                 ....*....|....*....|...
gi 90111747  568 FGNN----RIFSSAAYNAGPGRV 586
Cdd:PRK11671 284 GITNptsrRYAVITAYNGGAGSV 306
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
471-587 7.55e-10

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 61.81  E-value: 7.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  471 HLEERFPlAYNDLFKRYtsGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHtvkMfsipGYSSPgqlLDP 550
Cdd:PRK10859 282 AIDNRLP-KYQPLFEKY--AGELDWRLLAAIAYQESHWNPQATSPTGVRGLMMLTRNTAQS---M----GVTDR---LDP 348

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 90111747  551 ETNINIGTSYLQYVYQQF-----GNNRI-FSSAAYNAGPGRVR 587
Cdd:PRK10859 349 EQSIRGGARYLQDLMERLpesipEPERIwFALAAYNIGYGHML 391
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 497-560 1.20e-09

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: 54.34  E-value: 1.20e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111747 497 YAMAIARQESAWNPK--VKSPVGASGLMQIMPGTATHTVKmfsipgySSPGQLLDPETNINIGTSY 560
Cdd:cd00442   1 VLAAIIGQESGGNKPanAGSGSGAAGLFQFMPGTWKAYGK-------NSSSDLNDPEASIEAAAKY 59
PHA00658 PHA00658
putative lysin
 502-623 1.40e-08

putative lysin


Pssm-ID: 106967 [Multi-domain]  Cd Length: 720  Bit Score: 57.91  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747  502 ARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPgYSSPGQLLDPETNINIGTSYLQYVYQQFGNNRIFSSAAYNA 581
Cdd:PHA00658 314 GRQFGADGKPLTSPKGAVGIAQVMPDTAPEAAKLAGLP-WDENRYRNDAAYNRALGMAYFQKQLRDFGGDLPKAYAAYNA 392

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 90111747  582 GPGRVRTWLGNSAGRidavAFVESIPfSETRGY-VKNVLAYDA 623
Cdd:PHA00658 393 GPGALQSALKDAKDG----NWLALLP-KETQDYvVKNMQAYNA 430
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 492-584 1.55e-08

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: 52.70  E-value: 1.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747 492 EIPQSYAMAIARQESAWNPK-VKSPVGASGLMQIMPGTAthtvKMFSIPGYSSPGQLL-DPETNInigTSYLQYVYQQFG 569
Cdd:cd13399   2 GVPPGILAAILGVESGFGPNaGGSPAGAQGIAQFMPSTW----KAYGVDGNGDGKADPfNPEDAI---ASAANYLCRHGW 74

                        90       100
                ....*....|....*....|..
gi 90111747 570 NNRIFSS-------AAYNAGPG 584
Cdd:cd13399  75 DLNAFLGednflalAAYNAGPG 96
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 500-589 1.23e-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: 50.22  E-value: 1.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747 500 AIARQESAWNPKVKSPVGAS----GLMQImpgtATHTVKMFSIPGYSSPGQLLDPETNINIGTSYLQYVYQQFGNN--RI 573
Cdd:cd13400  10 AIAKVESGFNPNAINRNKNGsydiGLMQI----NSIWLPELARYGITREELLNDPCTNIYVGAWILARNIKRYGNTwkAV 85

                        90
                ....*....|....*.
gi 90111747 574 fssAAYNAGPGRVRTW 589
Cdd:cd13400  86 ---GAYNSGTPKKNDK 98
PHA00368 PHA00368
internal virion protein D
 477-619 2.54e-07

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 54.02  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111747   477 PLAYNDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPGYsspgqlLDPETNINI 556
Cdd:PHA00368    8 PSEYDGLFQKAADAHGVSYDLLRKVGWDESRFNPTAKSPTGPKGLMQFTKATAKALGLIVDDDDR------LDPELAIDA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111747   557 GTSYLQYVYQQFGNNRIFSSAAYNAGPGRvrtwlgNSAGRIDAVAFVESIPFSET-RGYVKNVL 619
Cdd:PHA00368   82 GARYLADLVGKYDGDELKAALAYNQGEGR------LGAPQLEAYDKGDFASISEEgRNYLRNLL 139
emtA PRK15470
membrane-bound lytic murein transglycosylase EmtA;
500-561 2.72e-05

membrane-bound lytic murein transglycosylase EmtA;


Pssm-ID: 185367 [Multi-domain]  Cd Length: 203  Bit Score: 45.73  E-value: 2.72e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111747  500 AIARQESAWNPKVKSPVGASGLMQIMPGTATHTV-KMFSIPGYSSPGQLLDPETNINIGTSYL 561
Cdd:PRK15470  59 AIIAIESGGNPNAVSKSNAIGLMQLKASTSGRDVyRRMGWSGEPTTSELKNPERNISMGAAYL 121
Cucumo_coat pfam00760
Cucumovirus coat protein;
153-204 1.27e-03

Cucumovirus coat protein;


Pssm-ID: 395617  Cd Length: 175  Bit Score: 40.12  E-value: 1.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 90111747   153 KELWLTGKSQPNACDKLFSVWRA--SGKQDPLAYLERIRLAMKAGNTGLVTVLA 204
Cdd:pfam00760  83 EQLWLTGKKLPASCDLLFAAINAmfADGASNSLIQQRAALAFDANNVGLLTDLS 136
 
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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