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Conserved domains on  [gi|490845316|ref|WP_004707379|]
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MULTISPECIES: transglycosylase SLT domain-containing protein [Acinetobacter]

Protein Classification

Periplasmic_Binding_Protein_Type_2 and MLTF-like domain-containing protein( domain architecture ID 13470621)

Periplasmic_Binding_Protein_Type_2 and MLTF-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 53-364 2.07e-77

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


:

Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 244.59  E-value: 2.07e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316  53 TLTVVAVESPTTVFKEDQFLHGFGYDLARNYAQSLNVKLDFKIVADNATALKWVQQGKANLAM----------------- 115
Cdd:COG4623   23 VLRVLTRNSPTTYFIYRGGPMGFEYELAKAFADYLGVKLEIIVPDNLDELLPALNAGEGDIAAagltitperkkqvrfsp 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 116 ------------------------------------------------------TTASLSSIE-----NKGLMSFSASCG 136
Cdd:COG4623  103 pyysvsqvlvyrkgsprpksledlagktvhvragssyaerlkqlnqegpplkweEDEDLETEDllemvAAGEIDYTVADS 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 137 DIVNLQKN-----------GLNPDLSWVFKQADDPLTQTASGFVCQSKQNGLTQQLASFYNRNVvkPESWSTIQRDISTR 205
Cdd:COG4623  183 NIAALNQRyypnlrvafdlSEPQPIAWAVRKNDPSLLAALNEFFAKIKKGGTLARLYERYFGHV--KRDTRAFLRRIEGR 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 206 LPIYKASFKQSAAKYDLDWHLLAAMSYQESYLKPESVSPTGVRGLMMLTNSTARAMGVSNRSDPAQSIQGGAKYYDLMLS 285
Cdd:COG4623  261 LPPYDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPATAKELGVDDRLDPEQSIRAGAKYLRWLYD 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 286 EYGD-IPYPDRNWYALVAYNMGPGAVNQIQKRLQTQGKDPNQWVNLYDYLQRN-QMRNGRYKQAVQYVTRIRAYLEHIKT 363
Cdd:COG4623  341 RFPEaIDEPDRWWFALAAYNAGPGHVQDARRLAKKQGLDPDRWFDVEKSQPKYyDTGYARGRETVNYVPNIRAYYDIYKR 420


                 .
gi 490845316 364 A 364
Cdd:COG4623  421 L 421
 
Name Accession Description Interval E-value
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 53-364 2.07e-77

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 244.59  E-value: 2.07e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316  53 TLTVVAVESPTTVFKEDQFLHGFGYDLARNYAQSLNVKLDFKIVADNATALKWVQQGKANLAM----------------- 115
Cdd:COG4623   23 VLRVLTRNSPTTYFIYRGGPMGFEYELAKAFADYLGVKLEIIVPDNLDELLPALNAGEGDIAAagltitperkkqvrfsp 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 116 ------------------------------------------------------TTASLSSIE-----NKGLMSFSASCG 136
Cdd:COG4623  103 pyysvsqvlvyrkgsprpksledlagktvhvragssyaerlkqlnqegpplkweEDEDLETEDllemvAAGEIDYTVADS 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 137 DIVNLQKN-----------GLNPDLSWVFKQADDPLTQTASGFVCQSKQNGLTQQLASFYNRNVvkPESWSTIQRDISTR 205
Cdd:COG4623  183 NIAALNQRyypnlrvafdlSEPQPIAWAVRKNDPSLLAALNEFFAKIKKGGTLARLYERYFGHV--KRDTRAFLRRIEGR 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 206 LPIYKASFKQSAAKYDLDWHLLAAMSYQESYLKPESVSPTGVRGLMMLTNSTARAMGVSNRSDPAQSIQGGAKYYDLMLS 285
Cdd:COG4623  261 LPPYDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPATAKELGVDDRLDPEQSIRAGAKYLRWLYD 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 286 EYGD-IPYPDRNWYALVAYNMGPGAVNQIQKRLQTQGKDPNQWVNLYDYLQRN-QMRNGRYKQAVQYVTRIRAYLEHIKT 363
Cdd:COG4623  341 RFPEaIDEPDRWWFALAAYNAGPGHVQDARRLAKKQGLDPDRWFDVEKSQPKYyDTGYARGRETVNYVPNIRAYYDIYKR 420


                 .
gi 490845316 364 A 364
Cdd:COG4623  421 L 421
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 213-363 1.26e-63

