NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|503992850|ref|WP_014226844|]
View 

MULTISPECIES: membrane-bound lytic murein transglycosylase MltC [Klebsiella]

Protein Classification

membrane-bound lytic murein transglycosylase C( domain architecture ID 11485457)

membrane-bound lytic murein transglycosylase C catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine residues

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
1-360 0e+00

membrane-bound lytic murein transglycosylase MltC;


:

Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 744.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850   1 MKKYLALALIAPLLVSCSSStKKGAEYNEAWVKDTNGFDILMGQFAHNIENIWGYNEVLLAGPKDYVKYTDQYQTRSHIN 80
Cdd:PRK11671   1 MKKYLALALIAPLLISCSST-KKGDTYNEAWVKDTNGFDILMGQFAHNIENIWGFNEVLIAGPKDYVKYTDQYQTRSHIN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850  81 FDAGTITVETIAGTDPAGRLRQAIIKTLLMGDDPNSIDLYSDVDDIQISKEPFLYGQVVDNTGESIRWEWRASRFADYLL 160
Cdd:PRK11671  80 FDDGTITIETIAGTNPAAHLRQAIIKTLLMGDDPGSIDLYSDVDDIPISKEPFLYGQVLDNTGQPIRWEGRASNFADYLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 161 QTRLKSRSNGPRMIYSITINLVPNHLDKRAHKYIGMVRQASRKYGVDESLILAIMQTESSFNPYAVSHADALGLMQVVQH 240
Cdd:PRK11671 160 QNKLQSRSNGLRIIYSVTINMVPNHLDKRAHKYLPMVRKASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQH 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 241 SAGKDVFRSQGKSGLPSRSYLFDPVNNIDTGTAYLAMLNNVYLSGITNPTSRRYAVITAYNGGAGSVLRVFSSDKVQAAN 320
Cdd:PRK11671 240 TAGKDVFRMKGKSGQPSRSYLFDPANNIDTGTAYLAILQNVYLGGITNPTSRRYAVITAYNGGAGSVLRVFSNDKIQAAN 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 503992850 321 IINNMTPGDVYQTITSRHPSAESRRYLYKVNSAQKGYRRR 360
Cdd:PRK11671 320 IINTMSPGDVYQTLTTRHPSAESRRYLYKVNTAQKSYRRR 359
 
Name Accession Description Interval E-value
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
1-360 0e+00

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 744.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850   1 MKKYLALALIAPLLVSCSSStKKGAEYNEAWVKDTNGFDILMGQFAHNIENIWGYNEVLLAGPKDYVKYTDQYQTRSHIN 80
Cdd:PRK11671   1 MKKYLALALIAPLLISCSST-KKGDTYNEAWVKDTNGFDILMGQFAHNIENIWGFNEVLIAGPKDYVKYTDQYQTRSHIN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850  81 FDAGTITVETIAGTDPAGRLRQAIIKTLLMGDDPNSIDLYSDVDDIQISKEPFLYGQVVDNTGESIRWEWRASRFADYLL 160
Cdd:PRK11671  80 FDDGTITIETIAGTNPAAHLRQAIIKTLLMGDDPGSIDLYSDVDDIPISKEPFLYGQVLDNTGQPIRWEGRASNFADYLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 161 QTRLKSRSNGPRMIYSITINLVPNHLDKRAHKYIGMVRQASRKYGVDESLILAIMQTESSFNPYAVSHADALGLMQVVQH 240
Cdd:PRK11671 160 QNKLQSRSNGLRIIYSVTINMVPNHLDKRAHKYLPMVRKASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQH 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 241 SAGKDVFRSQGKSGLPSRSYLFDPVNNIDTGTAYLAMLNNVYLSGITNPTSRRYAVITAYNGGAGSVLRVFSSDKVQAAN 320
Cdd:PRK11671 240 TAGKDVFRMKGKSGQPSRSYLFDPANNIDTGTAYLAILQNVYLGGITNPTSRRYAVITAYNGGAGSVLRVFSNDKIQAAN 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 503992850 321 IINNMTPGDVYQTITSRHPSAESRRYLYKVNSAQKGYRRR 360
Cdd:PRK11671 320 IINTMSPGDVYQTLTTRHPSAESRRYLYKVNTAQKSYRRR 359
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 196-355 1.69e-98

