NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|501455284|ref|WP_012478729|]
View 

MULTISPECIES: murein transglycosylase A [Stenotrophomonas]

Protein Classification

murein transglycosylase A( domain architecture ID 11458107)

membrane-bound lytic murein transglycosylase A cleaves the beta-1,4 glycosidic linkages between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MltA COG2821
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];
10-387 1.43e-175

Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442069 [Multi-domain]  Cd Length: 388  Bit Score: 494.01  E-value: 1.43e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284  10 RRHCILLAAAVLAGCATTAPrtgseaPTPTMPPAATYAKAAWSALPPVSNSDLQAGFVAWRSSCTRLKND---------- 79
Cdd:COG2821    2 RRLLLLLALLLLAACATQPP------PPGAAAPDARLQPVSFSDLPGWADDDLAAALPAFRRSCRRLARRpaasaygita 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284  80 AVWAKPCATAAAVSDKDPAAIRQFLQRDLDAYALRAGGHQADGLITGYYEPIYAGSLTRTDKATVPVYGTPDDLVVVQLE 159
Cdd:COG2821   76 ADWRAACAAARQLPAADPAAARAFFEREFQPYQVVGPDGGGNGLFTGYYEPELEGSRTRTAEYRYPLYRRPPDLVTVDLG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 160 SLypELKGKRLRGRVEGKVLKPYDDAGTIA--AQGANAPVLAWLTDPMDLQLLQIQGSGRVRLADGKQVRLAYAEQNGHP 237
Cdd:COG2821  156 SF--ELKGKRLRGRLEGGRLVPYPTRAEIEagALAGRGLELAWVDDPVDAFFLQIQGSGRVRLPDGSLIRVGYAGKNGHP 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 238 YRAVGRWLVDQGQLKKEDVTMDAIRAWARANPARVPELLRSNPSYVFFVRNPDSPEGPRGSLNVPLTAGYSVAVDRSVVP 317
Cdd:COG2821  234 YTSIGRLLIDRGELPLEQMSMQAIRAWLRANPEELRELLNQNPSYVFFRELPGPDAGPLGALGVPLTPGRSIAVDPSLIP 313

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501455284 318 LGSLLWLSTTRPD----GTPVVRPVAAQDTGGAIAGEVRADLYWGSGDAAGKLAGDMKQKGNIWMLWPKGAPLP 387
Cdd:COG2821  314 LGAPVWLETTLPDanfsGKPLRRLMIAQDTGGAIKGAVRADLFWGTGDEAGERAGRMKHPGRLWVLLPKGAAPP 387
 
Name Accession Description Interval E-value
MltA COG2821
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];
10-387 1.43e-175

Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442069 [Multi-domain]  Cd Length: 388  Bit Score: 494.01  E-value: 1.43e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284  10 RRHCILLAAAVLAGCATTAPrtgseaPTPTMPPAATYAKAAWSALPPVSNSDLQAGFVAWRSSCTRLKND---------- 79
Cdd:COG2821    2 RRLLLLLALLLLAACATQPP------PPGAAAPDARLQPVSFSDLPGWADDDLAAALPAFRRSCRRLARRpaasaygita 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284  80 AVWAKPCATAAAVSDKDPAAIRQFLQRDLDAYALRAGGHQADGLITGYYEPIYAGSLTRTDKATVPVYGTPDDLVVVQLE 159
Cdd:COG2821   76 ADWRAACAAARQLPAADPAAARAFFEREFQPYQVVGPDGGGNGLFTGYYEPELEGSRTRTAEYRYPLYRRPPDLVTVDLG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 160 SLypELKGKRLRGRVEGKVLKPYDDAGTIA--AQGANAPVLAWLTDPMDLQLLQIQGSGRVRLADGKQVRLAYAEQNGHP 237
Cdd:COG2821  156 SF--ELKGKRLRGRLEGGRLVPYPTRAEIEagALAGRGLELAWVDDPVDAFFLQIQGSGRVRLPDGSLIRVGYAGKNGHP 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 238 YRAVGRWLVDQGQLKKEDVTMDAIRAWARANPARVPELLRSNPSYVFFVRNPDSPEGPRGSLNVPLTAGYSVAVDRSVVP 317
Cdd:COG2821  234 YTSIGRLLIDRGELPLEQMSMQAIRAWLRANPEELRELLNQNPSYVFFRELPGPDAGPLGALGVPLTPGRSIAVDPSLIP 313

