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Conserved domains on  [gi|16130720|ref|NP_417293|]
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membrane-bound lytic murein transglycosylase A [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

murein transglycosylase A( domain architecture ID 11485235)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
mltA PRK11162
murein transglycosylase A; Provisional
1-354 0e+00

murein transglycosylase A; Provisional


:

Pssm-ID: 236866 [Multi-domain]  Cd Length: 355  Bit Score: 730.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720    1 MKGRWVKYLLMGTVVAMLAACSSKPTDRGQQYKDGKFTQPFSLVNQPDAVGAPINAGDFAEQINHIRNSSPRLYGNQSNV 80
Cdd:PRK11162   1 MKGRWVKYLLTGTVLALLAGCSSKPTDRGQQYKDGKFTQPLSLVNQPNASGKPINAGDFAEQVNQIRNSSPRLYGRYSNT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720   81 YNAVQEWLRAGGDTRNMRQFGIDAWQMEGADNYGNVQFTGYYTPVIQARHTRQGEFQYPIYRMPPKRGRLPSRAEIYAGA 160
Cdd:PRK11162  81 YNAVQEWLLAGGDTRELRQFGIQAWQMEGVDNYGNVQFTGYYTPVIQARHTPQGEFQYPIYRMPPKRGRLPSRAEIYAGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720  161 LSDK-YILAYSNSLMDNFIMDVQGSGYIDFGDGSPLNFFSYAGKNGHAYRSIGKVLIDRGEVKKEDMSMQAIRHWGETHS 239
Cdd:PRK11162 161 LSGKgLELAYSNSLIDNFIMEVQGSGYVDFGDGRPLNFFAYAGKNGHAYRSIGKVLIDRGEVPKEDMSMQAIREWGEKHS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720  240 EAEVRELLEQNPSFVFFKPQSFAPVKGASAVPLVGRASVASDRSIIPPGTTLLAEVPLLDNNGKFNGQYELRLMVALDVG 319
Cdd:PRK11162 241 EAEVRELLEQNPSFVFFKPQPFAPVKGASAVPLVAMASVASDRSIIPPGTVLLAEVPLLDNNGKFTGKYELRLMVALDVG 320
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 16130720  320 GAIKGQHFDIYQGIGPEAGHRAGWYNHYGRVWVLK 354
Cdd:PRK11162 321 GAIKGQHFDIYQGIGPEAGHRAGHYNHYGRVWVLK 355
 
Name Accession Description Interval E-value
mltA PRK11162
murein transglycosylase A; Provisional
1-354 0e+00

murein transglycosylase A; Provisional


Pssm-ID: 236866 [Multi-domain]  Cd Length: 355  Bit Score: 730.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720    1 MKGRWVKYLLMGTVVAMLAACSSKPTDRGQQYKDGKFTQPFSLVNQPDAVGAPINAGDFAEQINHIRNSSPRLYGNQSNV 80
Cdd:PRK11162   1 MKGRWVKYLLTGTVLALLAGCSSKPTDRGQQYKDGKFTQPLSLVNQPNASGKPINAGDFAEQVNQIRNSSPRLYGRYSNT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720   81 YNAVQEWLRAGGDTRNMRQFGIDAWQMEGADNYGNVQFTGYYTPVIQARHTRQGEFQYPIYRMPPKRGRLPSRAEIYAGA 160
Cdd:PRK11162  81 YNAVQEWLLAGGDTRELRQFGIQAWQMEGVDNYGNVQFTGYYTPVIQARHTPQGEFQYPIYRMPPKRGRLPSRAEIYAGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720  161 LSDK-YILAYSNSLMDNFIMDVQGSGYIDFGDGSPLNFFSYAGKNGHAYRSIGKVLIDRGEVKKEDMSMQAIRHWGETHS 239
Cdd:PRK11162 161 LSGKgLELAYSNSLIDNFIMEVQGSGYVDFGDGRPLNFFAYAGKNGHAYRSIGKVLIDRGEVPKEDMSMQAIREWGEKHS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720  240 EAEVRELLEQNPSFVFFKPQSFAPVKGASAVPLVGRASVASDRSIIPPGTTLLAEVPLLDNNGKFNGQYELRLMVALDVG 319
Cdd:PRK11162 241 EAEVRELLEQNPSFVFFKPQPFAPVKGASAVPLVAMASVASDRSIIPPGTVLLAEVPLLDNNGKFTGKYELRLMVALDVG 320
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 16130720  320 GAIKGQHFDIYQGIGPEAGHRAGWYNHYGRVWVLK 354
Cdd:PRK11162 321 GAIKGQHFDIYQGIGPEAGHRAGHYNHYGRVWVLK 355
MltA COG2821
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];
6-353 3.98e-143

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


Pssm-ID: 442069 [Multi-domain]  Cd Length: 388  Bit Score: 410.80  E-value: 3.98e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720   6 VKYLLMGTVVAMLAACSSKPTDRGQQYKDGKFTQpfslVNQPDAVGapINAGDFAEQINHIRNSSPRLYGNQSN------ 79
Cdd:COG2821   1 MRRLLLLLALLLLAACATQPPPPGAAAPDARLQP----VSFSDLPG--WADDDLAAALPAFRRSCRRLARRPAAsaygit 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720  80 ------VYNAVQEWLRA-GGDTRNMRQFGIDAWQMEGADNYGNVQFTGYYTPVIQARHTRQGEFQYPIYRMPPK------ 146
Cdd:COG2821  75 aadwraACAAARQLPAAdPAAARAFFEREFQPYQVVGPDGGGNGLFTGYYEPELEGSRTRTAEYRYPLYRRPPDlvtvdl 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720 147 ----------RGRL--------PSRAEIYAGALSDK-YILAYSNSLMDNFIMDVQGSGYIDFGDGSpLNFFSYAGKNGHA 207
Cdd:COG2821 155 gsfelkgkrlRGRLeggrlvpyPTRAEIEAGALAGRgLELAWVDDPVDAFFLQIQGSGRVRLPDGS-LIRVGYAGKNGHP 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720 208 YRSIGKVLIDRGEVKKEDMSMQAIRHWGETHsEAEVRELLEQNPSFVFFKPQ--SFAPVKGASAVPLVGRASVASDRSII 285
Cdd:COG2821 234 YTSIGRLLIDRGELPLEQMSMQAIRAWLRAN-PEELRELLNQNPSYVFFRELpgPDAGPLGALGVPLTPGRSIAVDPSLI 312
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130720 286 PPGTTLLAEVPLLDNNgkFNGQYELRLMVALDVGGAIKG-QHFDIYQGIGPEAGHRAGWYNHYGRVWVL 353
Cdd:COG2821 313 PLGAPVWLETTLPDAN--FSGKPLRRLMIAQDTGGAIKGaVRADLFWGTGDEAGERAGRMKHPGRLWVL 379
mltA_B_like cd14472
Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a ...
126-259 7.52e-84

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: 250.73  E-value: 7.52e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720 126 IQARHTRQGEFQYPIYRMPPKRGRLPSRAEIYAGALSDKYILAYSNSLMDNFIMDVQGSGYIDFGDGSPLNFFSYAGKNG 205
Cdd:cd14472   1 IQARHTRQGEFQYPIYRIPPKRGRLSSRAEIYAGALSDKYILAYSNSLVDNFIADVQGSGYIDFGDGSPLNFFSYAGKNG 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 16130720 206 HAYRSIGKVLIDRGEVKKEDMSMQAIRHWGETHSEAEVRELLEQNPSFVFFKPQ 259
Cdd:cd14472  81 HAYRSIGKVLIDRGEVKKEDISSQAIRHWGETHSEAEVRELLEQNPSFVFFKPQ 134
MltA smart00925
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
125-257 1.50e-60