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: 288.69  E-value: 1.69e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 196 MVRQASRKYGVDESLILAIMQTESSFNPYAVSHADALGLMQVVQHSAGKDVFRSQ-GKSGLPSRSYLFDPVNNIDTGTAY 274
Cdd:cd16893    2 IVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVYRLLgGKGGLPSKSYLFDPENNIDIGTAY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 275 LAMLNNVYLSGITNPTSRRYAVITAYNGGAGSVLRVFSSDKVQAANIINNMTPGDVYQTITSRHPSAESRRYLYKVNSAQ 354
Cdd:cd16893   82 LHILQNRYLKGIKNPKSREYCAIAAYNGGAGNVLRTFSSDRKKAISKINRLSPDEVYQHLTKKLPAAETRNYLKKVLKAK 161


                 .
gi 503992850 355 K 355
Cdd:cd16893  162 K 162
Mltc_N pfam11873
Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found ...
 31-192 2.03e-96

Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found associated with pfam01464. It is the N-terminal structural domain of MltC (Membrane-bound lytic murein transglycosylase C), one of the seven lytic transglycosylases found in the genome of the Gram-negative bacterium Escherichia coli. The role of the N-terminal domain is suggested to be important not as a mere structural extension of the active site beyond what is seen in other lytic transglycosylases but one that creates a peptide-binding site at position +2.


Pssm-ID: 432150  Cd Length: 161  Bit Score: 283.37  E-value: 2.03e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850   31 WVKDTNGFDILMGQFAHNIENIWGYNEVLLAGPKDYVKYTDQYQTRSHINFDAGTITVETIAGTDPAGRLRQAIIKTLLM 110
Cdd:pfam11873   1 FAKDTNALDILVGQFSGNIEKIWGKNEVLVASKKDYVKYTDNYKSRAHIDFDKGIITIETLATKNPKAHLRNAIITTLLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850  111 GDDPNSIDLYSDvDDIQISKEPFLYGQVVDNTGESIRWEWRASRFADYLLQTRLKSRSNGPRMIYSITINLVPNHLDKRA 190
Cdd:pfam11873  81 PDDPSDVDLYSD-KDIELSGKPFLYGQVLDQDGQPIRWEWRANRFADYLIKNKLKTRKKNGKKVYYVSIPMVANHLDQRA 159


                  ..
gi 503992850  191 HK 192
Cdd:pfam11873 160 YK 161
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 188-360 4.00e-44

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: 152.46  E-value: 4.00e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 188 KRAHKYIGMVRQASRKYGVDESLILAIMQTESSFNPYAVSHADALGLMQVVqHSAGKDVFRSQGKSglPSRSYLFDPVNN 267
Cdd:COG0741   98 RRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLM-PATARRLGLKLGLG--PSPDDLFDPETN 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 268 IDTGTAYLAMLNNVYLsgitnptSRRYAVITAYNGGAGSVLRVFSSDKVQAANIInnmtpgdvyqtitsrhPSAESRRYL 347
Cdd:COG0741  175 IRAGAAYLRELLDRFD-------GDLVLALAAYNAGPGRVRRWLRRNGDRDGEII----------------PYAETRNYV 231

                        170
                 ....*....|...
gi 503992850 348 YKVNSAQKGYRRR 360
Cdd:COG0741  232 KKVLANYAIYRAG 244
 
Name Accession Description Interval E-value
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
1-360 0e+00

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 744.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850   1 MKKYLALALIAPLLVSCSSStKKGAEYNEAWVKDTNGFDILMGQFAHNIENIWGYNEVLLAGPKDYVKYTDQYQTRSHIN 80
Cdd:PRK11671   1 MKKYLALALIAPLLISCSST-KKGDTYNEAWVKDTNGFDILMGQFAHNIENIWGFNEVLIAGPKDYVKYTDQYQTRSHIN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850  81 FDAGTITVETIAGTDPAGRLRQAIIKTLLMGDDPNSIDLYSDVDDIQISKEPFLYGQVVDNTGESIRWEWRASRFADYLL 160
Cdd:PRK11671  80 FDDGTITIETIAGTNPAAHLRQAIIKTLLMGDDPGSIDLYSDVDDIPISKEPFLYGQVLDNTGQPIRWEGRASNFADYLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 161 QTRLKSRSNGPRMIYSITINLVPNHLDKRAHKYIGMVRQASRKYGVDESLILAIMQTESSFNPYAVSHADALGLMQVVQH 240
Cdd:PRK11671 160 QNKLQSRSNGLRIIYSVTINMVPNHLDKRAHKYLPMVRKASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQH 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 241 SAGKDVFRSQGKSGLPSRSYLFDPVNNIDTGTAYLAMLNNVYLSGITNPTSRRYAVITAYNGGAGSVLRVFSSDKVQAAN 320
Cdd:PRK11671 240 TAGKDVFRMKGKSGQPSRSYLFDPANNIDTGTAYLAILQNVYLGGITNPTSRRYAVITAYNGGAGSVLRVFSNDKIQAAN 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 503992850 321 IINNMTPGDVYQTITSRHPSAESRRYLYKVNSAQKGYRRR 360
Cdd:PRK11671 320 IINTMSPGDVYQTLTTRHPSAESRRYLYKVNTAQKSYRRR 359
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 196-355 1.69e-98