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: 200.07  E-value: 1.26e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 213 FKQSAAKYDLDWHLLAAMSYQESYLKPESVSPTGVRGLMMLTNSTARAMGVSNRSDPAQSIQGGAKYYDLMLSEY-GDIP 291
Cdd:cd13403    1 FKKYAEKYGFDWRLLAAQAYQESRFNPNARSPAGARGLMQLMPSTARELGVNDRLDPEQNIHAGAKYLRYLRDRFpPDID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 292 YPDRNWYALVAYNMGPGAVNQIQKRLQTQGKDPNQWVNLYDYLQRN-------QMRNG--RYKQAVQYVTRIRAYLEHIK 362
Cdd:cd13403   81 EPDRLKFALAAYNAGPGHVRDARRLAKKYGLNPNVWFDNVEVLPLLkspyydpVVKYGyaRGRETVNYVRNIRKYYDAYK 160


                 .
gi 490845316 363 T 363
Cdd:cd13403  161 Q 161
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
24-357 1.29e-62

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 207.80  E-value: 1.29e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316  24 VLALSTMFFPFHSINAGKTLQYNTVVNTNTLTVVAVESPTTVFKEDQFLHGFGYDLARNYAQSLNVKLDFKiVADNATAL 103
Cdd:PRK10859  15 ALLLAAALWPSIPWFSKEENQLEQIQERGELRVGTINSPLTYYIGNDGPTGFEYELAKRFADYLGVKLEIK-VRDNISQL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 104 -KWVQQGK-----ANLAMTTA----------------------------SLSSIENKGLM--SFSASCGDIVNLQKNglN 147
Cdd:PRK10859  94 fDALDKGKadlaaAGLTYTPErlkqfrfgppyysvsqqlvyrkgqprprSLGDLKGGTLTvaAGSSHVETLQELKKK--Y 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 148 PDLSWVF---KQADDPLTQTASG------------------------------------FVCQSKQNGLTQQLASFYNR- 187
Cdd:PRK10859 172 PELSWEEsddKDSEELLEQVAEGkidytiadsveislnqryhpelavafdltdeqpvawALPPSGDDSLYAALLDFFNQi 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 188 -----------------NVVKPESWSTIQRDISTRLPIYKASFKQSAAkyDLDWHLLAAMSYQESYLKPESVSPTGVRGL 250
Cdd:PRK10859 252 kedgtlarleekyfghvDRFDYVDTRTFLRAIDNRLPKYQPLFEKYAG--ELDWRLLAAIAYQESHWNPQATSPTGVRGL 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 251 MMLTNSTARAMGVSNRSDPAQSIQGGAKYYDLMLSEYGD-IPYPDRNWYALVAYNMGPGAVNQIQKRLQTQGKDPNQWVN 329
Cdd:PRK10859 330 MMLTRNTAQSMGVTDRLDPEQSIRGGARYLQDLMERLPEsIPEPERIWFALAAYNIGYGHMLDARRLTKKQGGNPDSWAD 409

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 490845316 330 LYDYL----QRNQMRNGRY-----KQAVQYVTRIRAY 357
Cdd:PRK10859 410 VKKRLpllsQKKYYSKTRYgyargHEAVHYVENIRRY 446
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 213-323 2.55e-20

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: 85.05  E-value: 2.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316  213 FKQSAAKYDLDWHLLAAMSYQESYLKPESVSPTGVRGLMMLTNSTARAMG------VSNRSDPAQSIQGGAKYYDLMLSE 286
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGlrvnpgVDDLFDPEKNIKAGTKYLKELYKQ 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 490845316  287 YGdipypDRNWYALVAYNMGPGAVNQIQKRLQTQGKD 323
Cdd:pfam01464  81 YG-----GDLWLALAAYNAGPGRVRKWIKNAGAKDKK 112
 
Name Accession Description Interval E-value
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 53-364 2.07e-77

