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Conserved domains on  [gi|1070053496|gb|OEI61785|]
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murein transglycosylase [Escherichia coli]

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: 1344.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496   1 MEKAKHVTWRLLAAGVCLLTVSSVARADSLDEQRSRYAQIKQAWDNRQMDVVEQMMPGLKDYPLYPYLEYRQITDDLMNQ 80
Cdd:PRK11619    1 MEKAKMGKWRLLAAGVCLLTVSGVARADSLDEQRQRYQQIKQAWDNRQMDVVEQLMPTLKDYPLYPYLEYRQLTQDLMNQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496  81 PAVTVTNFVSANPTLPPARTLQSRFVNELARREDWRGLLAFSPEKPGTTEAQCNYYYAKWNTGQSEEAWQGAKELWLTGK 160
Cdd:PRK11619   81 PAVQVTNFIRANPTLPPARSLQSRFVNELARREDWRGLLAFSPEKPKPVEARCNYYYAKWATGQQQEAWQGAKELWLTGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 161 SQPNACDKLFSVWRASGKQDPLAYLERIRLAMKAGNTGLVTVLAGQMPADYQTIASAIISLANNPNTVLTFARTTGATDF 240
Cdd:PRK11619  161 SLPNACDKLFSVWQQSGKQDPLAYLERIRLAMKAGNTGLVTYLAKQLPADYQTIASALIKLQNDPNTVETFARTTGPTDF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 241 TRQMAAVAFASVARQDAENARLMIPSLAQAQQLNEDQIQELRDIVAWRLMGNDVTDEQAKWRDDAIMRSQSTSLIERRVR 320
Cdd:PRK11619  241 TRQMAAVAFASVARQDAENARLMIPSLVRAQKLNEDQRQELRDIVAWRLMGNDVTDEQAKWRDDVIMRSQSTSLLERRVR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 321 MALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLERGREAEAKEILHQLMQQRGFYPMVAAQRIGEEYELKIDKAPQ 400
Cdd:PRK11619  321 MALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLEQGRKAEAEEILRQLMQQRGFYPMVAAQRLGEEYPLKIDKAPK 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 401 nVDSALTQGPEMARVRELMYWNLDNTARSEWANLVKSKSKTEQAQLARYAFNNQWWDLSVQATIAGKLWDHLEERFPLAY 480
Cdd:PRK11619  401 -PDSALTQGPEMARVRELMYWNMDNTARSEWANLVASRSKTEQAQLARYAFNQQWWDLSVQATIAGKLWDHLEERFPLAW 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 481 KDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPGYSSPGQLLDPETNINIGTSY 560
Cdd:PRK11619  480 NDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFSIPGYSSSSQLLDPETNINIGTSY 559

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 561 LQYVYQQFGNNRIFSSAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGDKPTLMSATE 640
Cdd:PRK11619  560 LEYVYQQFGNNRILASAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGQKPTLLSDAE 639


                  ....*
gi 1070053496 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: 1344.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496   1 MEKAKHVTWRLLAAGVCLLTVSSVARADSLDEQRSRYAQIKQAWDNRQMDVVEQMMPGLKDYPLYPYLEYRQITDDLMNQ 80
Cdd:PRK11619    1 MEKAKMGKWRLLAAGVCLLTVSGVARADSLDEQRQRYQQIKQAWDNRQMDVVEQLMPTLKDYPLYPYLEYRQLTQDLMNQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496  81 PAVTVTNFVSANPTLPPARTLQSRFVNELARREDWRGLLAFSPEKPGTTEAQCNYYYAKWNTGQSEEAWQGAKELWLTGK 160
Cdd:PRK11619   81 PAVQVTNFIRANPTLPPARSLQSRFVNELARREDWRGLLAFSPEKPKPVEARCNYYYAKWATGQQQEAWQGAKELWLTGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 161 SQPNACDKLFSVWRASGKQDPLAYLERIRLAMKAGNTGLVTVLAGQMPADYQTIASAIISLANNPNTVLTFARTTGATDF 240
Cdd:PRK11619  161 SLPNACDKLFSVWQQSGKQDPLAYLERIRLAMKAGNTGLVTYLAKQLPADYQTIASALIKLQNDPNTVETFARTTGPTDF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 241 TRQMAAVAFASVARQDAENARLMIPSLAQAQQLNEDQIQELRDIVAWRLMGNDVTDEQAKWRDDAIMRSQSTSLIERRVR 320
Cdd:PRK11619  241 TRQMAAVAFASVARQDAENARLMIPSLVRAQKLNEDQRQELRDIVAWRLMGNDVTDEQAKWRDDVIMRSQSTSLLERRVR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 321 MALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLERGREAEAKEILHQLMQQRGFYPMVAAQRIGEEYELKIDKAPQ 400
Cdd:PRK11619  321 MALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLEQGRKAEAEEILRQLMQQRGFYPMVAAQRLGEEYPLKIDKAPK 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 401 nVDSALTQGPEMARVRELMYWNLDNTARSEWANLVKSKSKTEQAQLARYAFNNQWWDLSVQATIAGKLWDHLEERFPLAY 480
Cdd:PRK11619  401 -PDSALTQGPEMARVRELMYWNMDNTARSEWANLVASRSKTEQAQLARYAFNQQWWDLSVQATIAGKLWDHLEERFPLAW 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 481 KDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPGYSSPGQLLDPETNINIGTSY 560
Cdd:PRK11619  480 NDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFSIPGYSSSSQLLDPETNINIGTSY 559