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: 288.69  E-value: 1.69e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 196 MVRQASRKYGVDESLILAIMQTESSFNPYAVSHADALGLMQVVQHSAGKDVFRSQ-GKSGLPSRSYLFDPVNNIDTGTAY 274
Cdd:cd16893    2 IVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVYRLLgGKGGLPSKSYLFDPENNIDIGTAY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 275 LAMLNNVYLSGITNPTSRRYAVITAYNGGAGSVLRVFSSDKVQAANIINNMTPGDVYQTITSRHPSAESRRYLYKVNSAQ 354
Cdd:cd16893   82 LHILQNRYLKGIKNPKSREYCAIAAYNGGAGNVLRTFSSDRKKAISKINRLSPDEVYQHLTKKLPAAETRNYLKKVLKAK 161


                 .
gi 503992850 355 K 355
Cdd:cd16893  162 K 162
Mltc_N pfam11873
Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found ...
 31-192 2.03e-96

Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found associated with pfam01464. It is the N-terminal structural domain of MltC (Membrane-bound lytic murein transglycosylase C), one of the seven lytic transglycosylases found in the genome of the Gram-negative bacterium Escherichia coli. The role of the N-terminal domain is suggested to be important not as a mere structural extension of the active site beyond what is seen in other lytic transglycosylases but one that creates a peptide-binding site at position +2.


Pssm-ID: 432150  Cd Length: 161  Bit Score: 283.37  E-value: 2.03e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850   31 WVKDTNGFDILMGQFAHNIENIWGYNEVLLAGPKDYVKYTDQYQTRSHINFDAGTITVETIAGTDPAGRLRQAIIKTLLM 110
Cdd:pfam11873   1 FAKDTNALDILVGQFSGNIEKIWGKNEVLVASKKDYVKYTDNYKSRAHIDFDKGIITIETLATKNPKAHLRNAIITTLLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850  111 GDDPNSIDLYSDvDDIQISKEPFLYGQVVDNTGESIRWEWRASRFADYLLQTRLKSRSNGPRMIYSITINLVPNHLDKRA 190
Cdd:pfam11873  81 PDDPSDVDLYSD-KDIELSGKPFLYGQVLDQDGQPIRWEWRANRFADYLIKNKLKTRKKNGKKVYYVSIPMVANHLDQRA 159


                  ..
gi 503992850  191 HK 192
Cdd:pfam11873 160 YK 161
emtA PRK15470
membrane-bound lytic murein transglycosylase EmtA;
188-353 2.18e-44

membrane-bound lytic murein transglycosylase EmtA;


Pssm-ID: 185367 [Multi-domain]  Cd Length: 203  Bit Score: 151.66  E-value: 2.18e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 188 KRAHKYIGMVRQASRKYGVDESLILAIMQTESSFNPYAVSHADALGLMQVVQHSAGKDVFRSQGKSGLPSRSYLFDPVNN 267
Cdd:PRK15470  34 QRAMQWMPISQKAGAAWGVDPQLITAIIAIESGGNPNAVSKSNAIGLMQLKASTSGRDVYRRMGWSGEPTTSELKNPERN 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 268 IDTGTAYLAMLNNVYLSGITNPTSRRYAVITAYNGGAGSVLRVFSSDKVQAANIINNMTPGDVYQTITSRHPSAESRRYL 347
Cdd:PRK15470 114 ISMGAAYLNILETGPLAGIEDPKVLQYALVVSYANGAGALLRTFSSDRKKAISKINDLDADEFLEHVARNHPAPQAPRYI 193


                 ....*.
gi 503992850 348 YKVNSA 353
Cdd:PRK15470 194 YKLEQA 199
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 188-360 4.00e-44