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501455284 318 LGSLLWLSTTRPD----GTPVVRPVAAQDTGGAIAGEVRADLYWGSGDAAGKLAGDMKQKGNIWMLWPKGAPLP 387
Cdd:COG2821  314 LGAPVWLETTLPDanfsGKPLRRLMIAQDTGGAIKGAVRADLFWGTGDEAGERAGRMKHPGRLWVLLPKGAAPP 387
MltA pfam03562
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
 58-285 2.56e-102

MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein degrading transglycosylase enzyme. This domain may be involved in peptidoglycan binding.


Pssm-ID: 460973 [Multi-domain]  Cd Length: 231  Bit Score: 302.18  E-value: 2.56e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284   58 SNSDLQAGFVAWRSSCTRLKND-AVWAKPCATAAAV-SDKDPAAIRQFLQRDLDAYALRAGGHqaDGLITGYYEPIYAGS 135
Cdd:pfam03562   2 QDDDLAAALPAFRRSCARLKKRaPDWLPACAAARSLpPSDSPAAARAFFEREFTPYQVVGPGS--DGLFTGYYEPELEGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284  136 LTRTDKATVPVYGTPDDLVVVQLEslYPELKGKRLRGRVEGKVLKPYDDAGTIAAQGAN---APVLAWLTDPMDLQLLQI 212
Cdd:pfam03562  80 RTRTAEYRYPLYRRPPDLVTVDLG--FFPLKGKRLRGRLVGGWLVPYPTRAEIEGKGALsgrGLELAWLRDPVDAFFLQI 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501455284  213 QGSGRVRLADGKQVRLAYAEQNGHPYRAVGRWLVDQGQLKKEDVTMDAIRAWARANPARVPELLRSNPSYVFF 285
Cdd:pfam03562 158 QGSGRLRLPDGSVVRVGYAGQNGHPYTSIGRELIDRGELPLEQASMQGIRAWLRANPEELDELLNRNPSYVFF 230
mlta_B cd14668
Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a ...
 132-285 2.30e-77

Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct.


Pssm-ID: 270616  Cd Length: 159  Bit Score: 235.88  E-value: 2.30e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 132 YAGSLTRTDKATVPVYGTPDDLVVVQLESLYPELKGKRLRGRVEGKVLKPYDDAGTIAAQGAN--APVLAWLTDPMDLQL 209
Cdd:cd14668    1 LEGSRTPTAEYRYPLYGRPPDLVTVDLGEFYPELKGKRLRGRVEGGRLVPYYTRAEIEAGALLgrGLELAWLDDPVDAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501455284 210 LQIQGSGRVRLADGKQVRLAYAEQNGHPYRAVGRWLVDQGQLKKEDVTMDAIRAWARANPARVPELLRSNPSYVFF 285
Cdd:cd14668   81 LQIQGSGRLRLPDGSVVRVGYAGKNGHPYRSIGRVLIDRGELPKEQMSMQAIRAWLRANPERARELLNENPSYVFF 156
MltA smart00925
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
 131-285 1.25e-73

MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein degrading transglycosylase enzyme. This domain may be involved in peptidoglycan binding.


Pssm-ID: 214916  Cd Length: 153  Bit Score: 225.91  E-value: 1.25e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284   131 IYAGSLTRTDKATVPVYGTPDDLVVVQLesLYPELKGKRLRGrveGKVLKPYDDAGTIAaQGA---NAPVLAWLTDPMDL 207
Cdd:smart00925   1 VLEGSRTRTGRYRYPLYRRPDDLVVVDL--FDPELKGKRLRG---GGKLVPYPTRAEIE-DGAldgRGLELAWVDDPVDL 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501455284   208 QLLQIQGSGRVRLADGKQVRLAYAEQNGHPYRAVGRWLVDQGQLKKEDVTMDAIRAWARANPARVPELLRSNPSYVFF 285
Cdd:smart00925  75 FFLQIQGSGRVRLPDGRLIRVGYAGKNGHPYRSIGRLLIDRGEIPKEEASMQAIRAWLRANPERVDELLNRNPSYVFF 152
mltA PRK11162
murein transglycosylase A; Provisional
 96-379 1.46e-56