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 561 LQYVYQQFGNNRIFSSAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGDKPTLMSATE 640
Cdd:PRK11619  560 LEYVYQQFGNNRILASAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGQKPTLLSDAE 639


                  ....*
gi 1070053496 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 4.43e-68

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: 218.89  E-value: 4.43e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 475 RFPLAYKDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPgYSSPGQLLDPETNI 554
Cdd:cd13401     1 RYPLPYRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLP-YYSPRDLFDPEYNI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1070053496 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 3.18e-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: 174.80  E-value: 3.18e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 411 EMARVRELMYWNLDNTARSEWANLVKSKSKTEQAQLARYAFNNQWWDLSVQA----TIAGKLWDHLEERFPLAYKDLFKR 486
Cdd:COG0741    30 AAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAiaalAAELLALAALLLRRPLPYLPLIEE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 487 YTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPgySSPGQLLDPETNINIGTSYLQYVYQ 566
Cdd:COG0741   110 AAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLG--PSPDDLFDPETNIRAGAAYLRELLD 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1070053496 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 2.37e-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: 2.37e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 484 FKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMfsipGYSSPGQLLDPETNINIGTSYLQY 563
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLR----VNPGVDDLFDPEKNIKAGTKYLKE 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1070053496 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: 1344.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496   1 MEKAKHVTWRLLAAGVCLLTVSSVARADSLDEQRSRYAQIKQAWDNRQMDVVEQMMPGLKDYPLYPYLEYRQITDDLMNQ 80
Cdd:PRK11619    1 MEKAKMGKWRLLAAGVCLLTVSGVARADSLDEQRQRYQQIKQAWDNRQMDVVEQLMPTLKDYPLYPYLEYRQLTQDLMNQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496  81 PAVTVTNFVSANPTLPPARTLQSRFVNELARREDWRGLLAFSPEKPGTTEAQCNYYYAKWNTGQSEEAWQGAKELWLTGK 160
Cdd:PRK11619   81 PAVQVTNFIRANPTLPPARSLQSRFVNELARREDWRGLLAFSPEKPKPVEARCNYYYAKWATGQQQEAWQGAKELWLTGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 161 SQPNACDKLFSVWRASGKQDPLAYLERIRLAMKAGNTGLVTVLAGQMPADYQTIASAIISLANNPNTVLTFARTTGATDF 240
Cdd:PRK11619  161 SLPNACDKLFSVWQQSGKQDPLAYLERIRLAMKAGNTGLVTYLAKQLPADYQTIASALIKLQNDPNTVETFARTTGPTDF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 241 TRQMAAVAFASVARQDAENARLMIPSLAQAQQLNEDQIQELRDIVAWRLMGNDVTDEQAKWRDDAIMRSQSTSLIERRVR 320
Cdd:PRK11619  241 TRQMAAVAFASVARQDAENARLMIPSLVRAQKLNEDQRQELRDIVAWRLMGNDVTDEQAKWRDDVIMRSQSTSLLERRVR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 321 MALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLERGREAEAKEILHQLMQQRGFYPMVAAQRIGEEYELKIDKAPQ 400
Cdd:PRK11619  321 MALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLEQGRKAEAEEILRQLMQQRGFYPMVAAQRLGEEYPLKIDKAPK 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 401 nVDSALTQGPEMARVRELMYWNLDNTARSEWANLVKSKSKTEQAQLARYAFNNQWWDLSVQATIAGKLWDHLEERFPLAY 480
Cdd:PRK11619  401 -PDSALTQGPEMARVRELMYWNMDNTARSEWANLVASRSKTEQAQLARYAFNQQWWDLSVQATIAGKLWDHLEERFPLAW 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 481 KDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPGYSSPGQLLDPETNINIGTSY 560
Cdd:PRK11619  480 NDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFSIPGYSSSSQLLDPETNINIGTSY 559

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 561 LQYVYQQFGNNRIFSSAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGDKPTLMSATE 640
Cdd:PRK11619  560 LEYVYQQFGNNRILASAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGQKPTLLSDAE 639


                  ....*
gi 1070053496 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 4.43e-68