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: 152.46  E-value: 4.00e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 188 KRAHKYIGMVRQASRKYGVDESLILAIMQTESSFNPYAVSHADALGLMQVVqHSAGKDVFRSQGKSglPSRSYLFDPVNN 267
Cdd:COG0741   98 RRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLM-PATARRLGLKLGLG--PSPDDLFDPETN 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 268 IDTGTAYLAMLNNVYLsgitnptSRRYAVITAYNGGAGSVLRVFSSDKVQAANIInnmtpgdvyqtitsrhPSAESRRYL 347
Cdd:COG0741  175 IRAGAAYLRELLDRFD-------GDLVLALAAYNAGPGRVRRWLRRNGDRDGEII----------------PYAETRNYV 231

                        170
                 ....*....|...
gi 503992850 348 YKVNSAQKGYRRR 360
Cdd:COG0741  232 KKVLANYAIYRAG 244
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 197-322 6.14e-34

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: 121.26  E-value: 6.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850  197 VRQASRKYGVDESLILAIMQTESSFNPYAVSHADALGLMQVVQHSAGKDVFRSQgksglPSRSYLFDPVNNIDTGTAYLA 276
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVN-----PGVDDLFDPEKNIKAGTKYLK 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 503992850  277 MLNNVYLsgitnptSRRYAVITAYNGGAGSVLRVFSSDKVQAANII 322
Cdd:pfam01464  76 ELYKQYG-------GDLWLALAAYNAGPGRVRKWIKNAGAKDKKLL 114
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 192-355 1.01e-29

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: 111.45  E-value: 1.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 192 KYIGMVRQASRKYGVDESLILAIMQTESSFNPYAVSHADALGLMQVVQhSAGKDVFrsqGKSGLP--SRSYLFDPVNNID 269
Cdd:cd16896    3 KYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMP-ETAEWIA---EKLGLEdfSEDDLYDPETNIR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 270 TGTAYLAMLNNVYlsgitnpTSRRYAVITAYNGGAGSVLRvfssdkvqaanIINNMTPGDVYQTITsRHPSAESRRYLYK 349
Cdd:cd16896   79 LGTWYLSYLLKEF-------DGNLVLALAAYNAGPGNVDK-----------WLKDGGWSGDGKTLD-QIPFPETRHYVKK 139


                 ....*.
gi 503992850 350 VNSAQK 355
Cdd:cd16896  140 VLKNYK 145
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 193-307 4.83e-26

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: 101.78  E-value: 4.83e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 193 YIGMVRQASRKYGVDESLILAIMQTESSFNPYAVSHADALGLMQVVQhSAGKDVFRSQGKSgLPSRSYLFDPVNNIDTGT 272
Cdd:cd13401    6 YRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMP-ATAKDVAKKLGLP-YYSPRDLFDPEYNIRLGS 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 503992850 273 AYLAML-----NNVYLsgitnptsrryaVITAYNGGAGSV 307
Cdd:cd13401   84 AYLAELldrfdGNPVL------------ALAAYNAGPGRV 111
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 208-355 2.14e-20

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: 85.34  E-value: 2.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 208 ESLILAIMQTESSFNPYAVSHADALGLMQVVQHSAGKDVFRSQgksglpsrSYLFDPVNNIDTGTAYLAMLNNVYLSGIt 287
Cdd:cd00254    1 PALVLAVIRVESGFNPRAVSPAGARGLMQLMPGTARDLGRRGV--------DDLFDPEENIRAGARYLRELLDRFGGDL- 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503992850 288 nptsrrYAVITAYNGGAGSVlrvfssDKVQAANIInnmtpgdvyqtitsrhPSAESRRYLYKVNSAQK 355
Cdd:cd00254   72 ------ELALAAYNAGPGAV------DRWGGGEVP----------------PYKETRNYVQRVLAYYQ 111
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 184-309 2.61e-19

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 88.58  E-value: 2.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 184 NHLDKRAHKYIGMVRQASRKYGVDESLILAIMQTESSFNPYAVSHADALGLMQVVQhSAGKDVfrsqgksGLPSRsylFD 263
Cdd:COG4623  255 RRIEGRLPPYDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMP-ATAKEL-------GVDDR---LD 323

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 503992850 264 PVNNIDTGTAYLAMLNNVYLSGITNPTsRRYAVITAYNGGAGSVLR 309
Cdd:COG4623  324 PEQSIRAGAKYLRWLYDRFPEAIDEPD-RWWFALAAYNAGPGHVQD 368
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 197-309 5.38e-16