murein transglycosylase A; Provisional


Pssm-ID: 236866 [Multi-domain]  Cd Length: 355  Bit Score: 188.97  E-value: 1.46e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284  96 DPAAIRQFlqrDLDAYALRAGGHQADGLITGYYEPIYAGSLTRTDKATVPVYGTPDdlvvvqleslypelKGKRLRGRVE 175
Cdd:PRK11162  93 DTRELRQF---GIQAWQMEGVDNYGNVQFTGYYTPVIQARHTPQGEFQYPIYRMPP--------------KRGRLPSRAE 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 176 gkvlkPYddAGTIAAQGAnapVLAWLTDPMDLQLLQIQGSGRVRLADGKQVR-LAYAEQNGHPYRAVGRWLVDQGQLKKE 254
Cdd:PRK11162 156 -----IY--AGALSGKGL---ELAYSNSLIDNFIMEVQGSGYVDFGDGRPLNfFAYAGKNGHAYRSIGKVLIDRGEVPKE 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 255 DVTMDAIRAWARANP-ARVPELLRSNPSYVFFVRNPDSPegPRGSLNVPLTAGYSVAVDRSVVPLGSLLWLSTTRPD--- 330
Cdd:PRK11162 226 DMSMQAIREWGEKHSeAEVRELLEQNPSFVFFKPQPFAP--VKGASAVPLVAMASVASDRSIIPPGTVLLAEVPLLDnng 303

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501455284 331 ---GTPVVRPVAAQDTGGAIAGEvRADLYWGSGDAAGKLAGDMKQKGNIWML 379
Cdd:PRK11162 304 kftGKYELRLMVALDVGGAIKGQ-HFDIYQGIGPEAGHRAGHYNHYGRVWVL 354
 
Name Accession Description Interval E-value
MltA COG2821
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];
10-387 1.43e-175

Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442069 [Multi-domain]  Cd Length: 388  Bit Score: 494.01  E-value: 1.43e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284  10 RRHCILLAAAVLAGCATTAPrtgseaPTPTMPPAATYAKAAWSALPPVSNSDLQAGFVAWRSSCTRLKND---------- 79
Cdd:COG2821    2 RRLLLLLALLLLAACATQPP------PPGAAAPDARLQPVSFSDLPGWADDDLAAALPAFRRSCRRLARRpaasaygita 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284  80 AVWAKPCATAAAVSDKDPAAIRQFLQRDLDAYALRAGGHQADGLITGYYEPIYAGSLTRTDKATVPVYGTPDDLVVVQLE 159
Cdd:COG2821   76 ADWRAACAAARQLPAADPAAARAFFEREFQPYQVVGPDGGGNGLFTGYYEPELEGSRTRTAEYRYPLYRRPPDLVTVDLG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 160 SLypELKGKRLRGRVEGKVLKPYDDAGTIA--AQGANAPVLAWLTDPMDLQLLQIQGSGRVRLADGKQVRLAYAEQNGHP 237
Cdd:COG2821  156 SF--ELKGKRLRGRLEGGRLVPYPTRAEIEagALAGRGLELAWVDDPVDAFFLQIQGSGRVRLPDGSLIRVGYAGKNGHP 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 238 YRAVGRWLVDQGQLKKEDVTMDAIRAWARANPARVPELLRSNPSYVFFVRNPDSPEGPRGSLNVPLTAGYSVAVDRSVVP 317
Cdd:COG2821  234 YTSIGRLLIDRGELPLEQMSMQAIRAWLRANPEELRELLNQNPSYVFFRELPGPDAGPLGALGVPLTPGRSIAVDPSLIP 313

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501455284 318 LGSLLWLSTTRPD----GTPVVRPVAAQDTGGAIAGEVRADLYWGSGDAAGKLAGDMKQKGNIWMLWPKGAPLP 387
Cdd:COG2821  314 LGAPVWLETTLPDanfsGKPLRRLMIAQDTGGAIKGAVRADLFWGTGDEAGERAGRMKHPGRLWVLLPKGAAPP 387
MltA pfam03562
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
 58-285 2.56e-102

MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein degrading transglycosylase enzyme. This domain may be involved in peptidoglycan binding.


