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Conserved domains on  [gi|695695446|ref|WP_032636527|]
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transglycosylase SLT domain-containing protein [Enterobacter sp. MGH 15]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Lyz-like super family cl00222
lysozyme-like domains; This family contains several members, including soluble lytic ...
232-356 5.11e-16

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.


The actual alignment was detected with superfamily member cd16894:

Pssm-ID: 469668 [Multi-domain]  Cd Length: 129  Bit Score: 75.25  E-value: 5.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 232 DMRSVGIVESGgkhLNSDgsiVTSSAGAQGRFQLMPETGKELaarrGLKYNPA-DEQQHTMLASD----YAQELSNKYGS 306
Cdd:cd16894    9 ELKYLALVESG---FNPD---AVSSAGAAGLWQFMPATAREY----GLRVDSWvDERRDPEKSTRaaarYLKDLYKRFGD 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 695695446 307 ELLAGAAYNWGQGNVDKLIEKIGDPrkgeISQADFIKKLPSETQGWISRY 356
Cdd:cd16894   79 WLLALAAYNAGEGRVRRAIKRAGTD----KWEDYYRLYLPAETRRYVPKF 124
PHA00658 super family cl29091
putative lysin
1-355 5.94e-15

putative lysin


The actual alignment was detected with superfamily member PHA00658:

Pssm-ID: 106967 [Multi-domain]  Cd Length: 720  Bit Score: 79.10  E-value: 5.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446   1 MPTVP----------TVTGRQVESRGFQSPGFQAFEQPNVGDVISQVAPK---------------AIDMFAQAKQ-RANV 54
Cdd:PHA00658   1 MPRVPvydspqvspnTVPQARLATPSFATPTFRGADAPAFQDTANQQARQfsqgarqfsndvgriADSMVQQANQlRVDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446  55 AL--SQEASLKLSQaeeDLKTQLYSLKGQNAIGK------GQEFTQQYDEQIQSLASSLPDDASRQMFMQQAQQQRIQFQ 126
Cdd:PHA00658  81 ALnrAKEAALRLTY---DKDTGFANLKGINALERpegkplADEYGDNLKKQLDEISGTLGNDAQRRAFALHSNDILTSFR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 127 GNVGRYEQGQVSEFEGNQYDATRQLQIQKEADAWNNPQEAILAKNIRTVATAR----FGASRGWSQEQ------------ 190
Cdd:PHA00658 158 GQAVQHEASEYKTYALSTSEGIQSTALRDIALNWNNPDAINSAVDRIKAETFRqaqlLGKSAEWQEAQarkltsnahkia 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 191 ILAAIEKDNLAATEMRAKNYAvdnplgwmnGEFSADD--------TGGLDMRS--------VGIV--------------- 239
Cdd:PHA00658 238 LMSALEQNNPTYASAYLNKYS---------GQMDADDiltvrghiTKDMDGRAglaaatdaVGKVpiqvsdgerafniav 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 240 --ESGGKHLNSDGSIVTSSAGAQGRFQLMPETGKELAARRGLKYNP----ADEQQHTMLASDYAQELSNKYGSEL-LAGA 312
Cdd:PHA00658 309 gtESGGRQFGADGKPLTSPKGAVGIAQVMPDTAPEAAKLAGLPWDEnryrNDAAYNRALGMAYFQKQLRDFGGDLpKAYA 388
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 695695446 313 AYNWGQGNVDKLIEKIGDprkgeisqADFIKKLPSETQGWISR 355
Cdd:PHA00658 389 AYNAGPGALQSALKDAKD--------GNWLALLPKETQDYVVK 423
 
Name Accession Description Interval E-value
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
232-356 5.11e-16

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: 75.25  E-value: 5.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 232 DMRSVGIVESGgkhLNSDgsiVTSSAGAQGRFQLMPETGKELaarrGLKYNPA-DEQQHTMLASD----YAQELSNKYGS 306
Cdd:cd16894    9 ELKYLALVESG---FNPD---AVSSAGAAGLWQFMPATAREY----GLRVDSWvDERRDPEKSTRaaarYLKDLYKRFGD 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 695695446 307 ELLAGAAYNWGQGNVDKLIEKIGDPrkgeISQADFIKKLPSETQGWISRY 356
Cdd:cd16894   79 WLLALAAYNAGEGRVRRAIKRAGTD----KWEDYYRLYLPAETRRYVPKF 124
PHA00658 PHA00658
putative lysin
1-355 5.94e-15

putative lysin


Pssm-ID: 106967 [Multi-domain]  Cd Length: 720  Bit Score: 79.10  E-value: 5.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446   1 MPTVP----------TVTGRQVESRGFQSPGFQAFEQPNVGDVISQVAPK---------------AIDMFAQAKQ-RANV 54
Cdd:PHA00658   1 MPRVPvydspqvspnTVPQARLATPSFATPTFRGADAPAFQDTANQQARQfsqgarqfsndvgriADSMVQQANQlRVDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446  55 AL--SQEASLKLSQaeeDLKTQLYSLKGQNAIGK------GQEFTQQYDEQIQSLASSLPDDASRQMFMQQAQQQRIQFQ 126
Cdd:PHA00658  81 ALnrAKEAALRLTY---DKDTGFANLKGINALERpegkplADEYGDNLKKQLDEISGTLGNDAQRRAFALHSNDILTSFR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 127 GNVGRYEQGQVSEFEGNQYDATRQLQIQKEADAWNNPQEAILAKNIRTVATAR----FGASRGWSQEQ------------ 190
Cdd:PHA00658 158 GQAVQHEASEYKTYALSTSEGIQSTALRDIALNWNNPDAINSAVDRIKAETFRqaqlLGKSAEWQEAQarkltsnahkia 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 191 ILAAIEKDNLAATEMRAKNYAvdnplgwmnGEFSADD--------TGGLDMRS--------VGIV--------------- 239
Cdd:PHA00658 238 LMSALEQNNPTYASAYLNKYS---------GQMDADDiltvrghiTKDMDGRAglaaatdaVGKVpiqvsdgerafniav 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 240 --ESGGKHLNSDGSIVTSSAGAQGRFQLMPETGKELAARRGLKYNP----ADEQQHTMLASDYAQELSNKYGSEL-LAGA 312
Cdd:PHA00658 309 gtESGGRQFGADGKPLTSPKGAVGIAQVMPDTAPEAAKLAGLPWDEnryrNDAAYNRALGMAYFQKQLRDFGGDLpKAYA 388
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 695695446 313 AYNWGQGNVDKLIEKIGDprkgeisqADFIKKLPSETQGWISR 355
Cdd:PHA00658 389 AYNAGPGALQSALKDAKD--------GNWLALLPKETQDYVVK 423
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
239-336 1.38e-14

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: 74.26  E-value: 1.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 239 VESGGkhlNSDgsiVTSSAGAQGRFQLMPETGKELAARRGLKYNPA---DEQQHTMLASDYAQELSNKY-GSELLAGAAY 314
Cdd:COG0741  127 QESAF---NPN---AVSPAGARGLMQLMPATARRLGLKLGLGPSPDdlfDPETNIRAGAAYLRELLDRFdGDLVLALAAY 200
                         90       100
                 ....*....|....*....|..
gi 695695446 315 NWGQGNVDKLIEKIGDPRKGEI 336
Cdd:COG0741  201 NAGPGRVRRWLRRNGDRDGEII 222
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
238-331 2.66e-07

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: 50.00  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446  238 IVESGGkhlNSDgsiVTSSAGAQGRFQLMPETGKELAARRGLKYNPA-DEQQHTMLASDYAQELSNKYG-SELLAGAAYN 315
Cdd:pfam01464  20 QQESGF---NPK---AVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLfDPEKNIKAGTKYLKELYKQYGgDLWLALAAYN 93
                          90
                  ....*....|....*.
gi 695695446  316 WGQGNVDKLIEKIGDP 331
Cdd:pfam01464  94 AGPGRVRKWIKNAGAK 109
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
253-359 1.76e-03

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 41.97  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 253 VTSSAGAQGRFQLMPETGKELAARRGLK-Y-NPA---DEQQHTMLASDYAQELSNKYG-SELLAGAAYNWGQGNVDKLIE 326
Cdd:PRK11619 511 ARSPVGASGLMQIMPGTATHTVKMFSIPgYsSSSqllDPETNINIGTSYLEYVYQQFGnNRILASAAYNAGPGRVRTWLG 590
                         90       100       110
                 ....*....|....*....|....*....|....
gi 695695446 327 KIGdprkGEISQADFIKKLP-SETQGwisrYRKN 359
Cdd:PRK11619 591 NSA----GRIDAVAFVESIPfSETRG----YVKN 616
 
Name Accession Description Interval E-value
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
232-356 5.11e-16

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: 75.25  E-value: 5.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 232 DMRSVGIVESGgkhLNSDgsiVTSSAGAQGRFQLMPETGKELaarrGLKYNPA-DEQQHTMLASD----YAQELSNKYGS 306
Cdd:cd16894    9 ELKYLALVESG---FNPD---AVSSAGAAGLWQFMPATAREY----GLRVDSWvDERRDPEKSTRaaarYLKDLYKRFGD 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 695695446 307 ELLAGAAYNWGQGNVDKLIEKIGDPrkgeISQADFIKKLPSETQGWISRY 356
Cdd:cd16894   79 WLLALAAYNAGEGRVRRAIKRAGTD----KWEDYYRLYLPAETRRYVPKF 124
PHA00658 PHA00658
putative lysin
1-355 5.94e-15

putative lysin


Pssm-ID: 106967 [Multi-domain]  Cd Length: 720  Bit Score: 79.10  E-value: 5.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446   1 MPTVP----------TVTGRQVESRGFQSPGFQAFEQPNVGDVISQVAPK---------------AIDMFAQAKQ-RANV 54
Cdd:PHA00658   1 MPRVPvydspqvspnTVPQARLATPSFATPTFRGADAPAFQDTANQQARQfsqgarqfsndvgriADSMVQQANQlRVDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446  55 AL--SQEASLKLSQaeeDLKTQLYSLKGQNAIGK------GQEFTQQYDEQIQSLASSLPDDASRQMFMQQAQQQRIQFQ 126
Cdd:PHA00658  81 ALnrAKEAALRLTY---DKDTGFANLKGINALERpegkplADEYGDNLKKQLDEISGTLGNDAQRRAFALHSNDILTSFR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 127 GNVGRYEQGQVSEFEGNQYDATRQLQIQKEADAWNNPQEAILAKNIRTVATAR----FGASRGWSQEQ------------ 190
Cdd:PHA00658 158 GQAVQHEASEYKTYALSTSEGIQSTALRDIALNWNNPDAINSAVDRIKAETFRqaqlLGKSAEWQEAQarkltsnahkia 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 191 ILAAIEKDNLAATEMRAKNYAvdnplgwmnGEFSADD--------TGGLDMRS--------VGIV--------------- 239
Cdd:PHA00658 238 LMSALEQNNPTYASAYLNKYS---------GQMDADDiltvrghiTKDMDGRAglaaatdaVGKVpiqvsdgerafniav 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 240 --ESGGKHLNSDGSIVTSSAGAQGRFQLMPETGKELAARRGLKYNP----ADEQQHTMLASDYAQELSNKYGSEL-LAGA 312
Cdd:PHA00658 309 gtESGGRQFGADGKPLTSPKGAVGIAQVMPDTAPEAAKLAGLPWDEnryrNDAAYNRALGMAYFQKQLRDFGGDLpKAYA 388
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 695695446 313 AYNWGQGNVDKLIEKIGDprkgeisqADFIKKLPSETQGWISR 355
Cdd:PHA00658 389 AYNAGPGALQSALKDAKD--------GNWLALLPKETQDYVVK 423
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
239-336 1.38e-14

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: 74.26  E-value: 1.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 239 VESGGkhlNSDgsiVTSSAGAQGRFQLMPETGKELAARRGLKYNPA---DEQQHTMLASDYAQELSNKY-GSELLAGAAY 314
Cdd:COG0741  127 QESAF---NPN---AVSPAGARGLMQLMPATARRLGLKLGLGPSPDdlfDPETNIRAGAAYLRELLDRFdGDLVLALAAY 200
                         90       100
                 ....*....|....*....|..
gi 695695446 315 NWGQGNVDKLIEKIGDPRKGEI 336
Cdd:COG0741  201 NAGPGRVRRWLRRNGDRDGEII 222
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
253-349 1.51e-12

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: 65.96  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 253 VTSSAGAQGRFQLMPETGKELAARRGLKYNPADE----QQHTMLASDYAQELSNKY-GSELLAGAAYNWGQGNVDKLIek 327
Cdd:cd13401   38 AVSPAGALGLMQLMPATAKDVAKKLGLPYYSPRDlfdpEYNIRLGSAYLAELLDRFdGNPVLALAAYNAGPGRVRRWL-- 115
                         90       100
                 ....*....|....*....|...
gi 695695446 328 igdPRKGEISQADFIKKLP-SET 349
Cdd:cd13401  116 ---KRRGDLDPDLWIETIPfSET 135
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
239-359 6.98e-12

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: 63.00  E-value: 6.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 239 VESGGKHLnsdgsiVTSSAGAQGRFQLMPETGKELAarRGLKYNPADEQQHTMLASDYAQELSNKY-GSELLAGAAYNWG 317
Cdd:cd00254   10 VESGFNPR------AVSPAGARGLMQLMPGTARDLG--RRGVDDLFDPEENIRAGARYLRELLDRFgGDLELALAAYNAG 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 695695446 318 QGNVDKLIEKIGDPrkgeisqadfikklPSETQGWISRYRKN 359
Cdd:cd00254   82 PGAVDRWGGGEVPP--------------YKETRNYVQRVLAY 109
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
230-327 1.42e-09

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 61.23  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 230 GLDMR---SVGIVESggkHLNSDgsiVTSSAGAQGRFQLMPETGKELaarrGLKyNPADEQQHTMLASDYAQELSNKYGS 306
Cdd:COG4623  276 GLDWRllaALAYQES---HWNPR---ARSPTGARGLMQLMPATAKEL----GVD-DRLDPEQSIRAGAKYLRWLYDRFPE 344
                         90       100
                 ....*....|....*....|....*...
gi 695695446 307 E-------LLAGAAYNWGQGNVDKLIEK 327
Cdd:COG4623  345 AidepdrwWFALAAYNAGPGHVQDARRL 372
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
239-360 2.59e-09

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: 56.75  E-value: 2.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 239 VESGGKHLnsdgsiVTSSAGAQGRFQLMPETGKELAARRGLKYNPADeqqhtMLAsD----------YAQELSNKY-GSE 307
Cdd:cd16896   28 VESNFNPN------AVSSKGAIGLMQIMPETAEWIAEKLGLEDFSED-----DLY-DpetnirlgtwYLSYLLKEFdGNL 95
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 695695446 308 LLAGAAYNWGQGNVDKLIEKIGDPRKGeisqaDFIKKLP-SETQGWISRYRKNK 360
Cdd:cd16896   96 VLALAAYNAGPGNVDKWLKDGGWSGDG-----KTLDQIPfPETRHYVKKVLKNY 144
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
238-331 2.66e-07

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: 50.00  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446  238 IVESGGkhlNSDgsiVTSSAGAQGRFQLMPETGKELAARRGLKYNPA-DEQQHTMLASDYAQELSNKYG-SELLAGAAYN 315
Cdd:pfam01464  20 QQESGF---NPK---AVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLfDPEKNIKAGTKYLKELYKQYGgDLWLALAAYN 93
                          90
                  ....*....|....*.
gi 695695446  316 WGQGNVDKLIEKIGDP 331
Cdd:pfam01464  94 AGPGRVRKWIKNAGAK 109
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
239-320 3.24e-04

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: 40.75  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 239 VESGGkhlNSDgsIVTSSAGAQGRFQLMPETgkelAARRGL---------KYNPADEQQHTM--LASDYAQELSNKYGSE 307
Cdd:cd13399   14 VESGF---GPN--AGGSPAGAQGIAQFMPST----WKAYGVdgngdgkadPFNPEDAIASAAnyLCRHGWDLNAFLGEDN 84
                         90
                 ....*....|...
gi 695695446 308 LLAGAAYNWGQGN 320
Cdd:cd13399   85 FLALAAYNAGPGA 97
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
253-359 1.76e-03

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 41.97  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 253 VTSSAGAQGRFQLMPETGKELAARRGLK-Y-NPA---DEQQHTMLASDYAQELSNKYG-SELLAGAAYNWGQGNVDKLIE 326
Cdd:PRK11619 511 ARSPVGASGLMQIMPGTATHTVKMFSIPgYsSSSqllDPETNINIGTSYLEYVYQQFGnNRILASAAYNAGPGRVRTWLG 590
                         90       100       110
                 ....*....|....*....|....*....|....
gi 695695446 327 KIGdprkGEISQADFIKKLP-SETQGwisrYRKN 359
Cdd:PRK11619 591 NSA----GRIDAVAFVESIPfSETRG----YVKN 616
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
253-331 7.42e-03

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: 38.28  E-value: 7.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 253 VTSSAGAQGRFQLMPETGKELaarrGLKyNPADEQQHTMLASDYAQELSNKYGSE-------LLAGAAYNWGQGNV-D-- 322
Cdd:cd13403   29 ARSPAGARGLMQLMPSTAREL----GVN-DRLDPEQNIHAGAKYLRYLRDRFPPDidepdrlKFALAAYNAGPGHVrDar 103
                         90
                 ....*....|
gi 695695446 323 KLIEKIG-DP 331
Cdd:cd13403  104 RLAKKYGlNP 113
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
253-349 9.99e-03

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 39.33  E-value: 9.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695695446 253 VTSSAGAQGRFQLMPETGKELaarrGLKYNP-----ADEQQHTMLASDYAQELSNKY-GSELLAGAAYNWGQGNVDKLIE 326
Cdd:PRK10783 135 ATSGANAAGIWQIIPSTGRNY----GLKQTRwydarRDVVASTTAALDMMQRLNKMFdGDWLLTVAAYNSGEGRVMKAIK 210
                         90       100
                 ....*....|....*....|....
gi 695695446 327 kiGDPRKGEisQADFIK-KLPSET 349
Cdd:PRK10783 211 --ANKAKGK--PTDFWSlSLPRET 230
 
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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