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: 74.49  E-value: 5.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 197 VRQASRKYGVDESLILAIMQTESSFNPYAVSHADALGLMQVVqHSAGKDVfrsqgksGLPSRsylFDPVNNIDTGTAYLA 276
Cdd:cd13403    1 FKKYAEKYGFDWRLLAAQAYQESRFNPNARSPAGARGLMQLM-PSTAREL-------GVNDR---LDPEQNIHAGAKYLR 69

                         90       100       110
                 ....*....|....*....|....*....|...
gi 503992850 277 MLNNVYLSGITnPTSRRYAVITAYNGGAGSVLR 309
Cdd:cd13403   70 YLRDRFPPDID-EPDRLKFALAAYNAGPGHVRD 101
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 198-307 7.78e-11

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 63.54  E-value: 7.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 198 RQASRKYGVDESLILAIMQTESSFNPYAVSHADALGLMQVVQHSAGKDVfRSQGKSGLPSRSYLFDPVNNIDTGTAYlam 277
Cdd:PRK11619 484 RRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTV-KMFSIPGYSSSSQLLDPETNINIGTSY--- 559

                         90       100       110
                 ....*....|....*....|....*....|
gi 503992850 278 LNNVYLSGITNptsrRYAVITAYNGGAGSV 307
Cdd:PRK11619 560 LEYVYQQFGNN----RILASAAYNAGPGRV 585
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 204-277 2.27e-08

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: 51.38  E-value: 2.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 204 YGVDESLILAIMQTESSFNPYAVSH-----ADaLGLMQV-VQHsagkdvFRSQGKSGLPSRSYLFDPVNNIDTGTAYLAM 277
Cdd:cd13400    1 YGVPPRLLRAIAKVESGFNPNAINRnkngsYD-IGLMQInSIW------LPELARYGITREELLNDPCTNIYVGAWILAR 73
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 204-306 1.90e-06

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: 46.15  E-value: 1.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 204 YGVDESLILAIMQTESSFNPYAV-SHADALGLMQvvqhsagkdvFrsqgksgLPS------RSYLFDPVNN-IDTGTAYL 275
Cdd:cd13399    1 YGVPPGILAAILGVESGFGPNAGgSPAGAQGIAQ----------F-------MPStwkaygVDGNGDGKADpFNPEDAIA 63

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503992850 276 AMLNnvYLSGI-----TNPTSRRYAVITAYNGGAGS 306
Cdd:cd13399   64 SAAN--YLCRHgwdlnAFLGEDNFLALAAYNAGPGA 97
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 202-349 3.77e-06

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: 45.59  E-value: 3.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 202 RKYGVDESLI-LAImqTESSFNPYAVSHADALGLMQvvqhsagkdvF-RSQGKS-GLPSRSYL---FDPVNNIDTGTAYL 275
Cdd:cd16894    2 LKEGLPEELKyLAL--VESGFNPDAVSSAGAAGLWQ----------FmPATAREyGLRVDSWVderRDPEKSTRAAARYL 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503992850 276 ----AMLNNVYLsgitnptsrryaVITAYNGGAGSVLRVFssdkvqaaniinNMTPGDVYQTITSRHPSAESRRYLYK 349
Cdd:cd16894   70 kdlyKRFGDWLL------------ALAAYNAGEGRVRRAI------------KRAGTDKWEDYYRLYLPAETRRYVPK 123
PHA00368 PHA00368
internal virion protein D
 191-278 3.60e-05

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 45.93  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850  191 HKYIGMVRQASRKYGVDESLILAIMQTESSFNPYAVSHADALGLMQVvqhsaGKDVFRSQGKSGLPSRSYlfDPVNNIDT 270
Cdd:PHA00368    9 SEYDGLFQKAADAHGVSYDLLRKVGWDESRFNPTAKSPTGPKGLMQF-----TKATAKALGLIVDDDDRL--DPELAIDA 81


                  ....*...
gi 503992850  271 GTAYLAML 278
Cdd:PHA00368   82 GARYLADL 89
PRK15328 PRK15328
type III secretion system invasion protein IagB;
199-303 9.45e-05

type III secretion system invasion protein IagB;


