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Conserved domains on  [gi|479757551|gb|ENT27376|]
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hypothetical protein B985_01472 [Brucella suis 01-5744]

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

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List of domain hits

 Name Accession Description Interval E-value
MltA COG2821
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];
12-366 8.44e-171

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


:

Pssm-ID: 442069 [Multi-domain]  Cd Length: 388  Bit Score: 481.30  E-value: 8.44e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551  12 FRPASFGDCPGWDRDDQALAFAAFRRSADYAENNSYGSGsLGLSFEALKPIFAAARALDRPDRGEARRFFEAHFVPCRVE 91
Cdd:COG2821   32 LQPVSFSDLPGWADDDLAAALPAFRRSCRRLARRPAASA-YGITAADWRAACAAARQLPAADPAAARAFFEREFQPYQVV 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551  92 PE--QGKGFVTGFYEPEIEASRIADARFKVPFLRKPADLVKVSDENRpaGLDPSFAFARQTESGLEEYADRRAIEQGALS 169
Cdd:COG2821  111 GPdgGGNGLFTGYYEPELEGSRTRTAEYRYPLYRRPPDLVTVDLGSF--ELKGKRLRGRLEGGRLVPYPTRAEIEAGALA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 170 GHGLEIAFVADRVDAFFAHVQGAARLKLTDGETLRVTYAAKTGHPFTGIGRILVDEGEIAAAEISMQSIRRWLSAHPDRA 249
Cdd:COG2821  189 GRGLELAWVDDPVDAFFLQIQGSGRVRLPDGSLIRVGYAGKNGHPYTSIGRLLIDRGELPLEQMSMQAIRAWLRANPEEL 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 250 DELIWKNRSYIFFREAPvdDPAAGPVAAAKVPLTAGRSMAVDRLLHTFGTPFYVSAPTL-CAFGGEPFARLMIAQDTGTA 328
Cdd:COG2821  269 RELLNQNPSYVFFRELP--GPDAGPLGALGVPLTPGRSIAVDPSLIPLGAPVWLETTLPdANFSGKPLRRLMIAQDTGGA 346

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 479757551 329 IVGPARGDLFTGSGDEADKIAGGIKDEADFYVLVPRNM 366
Cdd:COG2821  347 IKGAVRADLFWGTGDEAGERAGRMKHPGRLWVLLPKGA 384
 
Name Accession Description Interval E-value
MltA COG2821
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];
12-366 8.44e-171

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


Pssm-ID: 442069 [Multi-domain]  Cd Length: 388  Bit Score: 481.30  E-value: 8.44e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551  12 FRPASFGDCPGWDRDDQALAFAAFRRSADYAENNSYGSGsLGLSFEALKPIFAAARALDRPDRGEARRFFEAHFVPCRVE 91
Cdd:COG2821   32 LQPVSFSDLPGWADDDLAAALPAFRRSCRRLARRPAASA-YGITAADWRAACAAARQLPAADPAAARAFFEREFQPYQVV 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551  92 PE--QGKGFVTGFYEPEIEASRIADARFKVPFLRKPADLVKVSDENRpaGLDPSFAFARQTESGLEEYADRRAIEQGALS 169
Cdd:COG2821  111 GPdgGGNGLFTGYYEPELEGSRTRTAEYRYPLYRRPPDLVTVDLGSF--ELKGKRLRGRLEGGRLVPYPTRAEIEAGALA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 170 GHGLEIAFVADRVDAFFAHVQGAARLKLTDGETLRVTYAAKTGHPFTGIGRILVDEGEIAAAEISMQSIRRWLSAHPDRA 249
Cdd:COG2821  189 GRGLELAWVDDPVDAFFLQIQGSGRVRLPDGSLIRVGYAGKNGHPYTSIGRLLIDRGELPLEQMSMQAIRAWLRANPEEL 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 250 DELIWKNRSYIFFREAPvdDPAAGPVAAAKVPLTAGRSMAVDRLLHTFGTPFYVSAPTL-CAFGGEPFARLMIAQDTGTA 328
Cdd:COG2821  269 RELLNQNPSYVFFRELP--GPDAGPLGALGVPLTPGRSIAVDPSLIPLGAPVWLETTLPdANFSGKPLRRLMIAQDTGGA 346

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 479757551 329 IVGPARGDLFTGSGDEADKIAGGIKDEADFYVLVPRNM 366
Cdd:COG2821  347 IKGAVRADLFWGTGDEAGERAGRMKHPGRLWVLLPKGA 384
MltA pfam03562
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
 23-263 8.25e-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: 300.25  E-value: 8.25e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551   23 WDRDDQALAFAAFRRSADYaennsygsgsLGLSFEALKPIFAAARALDRPDRG-EARRFFEAHFVPCRVEPEQGKGFVTG 101
Cdd:pfam03562   1 WQDDDLAAALPAFRRSCAR----------LKKRAPDWLPACAAARSLPPSDSPaAARAFFEREFTPYQVVGPGSDGLFTG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551  102 FYEPEIEASRIADARFKVPFLRKPADLVKVSDENRPagLDPSFAFARQTESGLEEYADRRAIEQ-GALSGHGLEIAFVAD 180
Cdd:pfam03562  71 YYEPELEGSRTRTAEYRYPLYRRPPDLVTVDLGFFP--LKGKRLRGRLVGGWLVPYPTRAEIEGkGALSGRGLELAWLRD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551  181 RVDAFFAHVQGAARLKLTDGETLRVTYAAKTGHPFTGIGRILVDEGEIAAAEISMQSIRRWLSAHPDRADELIWKNRSYI 260
Cdd:pfam03562 149 PVDAFFLQIQGSGRLRLPDGSVVRVGYAGQNGHPYTSIGRELIDRGELPLEQASMQGIRAWLRANPEELDELLNRNPSYV 228


                  ...
gi 479757551  261 FFR 263
Cdd:pfam03562 229 FFR 231
mlta_B cd14668
Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a ...
 107-265 2.63e-74

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: 227.41  E-value: 2.63e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 107 IEASRIADARFKVPFLRKPADLVKVSDENRPAGLDPSFAFARQTESGLEEYADRRAIEQGALSGHGLEIAFVADRVDAFF 186
Cdd:cd14668    1 LEGSRTPTAEYRYPLYGRPPDLVTVDLGEFYPELKGKRLRGRVEGGRLVPYYTRAEIEAGALLGRGLELAWLDDPVDAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 479757551 187 AHVQGAARLKLTDGETLRVTYAAKTGHPFTGIGRILVDEGEIAAAEISMQSIRRWLSAHPDRADELIWKNRSYIFFREA 265
Cdd:cd14668   81 LQIQGSGRLRLPDGSVVRVGYAGKNGHPYRSIGRVLIDRGELPKEQMSMQAIRAWLRANPERARELLNENPSYVFFREL 159
MltA smart00925
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
 106-263 3.48e-72

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: 221.67  E-value: 3.48e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551   106 EIEASRIADARFKVPFLRKPADLVKVSDenrpagLDPSFAFARQTESG-LEEYADRRAIEQGALSGHGLEIAFVADRVDA 184
Cdd:smart00925   1 VLEGSRTRTGRYRYPLYRRPDDLVVVDL------FDPELKGKRLRGGGkLVPYPTRAEIEDGALDGRGLELAWVDDPVDL 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 479757551   185 FFAHVQGAARLKLTDGETLRVTYAAKTGHPFTGIGRILVDEGEIAAAEISMQSIRRWLSAHPDRADELIWKNRSYIFFR 263
Cdd:smart00925  75 FFLQIQGSGRVRLPDGRLIRVGYAGKNGHPYRSIGRLLIDRGEIPKEEASMQAIRAWLRANPERVDELLNRNPSYVFFR 153
mltA PRK11162
murein transglycosylase A; Provisional
 100-350 9.79e-49

murein transglycosylase A; Provisional


Pssm-ID: 236866 [Multi-domain]  Cd Length: 355  Bit Score: 167.78  E-value: 9.79e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 100 TGFYEPEIEASRIADARFKVPFLRKPAdlvkvSDENRPagldpsfafarqtesgleeyaDRRAIEQGALSGHGLEIAFVA 179
Cdd:PRK11162 119 TGYYTPVIQARHTPQGEFQYPIYRMPP-----KRGRLP---------------------SRAEIYAGALSGKGLELAYSN 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 180 DRVDAFFAHVQGAARLKLTDGETLR-VTYAAKTGHPFTGIGRILVDEGEIAAAEISMQSIRRWLSAHPD-RADELIWKNR 257
Cdd:PRK11162 173 SLIDNFIMEVQGSGYVDFGDGRPLNfFAYAGKNGHAYRSIGKVLIDRGEVPKEDMSMQAIREWGEKHSEaEVRELLEQNP 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 258 SYIFFREAPvddpaAGPV-AAAKVPLTAGRSMAVDRLLHTFGTPFYVSAPTLCA---FGGEPFARLMIAQDTGTAIVGpA 333
Cdd:PRK11162 253 SFVFFKPQP-----FAPVkGASAVPLVAMASVASDRSIIPPGTVLLAEVPLLDNngkFTGKYELRLMVALDVGGAIKG-Q 326

                        250
                 ....*....|....*..
gi 479757551 334 RGDLFTGSGDEADKIAG 350
Cdd:PRK11162 327 HFDIYQGIGPEAGHRAG 343
 
Name Accession Description Interval E-value
MltA COG2821
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];
12-366 8.44e-171

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


Pssm-ID: 442069 [Multi-domain]  Cd Length: 388  Bit Score: 481.30  E-value: 8.44e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551  12 FRPASFGDCPGWDRDDQALAFAAFRRSADYAENNSYGSGsLGLSFEALKPIFAAARALDRPDRGEARRFFEAHFVPCRVE 91
Cdd:COG2821   32 LQPVSFSDLPGWADDDLAAALPAFRRSCRRLARRPAASA-YGITAADWRAACAAARQLPAADPAAARAFFEREFQPYQVV 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551  92 PE--QGKGFVTGFYEPEIEASRIADARFKVPFLRKPADLVKVSDENRpaGLDPSFAFARQTESGLEEYADRRAIEQGALS 169
Cdd:COG2821  111 GPdgGGNGLFTGYYEPELEGSRTRTAEYRYPLYRRPPDLVTVDLGSF--ELKGKRLRGRLEGGRLVPYPTRAEIEAGALA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 170 GHGLEIAFVADRVDAFFAHVQGAARLKLTDGETLRVTYAAKTGHPFTGIGRILVDEGEIAAAEISMQSIRRWLSAHPDRA 249
Cdd:COG2821  189 GRGLELAWVDDPVDAFFLQIQGSGRVRLPDGSLIRVGYAGKNGHPYTSIGRLLIDRGELPLEQMSMQAIRAWLRANPEEL 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 250 DELIWKNRSYIFFREAPvdDPAAGPVAAAKVPLTAGRSMAVDRLLHTFGTPFYVSAPTL-CAFGGEPFARLMIAQDTGTA 328
Cdd:COG2821  269 RELLNQNPSYVFFRELP--GPDAGPLGALGVPLTPGRSIAVDPSLIPLGAPVWLETTLPdANFSGKPLRRLMIAQDTGGA 346

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 479757551 329 IVGPARGDLFTGSGDEADKIAGGIKDEADFYVLVPRNM 366
Cdd:COG2821  347 IKGAVRADLFWGTGDEAGERAGRMKHPGRLWVLLPKGA 384
MltA pfam03562
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
 23-263 8.25e-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: 300.25  E-value: 8.25e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551   23 WDRDDQALAFAAFRRSADYaennsygsgsLGLSFEALKPIFAAARALDRPDRG-EARRFFEAHFVPCRVEPEQGKGFVTG 101
Cdd:pfam03562   1 WQDDDLAAALPAFRRSCAR----------LKKRAPDWLPACAAARSLPPSDSPaAARAFFEREFTPYQVVGPGSDGLFTG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551  102 FYEPEIEASRIADARFKVPFLRKPADLVKVSDENRPagLDPSFAFARQTESGLEEYADRRAIEQ-GALSGHGLEIAFVAD 180
Cdd:pfam03562  71 YYEPELEGSRTRTAEYRYPLYRRPPDLVTVDLGFFP--LKGKRLRGRLVGGWLVPYPTRAEIEGkGALSGRGLELAWLRD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551  181 RVDAFFAHVQGAARLKLTDGETLRVTYAAKTGHPFTGIGRILVDEGEIAAAEISMQSIRRWLSAHPDRADELIWKNRSYI 260
Cdd:pfam03562 149 PVDAFFLQIQGSGRLRLPDGSVVRVGYAGQNGHPYTSIGRELIDRGELPLEQASMQGIRAWLRANPEELDELLNRNPSYV 228


                  ...
gi 479757551  261 FFR 263
Cdd:pfam03562 229 FFR 231
mlta_B cd14668
Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a ...
 107-265 2.63e-74

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: 227.41  E-value: 2.63e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 107 IEASRIADARFKVPFLRKPADLVKVSDENRPAGLDPSFAFARQTESGLEEYADRRAIEQGALSGHGLEIAFVADRVDAFF 186
Cdd:cd14668    1 LEGSRTPTAEYRYPLYGRPPDLVTVDLGEFYPELKGKRLRGRVEGGRLVPYYTRAEIEAGALLGRGLELAWLDDPVDAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 479757551 187 AHVQGAARLKLTDGETLRVTYAAKTGHPFTGIGRILVDEGEIAAAEISMQSIRRWLSAHPDRADELIWKNRSYIFFREA 265
Cdd:cd14668   81 LQIQGSGRLRLPDGSVVRVGYAGKNGHPYRSIGRVLIDRGELPKEQMSMQAIRAWLRANPERARELLNENPSYVFFREL 159
MltA smart00925
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
 106-263 3.48e-72

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: 221.67  E-value: 3.48e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551   106 EIEASRIADARFKVPFLRKPADLVKVSDenrpagLDPSFAFARQTESG-LEEYADRRAIEQGALSGHGLEIAFVADRVDA 184
Cdd:smart00925   1 VLEGSRTRTGRYRYPLYRRPDDLVVVDL------FDPELKGKRLRGGGkLVPYPTRAEIEDGALDGRGLELAWVDDPVDL 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 479757551   185 FFAHVQGAARLKLTDGETLRVTYAAKTGHPFTGIGRILVDEGEIAAAEISMQSIRRWLSAHPDRADELIWKNRSYIFFR 263
Cdd:smart00925  75 FFLQIQGSGRVRLPDGRLIRVGYAGKNGHPYRSIGRLLIDRGEIPKEEASMQAIRAWLRANPERVDELLNRNPSYVFFR 153
mltA PRK11162
murein transglycosylase A; Provisional
 100-350 9.79e-49

murein transglycosylase A; Provisional


Pssm-ID: 236866 [Multi-domain]  Cd Length: 355  Bit Score: 167.78  E-value: 9.79e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 100 TGFYEPEIEASRIADARFKVPFLRKPAdlvkvSDENRPagldpsfafarqtesgleeyaDRRAIEQGALSGHGLEIAFVA 179
Cdd:PRK11162 119 TGYYTPVIQARHTPQGEFQYPIYRMPP-----KRGRLP---------------------SRAEIYAGALSGKGLELAYSN 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 180 DRVDAFFAHVQGAARLKLTDGETLR-VTYAAKTGHPFTGIGRILVDEGEIAAAEISMQSIRRWLSAHPD-RADELIWKNR 257
Cdd:PRK11162 173 SLIDNFIMEVQGSGYVDFGDGRPLNfFAYAGKNGHAYRSIGKVLIDRGEVPKEDMSMQAIREWGEKHSEaEVRELLEQNP 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 258 SYIFFREAPvddpaAGPV-AAAKVPLTAGRSMAVDRLLHTFGTPFYVSAPTLCA---FGGEPFARLMIAQDTGTAIVGpA 333
Cdd:PRK11162 253 SFVFFKPQP-----FAPVkGASAVPLVAMASVASDRSIIPPGTVLLAEVPLLDNngkFTGKYELRLMVALDVGGAIKG-Q 326

                        250
                 ....*....|....*..
gi 479757551 334 RGDLFTGSGDEADKIAG 350
Cdd:PRK11162 327 HFDIYQGIGPEAGHRAG 343
mltA_like_LT_A cd14485
Domain A of MltA and related lytic transglycosylase; domain A is interrupted by domain B; ...
 229-361 6.56e-35

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: 125.82  E-value: 6.56e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 229 AAAEISMQSIRRWLSAHPDRADELIWKNRSYIFFREAPVDDPAAG-------PvaaaKVPLTAGRSMAVDRLLHTFGTPF 301
Cdd:cd14485   23 GGLALTWGDLRASLEALLAFLLARLDAAPEALADFFQWVDGSGEGlftgyyeP----GVPLTPGRSLAVDRSLIPLGAPV 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 479757551 302 YVSAPTL-CAFGGEPFARLMIAQDTGTAIVGPARGDLFTGSGDEADKIAGGIKDEADFYVL 361
Cdd:cd14485   99 WLETPLPdANGGGKPLRRLVIAQDTGGAIKGPVRADLFWGSGDEAGELAGRMKHPGRLWVL 159
3D pfam06725
3D domain; This short presumed domain contains three conserved aspartate residues, hence the ...
 286-362 2.78e-25

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: 97.28  E-value: 2.78e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 479757551  286 RSMAVDRLLHTFGTPFYVSAPtlcaFGGEPFARLMIAQDTGTAIVGPaRGDLFTGSGDEADKIAGGIKDEADFYVLV 362
Cdd:pfam06725   1 RSIAVDPSVIPLGTPVYVEGP----LGGKPVYRLAIAQDTGGAIKGN-RIDLYFGTGDEAGNLAGLYRKTGRVYILL 72
DPBB_MltA-like cd22785
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
 274-361 8.05e-24

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: 94.25  E-value: 8.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 274 PVAAAKVPLTAGRSMAVDRLLHTFGTPFYVSAPT-LCAFGGEPFARLMIAQDTGTAIVGpARGDLFTGSGDEADKIAGGI 352
Cdd:cd22785   10 PRGALGVPLTPFRSVAVDPSVIPLGSVVYIPALDgVKLPDGEPHDGLFIAQDTGGAIKG-KHIDVFTGSGDEAGELAGKL 88


                 ....*....
gi 479757551 353 KDEADFYVL 361
Cdd:cd22785   89 NHTGRVYVL 97
mltA_B_like cd14472
Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a ...
 107-263 8.06e-19

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: 81.63  E-value: 8.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 107 IEASRIADARFKVPFLRKPADLVKvsdenrpagldpsfafarqtesgleeYADRRAIEQGALSGHGLeIAFVADRVDAFF 186
Cdd:cd14472    1 IQARHTRQGEFQYPIYRIPPKRGR--------------------------LSSRAEIYAGALSDKYI-LAYSNSLVDNFI 53

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 479757551 187 AHVQGAARLKLTDGETL-RVTYAAKTGHPFTGIGRILVDEGEIAAAEISMQSIRRWLSAHPDR-ADELIWKNRSYIFFR 263
Cdd:cd14472   54 ADVQGSGYIDFGDGSPLnFFSYAGKNGHAYRSIGKVLIDRGEVKKEDISSQAIRHWGETHSEAeVRELLEQNPSFVFFK 132
mlta_related_B cd14669
putative domain B insert of mltA_type lytic transglycosylases; Escherichia coli MltA is a ...
 157-265 6.34e-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: 6.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 157 YADRRAIEQGALSGHGLeIAFVADRVDAFFAHVQGAARLKLTDGETLRVTYAAKTGHPFTGIGRILvdEGEIAAAEismQ 236
Cdd:cd14669   28 YYTRAEIERGALWEAKV-IAYVKDPTDLYLMQLQGSGKVKLPDGTVFRIAYAEQNGRPFLPPVASA--KGSLTPSE---A 101

                         90       100
                 ....*....|....*....|....*....
gi 479757551 237 SIRRWLSahPDRADELIWKNRSYIFFREA 265
Cdd:cd14669  102 ANCIALN--PPEVAAFAISDPSYVFFRKE 128
3D_domain cd14486
3D domain, named for 3 conserved aspartate residues, is found in mltA-like lytic ...
 274-345 1.30e-05

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: 43.52  E-value: 1.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 479757551 274 PVAAAKVPLTAGRSMAVDRLLHTFGTPFYVSAptlcaFGGEPFARLMIAQDTGTAIVGpARGDLFTGSGDEA 345
Cdd:cd14486   26 RLTASGRPPVPYRTIAVDPSVIPLGSVVYIPE-----LRGLPNDGVFVAEDTGGAIKG-NHIDVYTGDGPDA 91
DPBB_MltA_YuiC-like cd22784
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
 280-345 3.30e-05

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: 42.25  E-value: 3.30e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 479757551 280 VPLTAGRSMAVDRLLHTFGTPFYVSaptlcafgGEPFARLMIAQDTGTAIvGPARGDLFTGSGDEA 345
Cdd:cd22784   24 VTLRGYGTVAVDRDLIPLGTKVKIE--------GPGSGGEYVVLDRGGAI-KGNRIDIYFPSEKEA 80
COG3584 COG3584
3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D ...
 266-361 2.58e-03

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: 36.62  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 266 PVDDPAAGPVAAAKVPLTAGRSMAVDRLLHTFGTPFYVSaptlcafgGEPFArlmIAQDTGTAIVGpARGDLFTGSGDEA 345
Cdd:COG3584   11 PECTGKGGGITASGTRLRPGGVIAVDPDVIPLGTKVYIE--------GYGYA---VAEDTGGAIKG-NRIDIYMPSVSEA 78

                         90
                 ....*....|....*.
gi 479757551 346 DKIagGIKDeADFYVL 361
Cdd:COG3584   79 LNW--GRRT-VTVYIL 91
3D_containing_proteins cd14667
Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; ...
 276-345 2.68e-03

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: 36.73  E-value: 2.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479757551 276 AAAKVPLTAGRSMAVDRLLHTFGTPFYVSAPTLCafggepfarlmIAQDTGTAIVGPaRGDLFTGSGDEA 345
Cdd:cd14667   20 TASGGLPVGGGTIAVDPSVIPLGTKVYIEGYGVY-----------VVEDTGGAIKGN-RIDIYMDSHAEA 77
 
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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