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: 218.89  E-value: 4.43e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 475 RFPLAYKDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPgYSSPGQLLDPETNI 554
Cdd:cd13401     1 RYPLPYRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLP-YYSPRDLFDPEYNI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1070053496 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 3.18e-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: 174.80  E-value: 3.18e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 411 EMARVRELMYWNLDNTARSEWANLVKSKSKTEQAQLARYAFNNQWWDLSVQA----TIAGKLWDHLEERFPLAYKDLFKR 486
Cdd:COG0741    30 AAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAiaalAAELLALAALLLRRPLPYLPLIEE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 487 YTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPgySSPGQLLDPETNINIGTSYLQYVYQ 566
Cdd:COG0741   110 AAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLG--PSPDDLFDPETNIRAGAAYLRELLD 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1070053496 567 QFGNNRIFSSAAYNAGPGRVRTWLGNSAGRidavaFVESIPFSETRGYVKNVLAYDAYYRY 627
Cdd:COG0741   188 RFDGDLVLALAAYNAGPGRVRRWLRRNGDR-----DGEIIPYAETRNYVKKVLANYAIYRA 243
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 477-621 9.71e-43

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: 150.74  E-value: 9.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 477 PLAYKDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPGYSsPGQLLDPETNINI 556
Cdd:cd16896     1 PLKYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAEWIAEKLGLEDFS-EDDLYDPETNIRL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1070053496 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 2.37e-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: 2.37e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 484 FKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMfsipGYSSPGQLLDPETNINIGTSYLQY 563
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLR----VNPGVDDLFDPEKNIKAGTKYLKE 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1070053496 564 VYQQFGNNRIFSSAAYNAGPGRVRTWLGNSAGRIDAV 600
Cdd:pfam01464  77 LYKQYGGDLWLALAAYNAGPGRVRKWIKNAGAKDKKL 113
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 499-621 2.11e-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: 131.95  E-value: 2.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 499 MAIARQESAWNPKVKSPVGASGLMQIMPGTATHtvkmfsiPGYSSPGQLLDPETNINIGTSYLQYVYQQFGNNRIFSSAA 578
Cdd:cd00254     5 LAVIRVESGFNPRAVSPAGARGLMQLMPGTARD-------LGRRGVDDLFDPEENIRAGARYLRELLDRFGGDLELALAA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1070053496 579 YNAGPGRVRTWLGNsagridavafvESIPFSETRGYVKNVLAY 621
Cdd:cd00254    78 YNAGPGAVDRWGGG-----------EVPPYKETRNYVQRVLAY 109
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 471-627 5.07e-27

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 114.00  E-value: 5.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 471 HLEERFPlAYKDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTAthtvKMFSIPgysspgQLLDP 550
Cdd:COG4623   256 RIEGRLP-PYDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPATA----KELGVD------DRLDP 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 551 ETNINIGTSYLQYVYQQFGN-----NRI-FSSAAYNAGPGRVR--------------TWLGN--SAGRIDAVAFVESipf 608
Cdd:COG4623   325 EQSIRAGAKYLRWLYDRFPEaidepDRWwFALAAYNAGPGHVQdarrlakkqgldpdRWFDVekSQPKYYDTGYARG--- 401

                         170       180
                  ....*....|....*....|
gi 1070053496 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 2.96e-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: 99.53  E-value: 2.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 499 MAIARQESAWNPKVKSPVGASGLMQIMPGTAthtvKMFSIpgysspGQLLDPETNINIGTSYLQYVYQQF-----GNNRI 573
Cdd:cd13403    16 AAQAYQESRFNPNARSPAGARGLMQLMPSTA----RELGV------NDRLDPEQNIHAGAKYLRYLRDRFppdidEPDRL 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1070053496 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 4.50e-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: 4.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 493 IPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTV--KMFSIPGYSSPGQLLDPETNINIGTSY---LQYVYQQ 567
Cdd:cd16893    12 VDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVyrLLGGKGGLPSKSYLFDPENNIDIGTAYlhiLQNRYLK 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1070053496 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 3.65e-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: 90.36  E-value: 3.65e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1070053496 408 QGPEMARVRELMYWNLDNTARSEWANLVKSKSKTEQAQLARYAFNNQWWDLSVQATIAGKLWDHL 472
Cdd:pfam14718   4 QLPALARIRELLALGRDAEARREWRHLLARLDKEQQLALARLALDWGWHDLAIQATIQAKLWDDL 68
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 501-621 6.86e-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: 6.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 501 IARQESAWNPKVKSPVGASGLMQIMPGTAthtvKMFSIPGYSSPGQLLDPETNINIGTSYLQYVYQQFGNNRIfSSAAYN 580
Cdd:cd16894    13 LALVESGFNPDAVSSAGAAGLWQFMPATA----REYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRFGDWLL-ALAAYN 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1070053496 581 AGPGRVRTWLGNSAGRIDAVAFVESIPFsETRGYVKNVLAY 621
Cdd:cd16894    88 AGEGRVRRAIKRAGTDKWEDYYRLYLPA-ETRRYVPKFLAA 127
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
423-586 1.98e-11