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 244.59  E-value: 2.07e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316  53 TLTVVAVESPTTVFKEDQFLHGFGYDLARNYAQSLNVKLDFKIVADNATALKWVQQGKANLAM----------------- 115
Cdd:COG4623   23 VLRVLTRNSPTTYFIYRGGPMGFEYELAKAFADYLGVKLEIIVPDNLDELLPALNAGEGDIAAagltitperkkqvrfsp 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 116 ------------------------------------------------------TTASLSSIE-----NKGLMSFSASCG 136
Cdd:COG4623  103 pyysvsqvlvyrkgsprpksledlagktvhvragssyaerlkqlnqegpplkweEDEDLETEDllemvAAGEIDYTVADS 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 137 DIVNLQKN-----------GLNPDLSWVFKQADDPLTQTASGFVCQSKQNGLTQQLASFYNRNVvkPESWSTIQRDISTR 205
Cdd:COG4623  183 NIAALNQRyypnlrvafdlSEPQPIAWAVRKNDPSLLAALNEFFAKIKKGGTLARLYERYFGHV--KRDTRAFLRRIEGR 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 206 LPIYKASFKQSAAKYDLDWHLLAAMSYQESYLKPESVSPTGVRGLMMLTNSTARAMGVSNRSDPAQSIQGGAKYYDLMLS 285
Cdd:COG4623  261 LPPYDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPATAKELGVDDRLDPEQSIRAGAKYLRWLYD 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 286 EYGD-IPYPDRNWYALVAYNMGPGAVNQIQKRLQTQGKDPNQWVNLYDYLQRN-QMRNGRYKQAVQYVTRIRAYLEHIKT 363
Cdd:COG4623  341 RFPEaIDEPDRWWFALAAYNAGPGHVQDARRLAKKQGLDPDRWFDVEKSQPKYyDTGYARGRETVNYVPNIRAYYDIYKR 420


                 .
gi 490845316 364 A 364
Cdd:COG4623  421 L 421
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 213-363 1.26e-63

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: 200.07  E-value: 1.26e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 213 FKQSAAKYDLDWHLLAAMSYQESYLKPESVSPTGVRGLMMLTNSTARAMGVSNRSDPAQSIQGGAKYYDLMLSEY-GDIP 291
Cdd:cd13403    1 FKKYAEKYGFDWRLLAAQAYQESRFNPNARSPAGARGLMQLMPSTARELGVNDRLDPEQNIHAGAKYLRYLRDRFpPDID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 292 YPDRNWYALVAYNMGPGAVNQIQKRLQTQGKDPNQWVNLYDYLQRN-------QMRNG--RYKQAVQYVTRIRAYLEHIK 362
Cdd:cd13403   81 EPDRLKFALAAYNAGPGHVRDARRLAKKYGLNPNVWFDNVEVLPLLkspyydpVVKYGyaRGRETVNYVRNIRKYYDAYK 160


                 .
gi 490845316 363 T 363
Cdd:cd13403  161 Q 161
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
24-357 1.29e-62

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 207.80  E-value: 1.29e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316  24 VLALSTMFFPFHSINAGKTLQYNTVVNTNTLTVVAVESPTTVFKEDQFLHGFGYDLARNYAQSLNVKLDFKiVADNATAL 103
Cdd:PRK10859  15 ALLLAAALWPSIPWFSKEENQLEQIQERGELRVGTINSPLTYYIGNDGPTGFEYELAKRFADYLGVKLEIK-VRDNISQL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 104 -KWVQQGK-----ANLAMTTA----------------------------SLSSIENKGLM--SFSASCGDIVNLQKNglN 147
Cdd:PRK10859  94 fDALDKGKadlaaAGLTYTPErlkqfrfgppyysvsqqlvyrkgqprprSLGDLKGGTLTvaAGSSHVETLQELKKK--Y 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 148 PDLSWVF---KQADDPLTQTASG------------------------------------FVCQSKQNGLTQQLASFYNR- 187
Cdd:PRK10859 172 PELSWEEsddKDSEELLEQVAEGkidytiadsveislnqryhpelavafdltdeqpvawALPPSGDDSLYAALLDFFNQi 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 188 -----------------NVVKPESWSTIQRDISTRLPIYKASFKQSAAkyDLDWHLLAAMSYQESYLKPESVSPTGVRGL 250
Cdd:PRK10859 252 kedgtlarleekyfghvDRFDYVDTRTFLRAIDNRLPKYQPLFEKYAG--ELDWRLLAAIAYQESHWNPQATSPTGVRGL 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 251 MMLTNSTARAMGVSNRSDPAQSIQGGAKYYDLMLSEYGD-IPYPDRNWYALVAYNMGPGAVNQIQKRLQTQGKDPNQWVN 329
Cdd:PRK10859 330 MMLTRNTAQSMGVTDRLDPEQSIRGGARYLQDLMERLPEsIPEPERIWFALAAYNIGYGHMLDARRLTKKQGGNPDSWAD 409