Pssm-ID: 460973 [Multi-domain]  Cd Length: 231  Bit Score: 302.18  E-value: 2.56e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284   58 SNSDLQAGFVAWRSSCTRLKND-AVWAKPCATAAAV-SDKDPAAIRQFLQRDLDAYALRAGGHqaDGLITGYYEPIYAGS 135
Cdd:pfam03562   2 QDDDLAAALPAFRRSCARLKKRaPDWLPACAAARSLpPSDSPAAARAFFEREFTPYQVVGPGS--DGLFTGYYEPELEGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284  136 LTRTDKATVPVYGTPDDLVVVQLEslYPELKGKRLRGRVEGKVLKPYDDAGTIAAQGAN---APVLAWLTDPMDLQLLQI 212
Cdd:pfam03562  80 RTRTAEYRYPLYRRPPDLVTVDLG--FFPLKGKRLRGRLVGGWLVPYPTRAEIEGKGALsgrGLELAWLRDPVDAFFLQI 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501455284  213 QGSGRVRLADGKQVRLAYAEQNGHPYRAVGRWLVDQGQLKKEDVTMDAIRAWARANPARVPELLRSNPSYVFF 285
Cdd:pfam03562 158 QGSGRLRLPDGSVVRVGYAGQNGHPYTSIGRELIDRGELPLEQASMQGIRAWLRANPEELDELLNRNPSYVFF 230
mlta_B cd14668
Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a ...
 132-285 2.30e-77

Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct.


Pssm-ID: 270616  Cd Length: 159  Bit Score: 235.88  E-value: 2.30e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 132 YAGSLTRTDKATVPVYGTPDDLVVVQLESLYPELKGKRLRGRVEGKVLKPYDDAGTIAAQGAN--APVLAWLTDPMDLQL 209
Cdd:cd14668    1 LEGSRTPTAEYRYPLYGRPPDLVTVDLGEFYPELKGKRLRGRVEGGRLVPYYTRAEIEAGALLgrGLELAWLDDPVDAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501455284 210 LQIQGSGRVRLADGKQVRLAYAEQNGHPYRAVGRWLVDQGQLKKEDVTMDAIRAWARANPARVPELLRSNPSYVFF 285
Cdd:cd14668   81 LQIQGSGRLRLPDGSVVRVGYAGKNGHPYRSIGRVLIDRGELPKEQMSMQAIRAWLRANPERARELLNENPSYVFF 156
MltA smart00925
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
 131-285 1.25e-73

MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein degrading transglycosylase enzyme. This domain may be involved in peptidoglycan binding.


Pssm-ID: 214916  Cd Length: 153  Bit Score: 225.91  E-value: 1.25e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284   131 IYAGSLTRTDKATVPVYGTPDDLVVVQLesLYPELKGKRLRGrveGKVLKPYDDAGTIAaQGA---NAPVLAWLTDPMDL 207
Cdd:smart00925   1 VLEGSRTRTGRYRYPLYRRPDDLVVVDL--FDPELKGKRLRG---GGKLVPYPTRAEIE-DGAldgRGLELAWVDDPVDL 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501455284   208 QLLQIQGSGRVRLADGKQVRLAYAEQNGHPYRAVGRWLVDQGQLKKEDVTMDAIRAWARANPARVPELLRSNPSYVFF 285
Cdd:smart00925  75 FFLQIQGSGRVRLPDGRLIRVGYAGKNGHPYRSIGRLLIDRGEIPKEEASMQAIRAWLRANPERVDELLNRNPSYVFF 152
mltA PRK11162
murein transglycosylase A; Provisional
 96-379 1.46e-56

murein transglycosylase A; Provisional


Pssm-ID: 236866 [Multi-domain]  Cd Length: 355  Bit Score: 188.97  E-value: 1.46e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284  96 DPAAIRQFlqrDLDAYALRAGGHQADGLITGYYEPIYAGSLTRTDKATVPVYGTPDdlvvvqleslypelKGKRLRGRVE 175
Cdd:PRK11162  93 DTRELRQF---GIQAWQMEGVDNYGNVQFTGYYTPVIQARHTPQGEFQYPIYRMPP--------------KRGRLPSRAE 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 176 gkvlkPYddAGTIAAQGAnapVLAWLTDPMDLQLLQIQGSGRVRLADGKQVR-LAYAEQNGHPYRAVGRWLVDQGQLKKE 254
Cdd:PRK11162 156 -----IY--AGALSGKGL---ELAYSNSLIDNFIMEVQGSGYVDFGDGRPLNfFAYAGKNGHAYRSIGKVLIDRGEVPKE 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 255 DVTMDAIRAWARANP-ARVPELLRSNPSYVFFVRNPDSPegPRGSLNVPLTAGYSVAVDRSVVPLGSLLWLSTTRPD--- 330
Cdd:PRK11162 226 DMSMQAIREWGEKHSeAEVRELLEQNPSFVFFKPQPFAP--VKGASAVPLVAMASVASDRSIIPPGTVLLAEVPLLDnng 303

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501455284 331 ---GTPVVRPVAAQDTGGAIAGEvRADLYWGSGDAAGKLAGDMKQKGNIWML 379
Cdd:PRK11162 304 kftGKYELRLMVALDVGGAIKGQ-HFDIYQGIGPEAGHRAGHYNHYGRVWVL 354
mltA_like_LT_A cd14485
Domain A of MltA and related lytic transglycosylase; domain A is interrupted by domain B; ...
 256-379 2.95e-40

Domain A of MltA and related lytic transglycosylase; domain A is interrupted by domain B; Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct.


Pssm-ID: 270618 [Multi-domain]  Cd Length: 159  Bit Score: 140.08  E-value: 2.95e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 256 VTMDAIRAWARANPARVPELLRSNPS--YVFFVRNPDSPEG-------PrgslNVPLTAGYSVAVDRSVVPLGSLLWLST 326
Cdd:cd14485   27 LTWGDLRASLEALLAFLLARLDAAPEalADFFQWVDGSGEGlftgyyeP----GVPLTPGRSLAVDRSLIPLGAPVWLET 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501455284 327 TRPD----GTPVVRPVAAQDTGGAIAGEVRADLYWGSGDAAGKLAGDMKQKGNIWML 379
Cdd:cd14485  103 PLPDanggGKPLRRLVIAQDTGGAIKGPVRADLFWGSGDEAGELAGRMKHPGRLWVL 159
DPBB_MltA-like cd22785
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
 293-379 1.82e-28

double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and similar proteins; MltA, also called murein hydrolase A, is a murein-degrading enzyme that may play a role in the recycling of muropeptides during cell elongation and/or cell division. It degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. Bacterial lytic transglycosylases (LTs) are classified into 4 families: family 1 includes slt70 MltC-MltF, family 2 includes MltA, family 3 includes MltB, and family 4 includes proteins of bacteriophage origin. MltA is distinct from other bacterial LTs, which are similar in structure and sequence with a lysozyme-like fold. MltA is a kidney bean-shaped monomeric protein comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which corresponds to a double-psi beta-barrel (DPBB) fold. Domain B also has a beta-barrel fold topology, but it is inserted within the linear sequence of domain A. This model corresponds to the DPBB fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis. It is involved in substrate binding and catalysis.


Pssm-ID: 439262 [Multi-domain]  Cd Length: 97  Bit Score: 106.96  E-value: 1.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 293 EGPRGSLNVPLTAGYSVAVDRSVVPLGSLLWLSTTR----PDGTPVVRPVAAQDTGGAIAGeVRADLYWGSGDAAGKLAG 368
Cdd:cd22785    8 TPPRGALGVPLTPFRSVAVDPSVIPLGSVVYIPALDgvklPDGEPHDGLFIAQDTGGAIKG-KHIDVFTGSGDEAGELAG 86

                         90
                 ....*....|.
gi 501455284 369 DMKQKGNIWML 379
Cdd:cd22785   87 KLNHTGRVYVL 97
mlta_related_B cd14669
putative domain B insert of mltA_type lytic transglycosylases; Escherichia coli MltA is a ...
 145-287 1.93e-24

putative domain B insert of mltA_type lytic transglycosylases; Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct.


Pssm-ID: 270617  Cd Length: 128  Bit Score: 97.10  E-value: 1.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 145 PVYGTPDDLVVVqleslYPelkgkrLRGRVEGKVLKPyddagtiaaqganAPVLAWLTDPMDLQLLQIQGSGRVRLADGK 224
Cdd:cd14669   16 PVYGNPGDMIVP-----YY------TRAEIERGALWE-------------AKVIAYVKDPTDLYLMQLQGSGKVKLPDGT 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501455284 225 QVRLAYAEQNGHPYRAVGRWLvdQGQLKKEDVTMDAIRawaraNPARVPELLRSNPSYVFFVR 287
Cdd:cd14669   72 VFRIAYAEQNGRPFLPPVASA--KGSLTPSEAANCIAL-----NPPEVAAFAISDPSYVFFRK 127
3D pfam06725
3D domain; This short presumed domain contains three conserved aspartate residues, hence the ...
 307-380 1.01e-23

3D domain; This short presumed domain contains three conserved aspartate residues, hence the name 3D. It has been shown to be part of the catalytic double psi beta barrel domain of MltA.


Pssm-ID: 399598 [Multi-domain]  Cd Length: 72  Bit Score: 93.42  E-value: 1.01e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501455284  307 YSVAVDRSVVPLGSLLWLSTTRpDGTPVVRPVAAQDTGGAIAGEvRADLYWGSGDAAGKLAGDMKQKGNIWMLW 380
Cdd:pfam06725   1 RSIAVDPSVIPLGTPVYVEGPL-GGKPVYRLAIAQDTGGAIKGN-RIDLYFGTGDEAGNLAGLYRKTGRVYILL 72
mltA_B_like cd14472
Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a ...
 157-287 5.90e-20

Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct.


Pssm-ID: 270615  Cd Length: 134  Bit Score: 85.10  E-value: 5.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 157 QLESLYPELKGKRLRGRVEGKvlkpyddAGTIAAQGANAPVLAWLTDPMDLQLLQIQGSGRVRLADGKQV-RLAYAEQNG 235
Cdd:cd14472    8 QGEFQYPIYRIPPKRGRLSSR-------AEIYAGALSDKYILAYSNSLVDNFIADVQGSGYIDFGDGSPLnFFSYAGKNG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501455284 236 HPYRAVGRWLVDQGQLKKEDVTMDAIRAWARA-NPARVPELLRSNPSYVFFVR 287
Cdd:cd14472   81 HAYRSIGKVLIDRGEVKKEDISSQAIRHWGEThSEAEVRELLEQNPSFVFFKP 133
3D_domain cd14486
3D domain, named for 3 conserved aspartate residues, is found in mltA-like lytic ...
 281-367 1.82e-10

3D domain, named for 3 conserved aspartate residues, is found in mltA-like lytic transglycosylases and numerous other contexts; This family contains the 3D domain, named for its 3 conserved aspartates. It is found in conjunction with numerous other domains such as MltA (membrane-bound lytic murein transglycosylase A). These aspartates are critical active site residues of mltA-like lytic transglycosylases. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. MltA has 2 domains, separated by a large groove, where the peptidoglycan strand binds. The C-terminus has a double-psi beta barrel fold within the 3D domain, which forms the larger A domain along with the N-terminal region of Mlts, but is also found in various other domain architectures. Peptigoglycan (also known as murein) chains, the primary structural component of bacterial cells walls, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc); lytic transglycosylases (LTs) cleave this beta-1-4 bond. Typically, LTs are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, membrane-bound lytic murein transglycosylase E (MltE) is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane- bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and family 4 of bacteriophage origin. While most LTs are related members of the lysozyme-like lytic transglycosylase family, MltA represents a distinct fold and sequence conservation.


Pssm-ID: 270619 [Multi-domain]  Cd Length: 104  Bit Score: 57.38  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 281 SYVFFVRNPDSPEGPRGSLNVPLTAGYSVAVDRSVVPLGSLLWLSTTRPDGTPVVRpvAAQDTGGAIAGEvRADLYWGSG 360
Cdd:cd14486   12 GKRPSPPDEFSFSFRLTASGRPPVPYRTIAVDPSVIPLGSVVYIPELRGLPNDGVF--VAEDTGGAIKGN-HIDVYTGDG 88


                 ....*..
gi 501455284 361 DAAGKLA 367
Cdd:cd14486   89 PDARSNA 95
DPBB_MltA_YuiC-like cd22784
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
 297-378 1.22e-07

double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and YuiC-like proteins; This family includes two subfamilies of conserved double-psi beta-barrel (DPBB) domain proteins, such as membrane-bound lytic murein transglycosylase A (MltA)-like proteins and YuiC-like proteins. MltA, also called murein hydrolase A, is a murein-degrading enzyme that may play a role in the recycling of muropeptides during cell elongation and/or cell division. It degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. Bacterial lytic transglycosylases (LTs) are classified into 4 families: family 1 includes slt70 MltC-MltF, family 2 includes MltA, family 3 includes MltB, and family 4 includes proteins of bacteriophage origin. MltA is distinct from other bacterial LTs, which are similar in structure and sequence with a lysozyme-like fold. MltA is a kidney bean-shaped monomeric protein comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which corresponds to a double-psi beta-barrel (DPBB) fold. Domain B also has a beta-barrel fold topology, but it is inserted within the linear sequence of domain A. YuiC is a Firmicute stationary phase survival (Sps) protein that closely resembles the Barwin-like endoglucanase beta barrel of MltA. It is a DPBB fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis and may be involved in substrate binding and catalysis.


Pssm-ID: 439261 [Multi-domain]  Cd Length: 92  Bit Score: 49.18  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 297 GSLNVPLTAGYSVAVDRSVVPLGSLLWLSTTRPDGTPVVrpvaaQDTGGAIAGEvRADLYWGSGDAAgKLAGdmKQKGNI 376
Cdd:cd22784   20 TASGVTLRGYGTVAVDRDLIPLGTKVKIEGPGSGGEYVV-----LDRGGAIKGN-RIDIYFPSEKEA-KKFG--RQKVTV 90


                 ..
gi 501455284 377 WM 378
Cdd:cd22784   91 TV 92
COG3584 COG3584
3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D ...
 301-363 1.07e-06

3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases is part of the Pathway/BioSystem: 3D


Pssm-ID: 442803 [Multi-domain]  Cd Length: 92  Bit Score: 46.25  E-value: 1.07e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501455284 301 VPLTAGYSVAVDRSVVPLGSLLWLSTtrpDGTPVvrpvaAQDTGGAIAGeVRADLYWGSGDAA 363
Cdd:COG3584   25 TRLRPGGVIAVDPDVIPLGTKVYIEG---YGYAV-----AEDTGGAIKG-NRIDIYMPSVSEA 78
3D_containing_proteins cd14667
Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; ...
 304-363 9.15e-06

Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; This family contains the 3D domain, named for its 3 conserved aspartates, including similar uncharacterized proteins. These proteins contain the critical active site aspartate of mltA-like lytic transglycosylases where the 3D domain forms a larger domain with the N-terminal region. This domain is also found in conjunction with numerous other domains such as the Escherichia coli MltA, a membrane-bound lytic transglycosylase comprised of 2 domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, corresponding to the 3D domain and Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial LTs, which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond.


Pssm-ID: 270620 [Multi-domain]  Cd Length: 90  Bit Score: 43.67  E-value: 9.15e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 501455284 304 TAGYSVAVDRSVVPLGSLLWLSTTrpdGTPVVrpvaaQDTGGAIAGeVRADLYWGSGDAA 363
Cdd:cd14667   27 VGGGTIAVDPSVIPLGTKVYIEGY---GVYVV-----EDTGGAIKG-NRIDIYMDSHAEA 77
DPBB_YuiC-like cd22786
double-psi beta-barrel fold of YuiC subfamily proteins; The YuiC subfamily includes a group of ...
 291-356 5.48e-04

double-psi beta-barrel fold of YuiC subfamily proteins; The YuiC subfamily includes a group of conserved double-psi beta-barrel (DPBB) fold proteins, such as Bacillus subtilis protein YuiC, cell wall shaping protein YabE, cell wall-binding protein YocH, as well as Clostridium tetani phosphatase-associated protein PapQ. YuiC is a Firmicute stationary phase survival (Sps) protein that closely resembles the Barwin-like endoglucanase beta barrel of MltA. It is a double-psi beta-barrel (DPBB) fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis and may be involved in substrate binding and catalysis.


Pssm-ID: 439263 [Multi-domain]  Cd Length: 96  Bit Score: 38.74  E-value: 5.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501455284 291 SPEGPRGSLNVPLTAGYSVAVDRSVVPLGSLLWLsttrPDGTPVVrpvaAQDTGGAIaGEVRADLY 356
Cdd:cd22786   19 GGCYGITASGTPLKRKGTIAVDPSVIPLGTKVYI----PGYGYAV----VADTGGAI-KGNRIDLY 75
 
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