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 65.84  E-value: 1.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 423 LDNTA---RSEW-AN-----LVKSKSKTEQAQLaryafnNQWWDLSVQaTIAgklwDHLEERfplAYKDL-FKRYTSGKE 492
Cdd:PRK11671  138 LDNTGqpiRWEGrASnfadyLLQNKLQSRSNGL------RIIYSVTIN-MVP----NHLDKR---AHKYLpMVRKASRKY 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 493 -IPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTV-KMFSIPGYSSPGQLLDPETNINIGTSY---LQYVYQQ 567
Cdd:PRK11671  204 gVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHTAGKDVfRMKGKSGQPSRSYLFDPANNIDTGTAYlaiLQNVYLG 283

                         170       180
                  ....*....|....*....|...
gi 1070053496 568 FGNN----RIFSSAAYNAGPGRV 586
Cdd:PRK11671  284 GITNptsrRYAVITAYNGGAGSV 306
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
471-587 2.32e-10

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 63.35  E-value: 2.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 471 HLEERFPlAYKDLFKRYtsGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHtvkMfsipGYSSPgqlLDP 550
Cdd:PRK10859  282 AIDNRLP-KYQPLFEKY--AGELDWRLLAAIAYQESHWNPQATSPTGVRGLMMLTRNTAQS---M----GVTDR---LDP 348

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1070053496 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 1.11e-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: 1.11e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1070053496 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 1070053496 502 ARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPgYSSPGQLLDPETNINIGTSYLQYVYQQFGNNRIFSSAAYNA 581
Cdd:PHA00658  314 GRQFGADGKPLTSPKGAVGIAQVMPDTAPEAAKLAGLP-WDENRYRNDAAYNRALGMAYFQKQLRDFGGDLPKAYAAYNA 392

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1070053496 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 1.54e-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: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 492 EIPQSYAMAIARQESAWNPK-VKSPVGASGLMQIMPGTAthtvKMFSIPGYSSPGQLL-DPETNInigTSYLQYVYQQFG 569
Cdd:cd13399     2 GVPPGILAAILGVESGFGPNaGGSPAGAQGIAQFMPSTW----KAYGVDGNGDGKADPfNPEDAI---ASAANYLCRHGW 74

                          90       100
                  ....*....|....*....|..
gi 1070053496 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 1.14e-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: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496 500 AIARQESAWNPKVKSPVGAS----GLMQImpgtATHTVKMFSIPGYSSPGQLLDPETNINIGTSYLQYVYQQFGNN--RI 573
Cdd:cd13400    10 AIAKVESGFNPNAINRNKNGsydiGLMQI----NSIWLPELARYGITREELLNDPCTNIYVGAWILARNIKRYGNTwkAV 85

                          90
                  ....*....|....*.
gi 1070053496 574 fssAAYNAGPGRVRTW 589
Cdd:cd13400    86 ---GAYNSGTPKKNDK 98
PHA00368 PHA00368
internal virion protein D
 477-619 3.33e-07

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 53.63  E-value: 3.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070053496  477 PLAYKDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPGYsspgqlLDPETNINI 556
Cdd:PHA00368     8 PSEYDGLFQKAADAHGVSYDLLRKVGWDESRFNPTAKSPTGPKGLMQFTKATAKALGLIVDDDDR------LDPELAIDA 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1070053496  557 GTSYLQYVYQQFGNNRIFSSAAYNAGPGRvrtwlgNSAGRIDAVAFVESIPFSET-RGYVKNVL 619
Cdd:PHA00368    82 GARYLADLVGKYDGDELKAALAYNQGEGR------LGAPQLEAYDKGDFASISEEgRNYLRNLL 139
emtA PRK15470
membrane-bound lytic murein transglycosylase EmtA;
500-561 2.64e-05

membrane-bound lytic murein transglycosylase EmtA;


Pssm-ID: 185367 [Multi-domain]  Cd Length: 203  Bit Score: 45.73  E-value: 2.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1070053496 500 AIARQESAWNPKVKSPVGASGLMQIMPGTATHTV-KMFSIPGYSSPGQLLDPETNINIGTSYL 561
Cdd:PRK15470   59 AIIAIESGGNPNAVSKSNAIGLMQLKASTSGRDVyRRMGWSGEPTTSELKNPERNISMGAAYL 121
Cucumo_coat pfam00760
Cucumovirus coat protein;
153-204 1.21e-03

Cucumovirus coat protein;


Pssm-ID: 395617  Cd Length: 175  Bit Score: 40.12  E-value: 1.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1070053496 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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