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 490845316 330 LYDYL----QRNQMRNGRY-----KQAVQYVTRIRAY 357
Cdd:PRK10859 410 VKKRLpllsQKKYYSKTRYgyargHEAVHYVENIRRY 446
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 209-364 2.51e-24

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: 100.07  E-value: 2.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 209 YKASFKQSAAKYDLDWHLLAAMSYQESYLKPESVSPTGVRGLMMLTNSTARAMGV--------SNRSDPAQSIQGGAKYY 280
Cdd:COG0741  103 YLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLklglgpspDDLFDPETNIRAGAAYL 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 281 DLMLSEYGDipypdrNWY-ALVAYNMGPGAVNQiqkrlqtqgkdpnqwvnlydYLQRNQMRNGR---YKQAVQYVTRIRA 356
Cdd:COG0741  183 RELLDRFDG------DLVlALAAYNAGPGRVRR--------------------WLRRNGDRDGEiipYAETRNYVKKVLA 236


                 ....*...
gi 490845316 357 YLEHIKTA 364
Cdd:COG0741  237 NYAIYRAG 244
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 213-323 2.55e-20

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: 85.05  E-value: 2.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316  213 FKQSAAKYDLDWHLLAAMSYQESYLKPESVSPTGVRGLMMLTNSTARAMG------VSNRSDPAQSIQGGAKYYDLMLSE 286
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGlrvnpgVDDLFDPEKNIKAGTKYLKELYKQ 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 490845316  287 YGdipypDRNWYALVAYNMGPGAVNQIQKRLQTQGKD 323
Cdd:pfam01464  81 YG-----GDLWLALAAYNAGPGRVRKWIKNAGAKDKK 112
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 226-359 1.23e-19

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: 83.03  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 226 LLAAMSYQESYLKPESVSPTGVRGLMMLTNSTARAMG---VSNRSDPAQSIQGGAKYYDLMLSEYGdipypDRNWYALVA 302
Cdd:cd00254    3 LVLAVIRVESGFNPRAVSPAGARGLMQLMPGTARDLGrrgVDDLFDPEENIRAGARYLRELLDRFG-----GDLELALAA 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490845316 303 YNMGPGAVNQIQKRLQTqgkdpnqwvnlydylqrnqmrngRYKQAVQYVTRIRAYLE 359
Cdd:cd00254   78 YNAGPGAVDRWGGGEVP-----------------------PYKETRNYVQRVLAYYQ 111
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 209-328 4.14e-17

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: 77.52  E-value: 4.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 209 YKASFKQSAAKYDLDWHLLAAMSYQESYLKPESVSPTGVRGLMMLTNSTARAM----GVSNRS-----DPAQSIQGGAKY 279
Cdd:cd13401    6 YRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVakklGLPYYSprdlfDPEYNIRLGSAY 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 490845316 280 YDLMLSEYGDIPYpdrnwYALVAYNMGPGAVNQIQKRLqtQGKDPNQWV 328
Cdd:cd13401   86 LAELLDRFDGNPV-----LALAAYNAGPGRVRRWLKRR--GDLDPDLWI 127
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 207-359 1.37e-15

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: 72.93  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 207 PI-YKASFKQSAAKYDLDWHLLAAMSYQESYLKPESVSPTGVRGLMMLTNSTAR----AMGVSNRS-----DPAQSIQGG 276
Cdd:cd16896    1 PLkYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAEwiaeKLGLEDFSeddlyDPETNIRLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 277 AKYYDLMLSEY-GDIPypdrnwYALVAYNMGPGAVNqiqKRLQTQGKDPNqWVNLYDYlqrnqmrngRYKQAVQYVTRIR 355
Cdd:cd16896   81 TWYLSYLLKEFdGNLV------LALAAYNAGPGNVD---KWLKDGGWSGD-GKTLDQI---------PFPETRHYVKKVL 141


                 ....
gi 490845316 356 AYLE 359
Cdd:cd16896  142 KNYK 145
PHA00368 PHA00368
internal virion protein D
 209-308 2.17e-12

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 68.65  E-value: 2.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316  209 YKASFKQSAAKYDLDWHLLAAMSYQESYLKPESVSPTGVRGLMMLTNSTARAMGV----SNRSDPAQSIQGGAKYY-DLM 283
Cdd:PHA00368   11 YDGLFQKAADAHGVSYDLLRKVGWDESRFNPTAKSPTGPKGLMQFTKATAKALGLivddDDRLDPELAIDAGARYLaDLV 90

                          90       100
                  ....*....|....*....|....*
gi 490845316  284 LSEYGDipypdrNWYALVAYNMGPG 308
Cdd:PHA00368   91 GKYDGD------ELKAALAYNQGEG 109
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 227-359 1.02e-10

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: 58.68  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 227 LAAMSYQESYLKPESVSPTGVRGLMMLTNSTARAMGVSN------RSDPAQSIQGGAKYydlmLSEYGDIpypDRNWY-A 299
Cdd:cd16894   10 LKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVdswvdeRRDPEKSTRAAARY----LKDLYKR---FGDWLlA 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 300 LVAYNMGPGAVnqiQKRLQTQGKDPNQWVNLyDYLQRNQMRngrykqavqYVTRIRAYLE 359
Cdd:cd16894   83 LAAYNAGEGRV---RRAIKRAGTDKWEDYYR-LYLPAETRR---------YVPKFLAAKI 129
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 220-314 1.09e-07

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: 49.61  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 220 YDLDWHLLAAMSYQESYLKPESV-SPTGVRGLMMLTNSTARAMGVSNRSD-------PAQSIQGGAKYydlmLSEYGDI- 290
Cdd:cd13399    1 YGVPPGILAAILGVESGFGPNAGgSPAGAQGIAQFMPSTWKAYGVDGNGDgkadpfnPEDAIASAANY----LCRHGWDl 76

                         90       100
                 ....*....|....*....|....*..
gi 490845316 291 --PYPDRNWYALVAYNMGPGA-VNQIQ 314
Cdd:cd13399   77 naFLGEDNFLALAAYNAGPGAyANAVL 103
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 214-365 2.71e-07

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: 49.86  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 214 KQSAAKYDLDWHLLAAMSYQESYLKPESVSPTGVRGLMMLTNSTA-----RAMGVSNRS-------DPAQSIQGGAKYYD 281
Cdd:cd16893    4 EKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAgrdvyRLLGGKGGLpsksylfDPENNIDIGTAYLH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 282 LMLSEY-GDIPYPD-RNWYALVAYNMGPGAVnqiqkrLQTQGKDPNQWVN---------LYDYLQRNQmrngRYKQAvqy 350
Cdd:cd16893   84 ILQNRYlKGIKNPKsREYCAIAAYNGGAGNV------LRTFSSDRKKAISkinrlspdeVYQHLTKKL----PAAET--- 150

                        170
                 ....*....|....*
gi 490845316 351 vtriRAYLEHIKTAQ 365
Cdd:cd16893  151 ----RNYLKKVLKAK 161
PBP2_YfhD_N cd01009
The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold ...
 53-114 2.81e-07

The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold protein superfamily; This subfamily includes the solute binding domain YfhD_N. These domains are found in the YfhD proteins that are predicted to function as lytic transglycosylases that cleave the glycosidic bond between N-acetylmuramic acid and N-acetylglucosamin in peptidoglycan, while the YfhD_N domain might act as an auxiliary or regulatory subunit. In addition to periplasmic solute binding domain, they have an SLT domain, typically found in soluble lytic transglycosylases, and a C-terminal low complexity domain. The YfhD proteins might have been recruited to create localized cell wall openings required for transport of large substrates such as DNA. They belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270230 [Multi-domain]  Cd Length: 223  Bit Score: 50.67  E-value: 2.81e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490845316  53 TLTVVAVESPTTVFKEDQFLHGFGYDLARNYAQSLNVKLDFKIVADNATALKWVQQGKANLA 114
Cdd:cd01009    2 ELRVLTRNSPTTYYIDRGGPRGFEYELAKAFADYLGVELEIVPADNLEELLEALEEGKGDLA 63
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
214-365 2.93e-06

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 48.51  E-value: 2.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 214 KQSAAKYDLDWHLLAAMSYQESYLKPESVSPTGVRGLMMLTNSTA-----RAMGVS---NRS---DPAQSIQGGAKYYDL 282
Cdd:PRK11671 197 RKASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHTAgkdvfRMKGKSgqpSRSylfDPANNIDTGTAYLAI 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 283 MLSEY-GDIPYPDRNWYALV-AYNMGPGAVnqiqkrLQTQGKDPNQWVNLYdylqrNQMRNGrykQAVQYVT------RI 354
Cdd:PRK11671 277 LQNVYlGGITNPTSRRYAVItAYNGGAGSV------LRVFSNDKIQAANII-----NTMSPG---DVYQTLTtrhpsaES 342

                        170
                 ....*....|.
gi 490845316 355 RAYLEHIKTAQ 365
Cdd:PRK11671 343 RRYLYKVNTAQ 353
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 205-311 7.87e-05

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 44.67  E-value: 7.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 205 RLPI-YKASFKQSAAKYDLDWHLLAAMSYQESYLKPESVSPTGVRGLMMLTNSTARAM-------GVSNRS---DPAQSI 273
Cdd:PRK11619 474 RFPLaWNDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTvkmfsipGYSSSSqllDPETNI 553

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490845316 274 QGGAKYYDLMLSEYGdipypdRN-WYALVAYNMGPGAVN 311
Cdd:PRK11619 554 NIGTSYLEYVYQQFG------NNrILASAAYNAGPGRVR 586
emtA PRK15470
membrane-bound lytic murein transglycosylase EmtA;
214-310 2.01e-04

membrane-bound lytic murein transglycosylase EmtA;


Pssm-ID: 185367 [Multi-domain]  Cd Length: 203  Bit Score: 41.87  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 214 KQSAAKYDLDWHLLAAMSYQESYLKPESVSPTGVRGLMMLTNSTA-----RAMG------VSNRSDPAQSIQGGAKYYDL 282
Cdd:PRK15470  44 QKAGAAWGVDPQLITAIIAIESGGNPNAVSKSNAIGLMQLKASTSgrdvyRRMGwsgeptTSELKNPERNISMGAAYLNI 123

                         90       100       110
                 ....*....|....*....|....*....|..
gi 490845316 283 MlsEYG---DIPYPDRNWYAL-VAYNMGPGAV 310
Cdd:PRK15470 124 L--ETGplaGIEDPKVLQYALvVSYANGAGAL 153
PRK15328 PRK15328
type III secretion system invasion protein IagB;
215-306 2.01e-04

type III secretion system invasion protein IagB;


Pssm-ID: 185228 [Multi-domain]  Cd Length: 160  Bit Score: 41.39  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316 215 QSAAKYDLDWHLLAAMSYQESYLKPESV--SPTGVR--GLMMLTNS---TARAMGVSNR---SDPAQSIQGGAKYYDLML 284
Cdd:PRK15328  24 QAEKMFNIESELLYAIAQQESAMKPGAIghNRDGSTdlGLMQINSFhmkRLKKMGISEKqllQDPCISVIVGASILSDMM 103

                         90       100
                 ....*....|....*....|..
gi 490845316 285 SEYGdipypdRNWYALVAYNMG 306
Cdd:PRK15328 104 KIYG------YSWEAVGAYNAG 119
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
 56-134 3.19e-03

ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino acid transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 38.42  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316  56 VVAVES---PTTVFKEDQFLHGFGYDLARNYAQSLNVKLDFKIVaDNATALKWVQQGKANLAMTTASLSSiENKGLMSFS 132
Cdd:COG0834    2 RVGVDPdypPFSFRDEDGKLVGFDVDLARAIAKRLGLKVEFVPV-PWDRLIPALQSGKVDLIIAGMTITP-EREKQVDFS 79


                 ..
gi 490845316 133 AS 134
Cdd:COG0834   80 DP 81
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
 53-132 5.03e-03

Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate receptor domain GluR0. These domains are found in the GluR0 proteins that have been shown to function as prokaryotic L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. The GluR0 proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270218 [Multi-domain]  Cd Length: 218  Bit Score: 38.09  E-value: 5.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490845316  53 TLTVVAVESPTTVFKEDQFLHGFGYDLARNYAQSLNVKLDFKIVADNATALKWVQQGKANLAMTTASLSSiENKGLMSFS 132
Cdd:cd00997    4 TLTVATVPRPPFVFYNDGELTGFSIDLWRAIAERLGWETEYVRVDSVSALLAAVAEGEADIAIAAISITA-EREAEFDFS 82
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
 74-132 6.00e-03

Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognizes Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 425719 [Multi-domain]  Cd Length: 221  Bit Score: 37.66  E-value: 6.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490845316   74 GFGYDLARNYAQSLNVKLDFKIVaDNATALKWVQQGKANLAMTTASLSSiENKGLMSFS 132
Cdd:pfam00497  23 GFDVDLAKAIAKRLGVKVEFVPV-SWDGLIPALQSGKVDLIIAGMTITP-ERAKQVDFS 79
 
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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