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: 191.62  E-value: 1.50e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720    125 VIQARHTRQGEFQYPIYRMPP---------------------KRGRLPSRAEIYAGALSDK-YILAYSNSLMDNFIMDVQ 182
Cdd:smart00925   1 VLEGSRTRTGRYRYPLYRRPDdlvvvdlfdpelkgkrlrgggKLVPYPTRAEIEDGALDGRgLELAWVDDPVDLFFLQIQ 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130720    183 GSGYIDFGDGSpLNFFSYAGKNGHAYRSIGKVLIDRGEVKKEDMSMQAIRHWGETHsEAEVRELLEQNPSFVFFK 257
Cdd:smart00925  81 GSGRVRLPDGR-LIRVGYAGKNGHPYRSIGRLLIDRGEIPKEEASMQAIRAWLRAN-PERVDELLNRNPSYVFFR 153
MltA pfam03562
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
55-257 5.68e-51

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: 169.67  E-value: 5.68e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720    55 NAGDFAEQINHIRNSSPRLyGNQSNVYNAV---QEWLRAGGDTRNMRQF---GIDAWQMEGADNYGnvQFTGYYTPVIQA 128
Cdd:pfam03562   2 QDDDLAAALPAFRRSCARL-KKRAPDWLPAcaaARSLPPSDSPAAARAFferEFTPYQVVGPGSDG--LFTGYYEPELEG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720   129 RHTRQGEFQYPIYRMPP----------------KRGRL--------PSRAEIYA-GALSDK-YILAYSNSLMDNFIMDVQ 182
Cdd:pfam03562  79 SRTRTAEYRYPLYRRPPdlvtvdlgffplkgkrLRGRLvggwlvpyPTRAEIEGkGALSGRgLELAWLRDPVDAFFLQIQ 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130720   183 GSGYIDFGDGSPLnFFSYAGKNGHAYRSIGKVLIDRGEVKKEDMSMQAIRHWGETHSEaEVRELLEQNPSFVFFK 257
Cdd:pfam03562 159 GSGRLRLPDGSVV-RVGYAGQNGHPYTSIGRELIDRGELPLEQASMQGIRAWLRANPE-ELDELLNRNPSYVFFR 231
 
Name Accession Description Interval E-value
mltA PRK11162
murein transglycosylase A; Provisional
1-354 0e+00

murein transglycosylase A; Provisional


Pssm-ID: 236866 [Multi-domain]  Cd Length: 355  Bit Score: 730.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720    1 MKGRWVKYLLMGTVVAMLAACSSKPTDRGQQYKDGKFTQPFSLVNQPDAVGAPINAGDFAEQINHIRNSSPRLYGNQSNV 80
Cdd:PRK11162   1 MKGRWVKYLLTGTVLALLAGCSSKPTDRGQQYKDGKFTQPLSLVNQPNASGKPINAGDFAEQVNQIRNSSPRLYGRYSNT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720   81 YNAVQEWLRAGGDTRNMRQFGIDAWQMEGADNYGNVQFTGYYTPVIQARHTRQGEFQYPIYRMPPKRGRLPSRAEIYAGA 160
Cdd:PRK11162  81 YNAVQEWLLAGGDTRELRQFGIQAWQMEGVDNYGNVQFTGYYTPVIQARHTPQGEFQYPIYRMPPKRGRLPSRAEIYAGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720  161 LSDK-YILAYSNSLMDNFIMDVQGSGYIDFGDGSPLNFFSYAGKNGHAYRSIGKVLIDRGEVKKEDMSMQAIRHWGETHS 239
Cdd:PRK11162 161 LSGKgLELAYSNSLIDNFIMEVQGSGYVDFGDGRPLNFFAYAGKNGHAYRSIGKVLIDRGEVPKEDMSMQAIREWGEKHS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720  240 EAEVRELLEQNPSFVFFKPQSFAPVKGASAVPLVGRASVASDRSIIPPGTTLLAEVPLLDNNGKFNGQYELRLMVALDVG 319
Cdd:PRK11162 241 EAEVRELLEQNPSFVFFKPQPFAPVKGASAVPLVAMASVASDRSIIPPGTVLLAEVPLLDNNGKFTGKYELRLMVALDVG 320
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 16130720  320 GAIKGQHFDIYQGIGPEAGHRAGWYNHYGRVWVLK 354
Cdd:PRK11162 321 GAIKGQHFDIYQGIGPEAGHRAGHYNHYGRVWVLK 355
MltA COG2821
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];
6-353 3.98e-143

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


Pssm-ID: 442069 [Multi-domain]  Cd Length: 388  Bit Score: 410.80  E-value: 3.98e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720   6 VKYLLMGTVVAMLAACSSKPTDRGQQYKDGKFTQpfslVNQPDAVGapINAGDFAEQINHIRNSSPRLYGNQSN------ 79
Cdd:COG2821   1 MRRLLLLLALLLLAACATQPPPPGAAAPDARLQP----VSFSDLPG--WADDDLAAALPAFRRSCRRLARRPAAsaygit 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720  80 ------VYNAVQEWLRA-GGDTRNMRQFGIDAWQMEGADNYGNVQFTGYYTPVIQARHTRQGEFQYPIYRMPPK------ 146
Cdd:COG2821  75 aadwraACAAARQLPAAdPAAARAFFEREFQPYQVVGPDGGGNGLFTGYYEPELEGSRTRTAEYRYPLYRRPPDlvtvdl 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720 147 ----------RGRL--------PSRAEIYAGALSDK-YILAYSNSLMDNFIMDVQGSGYIDFGDGSpLNFFSYAGKNGHA 207
Cdd:COG2821 155 gsfelkgkrlRGRLeggrlvpyPTRAEIEAGALAGRgLELAWVDDPVDAFFLQIQGSGRVRLPDGS-LIRVGYAGKNGHP 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720 208 YRSIGKVLIDRGEVKKEDMSMQAIRHWGETHsEAEVRELLEQNPSFVFFKPQ--SFAPVKGASAVPLVGRASVASDRSII 285
Cdd:COG2821 234 YTSIGRLLIDRGELPLEQMSMQAIRAWLRAN-PEELRELLNQNPSYVFFRELpgPDAGPLGALGVPLTPGRSIAVDPSLI 312
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130720 286 PPGTTLLAEVPLLDNNgkFNGQYELRLMVALDVGGAIKG-QHFDIYQGIGPEAGHRAGWYNHYGRVWVL 353
Cdd:COG2821 313 PLGAPVWLETTLPDAN--FSGKPLRRLMIAQDTGGAIKGaVRADLFWGTGDEAGERAGRMKHPGRLWVL 379
mltA_B_like cd14472
Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a ...
126-259 7.52e-84

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: 250.73  E-value: 7.52e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720 126 IQARHTRQGEFQYPIYRMPPKRGRLPSRAEIYAGALSDKYILAYSNSLMDNFIMDVQGSGYIDFGDGSPLNFFSYAGKNG 205
Cdd:cd14472   1 IQARHTRQGEFQYPIYRIPPKRGRLSSRAEIYAGALSDKYILAYSNSLVDNFIADVQGSGYIDFGDGSPLNFFSYAGKNG 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 16130720 206 HAYRSIGKVLIDRGEVKKEDMSMQAIRHWGETHSEAEVRELLEQNPSFVFFKPQ 259
Cdd:cd14472  81 HAYRSIGKVLIDRGEVKKEDISSQAIRHWGETHSEAEVRELLEQNPSFVFFKPQ 134
MltA smart00925
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
125-257 1.50e-60

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: 191.62  E-value: 1.50e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720    125 VIQARHTRQGEFQYPIYRMPP---------------------KRGRLPSRAEIYAGALSDK-YILAYSNSLMDNFIMDVQ 182
Cdd:smart00925   1 VLEGSRTRTGRYRYPLYRRPDdlvvvdlfdpelkgkrlrgggKLVPYPTRAEIEDGALDGRgLELAWVDDPVDLFFLQIQ 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130720    183 GSGYIDFGDGSpLNFFSYAGKNGHAYRSIGKVLIDRGEVKKEDMSMQAIRHWGETHsEAEVRELLEQNPSFVFFK 257
Cdd:smart00925  81 GSGRVRLPDGR-LIRVGYAGKNGHPYRSIGRLLIDRGEIPKEEASMQAIRAWLRAN-PERVDELLNRNPSYVFFR 153
mlta_B cd14668
Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a ...
126-259 1.35e-54

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: 176.56  E-value: 1.35e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720 126 IQARHTRQGEFQYPIYRMPP------------------KRGRL--------PSRAEIYAGALSDK-YILAYSNSLMDNFI 178
Cdd:cd14668   1 LEGSRTPTAEYRYPLYGRPPdlvtvdlgefypelkgkrLRGRVeggrlvpyYTRAEIEAGALLGRgLELAWLDDPVDAFF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720 179 MDVQGSGYIDFGDGSpLNFFSYAGKNGHAYRSIGKVLIDRGEVKKEDMSMQAIRHWGETHSEaEVRELLEQNPSFVFFKP 258
Cdd:cd14668  81 LQIQGSGRLRLPDGS-VVRVGYAGKNGHPYRSIGRVLIDRGELPKEQMSMQAIRAWLRANPE-RARELLNENPSYVFFRE 158

                .
gi 16130720 259 Q 259
Cdd:cd14668 159 L 159
MltA pfam03562
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
55-257 5.68e-51

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: 169.67  E-value: 5.68e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720    55 NAGDFAEQINHIRNSSPRLyGNQSNVYNAV---QEWLRAGGDTRNMRQF---GIDAWQMEGADNYGnvQFTGYYTPVIQA 128
Cdd:pfam03562   2 QDDDLAAALPAFRRSCARL-KKRAPDWLPAcaaARSLPPSDSPAAARAFferEFTPYQVVGPGSDG--LFTGYYEPELEG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720   129 RHTRQGEFQYPIYRMPP----------------KRGRL--------PSRAEIYA-GALSDK-YILAYSNSLMDNFIMDVQ 182
Cdd:pfam03562  79 SRTRTAEYRYPLYRRPPdlvtvdlgffplkgkrLRGRLvggwlvpyPTRAEIEGkGALSGRgLELAWLRDPVDAFFLQIQ 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130720   183 GSGYIDFGDGSPLnFFSYAGKNGHAYRSIGKVLIDRGEVKKEDMSMQAIRHWGETHSEaEVRELLEQNPSFVFFK 257
Cdd:pfam03562 159 GSGRLRLPDGSVV-RVGYAGQNGHPYTSIGRELIDRGELPLEQASMQGIRAWLRANPE-ELDELLNRNPSYVFFR 231
DPBB_MltA-like cd22785
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
261-353 4.69e-33

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: 118.51  E-value: 4.69e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720 261 FAPVKGASAVPLVGRASVASDRSIIPPGTTLLaeVPLLDNNGKFNGQYELRLMVALDVGGAIKGQHFDIYQGIGPEAGHR 340
Cdd:cd22785   7 YTPPRGALGVPLTPFRSVAVDPSVIPLGSVVY--IPALDGVKLPDGEPHDGLFIAQDTGGAIKGKHIDVFTGSGDEAGEL 84
                        90
                ....*....|...
gi 16130720 341 AGWYNHYGRVWVL 353
Cdd:cd22785  85 AGKLNHTGRVYVL 97
mltA_like_LT_A cd14485
Domain A of MltA and related lytic transglycosylase; domain A is interrupted by domain B; ...
270-353 1.33e-31

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: 116.96  E-value: 1.33e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720 270 VPLVGRASVASDRSIIPPGTTLLAEVPLLDNNGkfNGQYELRLMVALDVGGAIKG-QHFDIYQGIGPEAGHRAGWYNHYG 348
Cdd:cd14485  77 VPLTPGRSLAVDRSLIPLGAPVWLETPLPDANG--GGKPLRRLVIAQDTGGAIKGpVRADLFWGSGDEAGELAGRMKHPG 154

                ....*
gi 16130720 349 RVWVL 353
Cdd:cd14485 155 RLWVL 159
3D pfam06725
3D domain; This short presumed domain contains three conserved aspartate residues, hence the ...
276-354 1.49e-28

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: 105.75  E-value: 1.49e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130720   276 ASVASDRSIIPPGTTLLAEVPLldnngkfNGQYELRLMVALDVGGAIKGQHFDIYQGIGPEAGHRAGWYNHYGRVWVLK 354
Cdd:pfam06725   1 RSIAVDPSVIPLGTPVYVEGPL-------GGKPVYRLAIAQDTGGAIKGNRIDLYFGTGDEAGNLAGLYRKTGRVYILL 72
3D_domain cd14486
3D domain, named for 3 conserved aspartate residues, is found in mltA-like lytic ...
258-351 1.17e-22

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: 91.28  E-value: 1.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720 258 PQSFAPVKGASAVPLVGRASVASDRSIIPPGTTLLAEVplldnngkFNGQYELRLMVALDVGGAIKGQHFDIYQGIGPEA 337
Cdd:cd14486  20 EFSFSFRLTASGRPPVPYRTIAVDPSVIPLGSVVYIPE--------LRGLPNDGVFVAEDTGGAIKGNHIDVYTGDGPDA 91
                        90
                ....*....|....
gi 16130720 338 GHRAGWYnHYGRVW 351
Cdd:cd14486  92 RSNALKT-VTVYVV 104
mlta_related_B cd14669
putative domain B insert of mltA_type lytic transglycosylases; Escherichia coli MltA is a ...
126-257 6.54e-16

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: 73.61  E-value: 6.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720 126 IQARHTRQGEFQYPIYRMP-----PKrgrlPSRAEIYAGALSDKYILAYSNSLMDNFIMDVQGSGYIDFGDGSPLNfFSY 200
Cdd:cd14669   3 IGSRTYPGGAFLYPVYGNPgdmivPY----YTRAEIERGALWEAKVIAYVKDPTDLYLMQLQGSGKVKLPDGTVFR-IAY 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16130720 201 AGKNGHAYRSIGKVLidRGEVKKedmSMQAIRHWGETHseaEVRELLEQNPSFVFFK 257
Cdd:cd14669  78 AEQNGRPFLPPVASA--KGSLTP---SEAANCIALNPP---EVAAFAISDPSYVFFR 126
DPBB_MltA_YuiC-like cd22784
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
257-350 9.85e-15

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: 68.83  E-value: 9.85e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130720 257 KPQSFAPVKGASAVPLVGRASVASDRSIIPPGTTLLAEvplldnNGKFNGQYelrlmVALDVGGAIKGQHFDIYQGIGPE 336
Cdd:cd22784  11 EQTDGGPGITASGVTLRGYGTVAVDRDLIPLGTKVKIE------GPGSGGEY-----VVLDRGGAIKGNRIDIYFPSEKE 79
                        90
                ....*....|....
gi 16130720 337 AgHRAGWYNHYGRV 350
Cdd:cd22784  80 A-KKFGRQKVTVTV 92
3D_containing_proteins cd14667
Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; ...
267-330 2.43e-05

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: 42.51  E-value: 2.43e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130720 267 ASAVPLVGRAsVASDRSIIPPGTTLLAEvplldnngkFNGQYelrlmVALDVGGAIKGQHFDIY 330
Cdd:cd14667  22 SGGLPVGGGT-IAVDPSVIPLGTKVYIE---------GYGVY-----VVEDTGGAIKGNRIDIY 70
COG3584 COG3584
3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D ...
267-330 2.64e-04

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: 39.32  E-value: 2.64e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130720 267 ASAVPLVGRASVASDRSIIPPGTTLLAEvplldnnGkfNGQYelrlmVALDVGGAIKGQHFDIY 330
Cdd:COG3584  22 ASGTRLRPGGVIAVDPDVIPLGTKVYIE-------G--YGYA-----VAEDTGGAIKGNRIDIY 71
 
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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