Pssm-ID: 185228 [Multi-domain]  Cd Length: 160  Bit Score: 42.16  E-value: 9.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 199 QASRKYGVDESLILAIMQTESSFNPYAVSH----ADALGLMQVvqHSAGkdvFRSQGKSGLPSRSYLFDPVNNIDTGTAY 274
Cdd:PRK15328  24 QAEKMFNIESELLYAIAQQESAMKPGAIGHnrdgSTDLGLMQI--NSFH---MKRLKKMGISEKQLLQDPCISVIVGASI 98

                         90       100
                 ....*....|....*....|....*....
gi 503992850 275 LAMLNNVYlsgitnptSRRYAVITAYNGG 303
Cdd:PRK15328  99 LSDMMKIY--------GYSWEAVGAYNAG 119
GEWL cd01021
Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; ...
 188-307 8.63e-04

Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; GEWL) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). Mammals have two lysozymes. This family corresponds to human and mouse lysozyme G-like protein 2.


Pssm-ID: 381601 [Multi-domain]  Cd Length: 174  Bit Score: 39.89  E-value: 8.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 188 KRAHKYIGMVRQASRKYGVDESLILAIMQTESSF-----NPYAVSHADALGLMQV-VQHSAGKDVFRSQgksglpsrsyl 261
Cdd:cd01021   32 NRLNKYKDCIKQVGKKLCIDPALIAAIISRESRAgaaldKNGWGDHGNGFGLMQVdKRYHPPKGAWDSE----------- 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503992850 262 fdpvNNIDTGTAYLAmlnnVYLSGITN--PT-SRRYAV---ITAYNGGAGSV 307
Cdd:cd01021  101 ----EHIEQATGILI----DFIKTVQRkhPSwSPEQQLkggIAAYNAGVGNV 144
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
184-308 1.75e-03

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 40.24  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 184 NHLDKRAHKYIGMVRQASRkyGVDESLILAIMQTESSFNPYAVSHADALGLMQVVQHSAgKDVfrsqgksGLPSRsylFD 263
Cdd:PRK10859 281 RAIDNRLPKYQPLFEKYAG--ELDWRLLAAIAYQESHWNPQATSPTGVRGLMMLTRNTA-QSM-------GVTDR---LD 347

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 503992850 264 PVNNIDTGTAYLAMLNNVYLSGITNPTSRRYAvITAYNGGAGSVL 308
Cdd:PRK10859 348 PEQSIRGGARYLQDLMERLPESIPEPERIWFA-LAAYNIGYGHML 391
CwlT-like cd16891
CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall ...
 193-305 1.91e-03

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: 38.35  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 193 YIGMVRQASRKYGVDE--SLILAIMQTESSFNpyavshadalglmqvvqhsaGKDVFRSQGKSGLPSRSYLfDPVNNIDT 270
Cdd:cd16891    1 YRPLVEKEAKKYGIPEyvPLILAIIMQESGGK--------------------GPDIMQSSESAGLPPNTIT-DPEESIEQ 59

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 503992850 271 GTAYLAmlnNVYLSGITNpTSRRYAVITAYNGGAG 305
Cdd:cd16891   60 GVKYFA---DVLKKAKGK-GVDIWTAVQAYNFGGG 90
LT_VirB1-like cd16892
VirB1-like subfamily; This subfamily includes VirB1 protein, one of twelve proteins making up ...
 205-313 8.98e-03

VirB1-like subfamily; This subfamily includes VirB1 protein, one of twelve proteins making up type IV secretion systems (T4SS). T4SS are macromolecular assemblies generally composed of VirB1-11 and VirD4 proteins, and are used by bacteria to transport material across their membranes. VirB1 acts as a lytic transglycosylase (LT), and is important with respect to piercing the peptidoglycan layer in the periplasm. 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, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381613 [Multi-domain]  Cd Length: 143  Bit Score: 36.37  E-value: 8.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992850 205 GVDESLILAIMQTESSFNPYAV------------SHADA---------------LGLMQV-VQHsagkdvFRSQGKSGlp 256
Cdd:cd16892    8 GVHPETLAAIVQVESGGNPYAIgvnggklsrqpkTKAEAiatarqliaaghnfdVGLGQInSRN------LARLGLTV-- 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503992850 257 srSYLFDPVNNIDTGTAYLAMLNNVYLSGITNPTSRRYAVITAYNGG-------AGSVLRVFSS 313
Cdd:cd16892   80 --EDVFDPCTNLKAGATILTECYARAKKTGGDGQAALRAALSCYNTGnftrgfsNGYVQKVVAA 141
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH