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Conserved domains on  [gi|565865137|ref|WP_023946949|]
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MULTISPECIES: glycoside hydrolase family 25 protein [Streptococcus]

Protein Classification

glycoside hydrolase family 25 protein( domain architecture ID 10158183)

glycoside hydrolase family 25 protein similar to PlyB, a bacteriophage endolysin active against Bacillus anthracis; endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH25_PlyB-like cd06523
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus ...
 53-249 5.97e-69

PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.


:

Pssm-ID: 119383  Cd Length: 177  Bit Score: 210.68  E-value: 5.97e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137  53 PVIDVSGWQRPEEINYDTLSQNISGAIVRVHSGAqtskendasyvNGVDKAFKTHITEFQKRNVPVAVYAYVAGKNVQEM 132
Cdd:cd06523    1 AIVDISEWQGPINWDYDTLSKQLDLVIIRVQYGS-----------NYVDLKYKNNIKEFKKRGIPFGVYAFARGTSTADA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137 133 EKAAEVFYNASSPySPSYYWLDVEEKTMSNMNDGVEAFRAKLESLGAKNIGIYVGVYFMEEHSIDTDKFTSVWIPSYGSD 212
Cdd:cd06523   70 KAEARDFYNRANK-KPTFYVLDVEVTSMSDMNAGVQAFISELRRLGAKKVGLYIGHHFYTTFNLAVSKFDAIWIPAYGSN 148

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 565865137 213 SGFYEatpktdldYDIHQYTSKGKIAGFDHDLDINVI 249
Cdd:cd06523  149 PGTYP--------YDLWQYTDSGYLPGISGNVDLNRL 177
 
Name Accession Description Interval E-value
GH25_PlyB-like cd06523
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus ...
 53-249 5.97e-69

PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.


Pssm-ID: 119383  Cd Length: 177  Bit Score: 210.68  E-value: 5.97e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137  53 PVIDVSGWQRPEEINYDTLSQNISGAIVRVHSGAqtskendasyvNGVDKAFKTHITEFQKRNVPVAVYAYVAGKNVQEM 132
Cdd:cd06523    1 AIVDISEWQGPINWDYDTLSKQLDLVIIRVQYGS-----------NYVDLKYKNNIKEFKKRGIPFGVYAFARGTSTADA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137 133 EKAAEVFYNASSPySPSYYWLDVEEKTMSNMNDGVEAFRAKLESLGAKNIGIYVGVYFMEEHSIDTDKFTSVWIPSYGSD 212
Cdd:cd06523   70 KAEARDFYNRANK-KPTFYVLDVEVTSMSDMNAGVQAFISELRRLGAKKVGLYIGHHFYTTFNLAVSKFDAIWIPAYGSN 148

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 565865137 213 SGFYEatpktdldYDIHQYTSKGKIAGFDHDLDINVI 249
Cdd:cd06523  149 PGTYP--------YDLWQYTDSGYLPGISGNVDLNRL 177
Acm COG3757
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis] ...
 53-264 3.75e-35

Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442971  Cd Length: 208  Bit Score: 125.01  E-value: 3.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137  53 PVIDVSGWQrpEEINYDTL-SQNISGAIVRVHSGAqtskendasyvNGVDKAFKTHITEFQKRNVPVAVYAYVagKNVQE 131
Cdd:COG3757   12 HGIDVSHYQ--GDIDWAAVkAAGIDFAYIKATEGT-----------DYVDPKFARNWAGARAAGLPRGAYHFF--RPCSD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137 132 MEKAAEVFYNASSPYSPSY-YWLDVEEKTMSN-----MNDGVEAFRAKLESLGAKNIGIYVGVYFMEEHsIDTDKFTS-- 203
Cdd:COG3757   77 AAAQADNFISTVPRDPGDLpPVLDLEENGYYGlspaqLRAWLKAFLDEVEAHTGRKPIIYTSPSFYNDY-LGNSDFSDyp 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565865137 204 VWIPSYGSDSGfyeatPKTDLDYDIHQYTSKGKIAGFDHDLDINVisaLKNKEETFRKLFL 264
Cdd:COG3757  156 LWIARYGSSPG-----YLPGRNWTFWQYTSSGRVPGISGNVDLNV---FNGSRDELKALAL 208
Glyco_hydro_25 pfam01183
Glycosyl hydrolases family 25;
55-239 9.34e-11

Glycosyl hydrolases family 25;


Pssm-ID: 426105  Cd Length: 180  Bit Score: 59.30  E-value: 9.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137   55 IDVSGWQrpEEINYDTLSQN-ISGAIVRVHSGAqtskendaSYVngvDKAFKTHITEFQKRNVPVAVYAYVAGKNVQEME 133
Cdd:pfam01183   1 IDVSSYQ--GDIDWQKVKASgVSFVFIKATEGT--------DYV---DPYFTTQYANARAAGLKVGAYHFARPCNSSTAA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137  134 KAAEVFY-NASSPYSPSYYW---LDVEEK---TMSNMNDGVEAFRAKLESLGAKNIGIYVGVYFMEEHSIDTD--KFTSV 204
Cdd:pfam01183  68 AQADYFLsNVQGLGLDAGTLppvLDVEVTtglTKAAATSNILRFLDRVKKQTGYKPVIYTGTSFWTNNLLYGQfiADYPL 147

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 565865137  205 WIPSYGSDsgfYEATPKTDLDYDIHQYTSKGKIAG 239
Cdd:pfam01183 148 WIASYAVT---PPKDYPGWTKWTFWQYTSSGSIPG 179
 
Name Accession Description Interval E-value
GH25_PlyB-like cd06523
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus ...
 53-249 5.97e-69

PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.


Pssm-ID: 119383  Cd Length: 177  Bit Score: 210.68  E-value: 5.97e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137  53 PVIDVSGWQRPEEINYDTLSQNISGAIVRVHSGAqtskendasyvNGVDKAFKTHITEFQKRNVPVAVYAYVAGKNVQEM 132
Cdd:cd06523    1 AIVDISEWQGPINWDYDTLSKQLDLVIIRVQYGS-----------NYVDLKYKNNIKEFKKRGIPFGVYAFARGTSTADA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137 133 EKAAEVFYNASSPySPSYYWLDVEEKTMSNMNDGVEAFRAKLESLGAKNIGIYVGVYFMEEHSIDTDKFTSVWIPSYGSD 212
Cdd:cd06523   70 KAEARDFYNRANK-KPTFYVLDVEVTSMSDMNAGVQAFISELRRLGAKKVGLYIGHHFYTTFNLAVSKFDAIWIPAYGSN 148

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 565865137 213 SGFYEatpktdldYDIHQYTSKGKIAGFDHDLDINVI 249
Cdd:cd06523  149 PGTYP--------YDLWQYTDSGYLPGISGNVDLNRL 177
Acm COG3757
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis] ...
 53-264 3.75e-35

Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442971  Cd Length: 208  Bit Score: 125.01  E-value: 3.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137  53 PVIDVSGWQrpEEINYDTL-SQNISGAIVRVHSGAqtskendasyvNGVDKAFKTHITEFQKRNVPVAVYAYVagKNVQE 131
Cdd:COG3757   12 HGIDVSHYQ--GDIDWAAVkAAGIDFAYIKATEGT-----------DYVDPKFARNWAGARAAGLPRGAYHFF--RPCSD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137 132 MEKAAEVFYNASSPYSPSY-YWLDVEEKTMSN-----MNDGVEAFRAKLESLGAKNIGIYVGVYFMEEHsIDTDKFTS-- 203
Cdd:COG3757   77 AAAQADNFISTVPRDPGDLpPVLDLEENGYYGlspaqLRAWLKAFLDEVEAHTGRKPIIYTSPSFYNDY-LGNSDFSDyp 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565865137 204 VWIPSYGSDSGfyeatPKTDLDYDIHQYTSKGKIAGFDHDLDINVisaLKNKEETFRKLFL 264
Cdd:COG3757  156 LWIARYGSSPG-----YLPGRNWTFWQYTSSGRVPGISGNVDLNV---FNGSRDELKALAL 208
GH25_LytC-like cd06414
The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves ...
 52-248 7.80e-19

The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.


Pssm-ID: 119376  Cd Length: 191  Bit Score: 81.46  E-value: 7.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137  52 KPVIDVSGWQRpeEINYDTLSQN-ISGAIVRVHSGAQTSKEndasyvngVDKAFKTHITEFQKRNVPVAVYAYVAGKNVQ 130
Cdd:cd06414    1 KKGIDVSEWQG--DIDWKKVKASgVDFAIIRAGYGGYGELQ--------EDKYFEENIKGAKAAGIPVGVYFYSYAVTVA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137 131 EMEKAAEVFYNASSPYSPSY-YWLDVEEKTMSNMN-------DGVEAFRAKLESLGAkNIGIYVGVYFMEeHSIDTDKFT 202
Cdd:cd06414   71 EAREEAEFVLRLIKGYKLSYpVYYDLEDETQLGAGlskdqrtDIANAFCETIEAAGY-YPGIYANLSWLT-NKLDDERLS 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 565865137 203 S--VWIPSYGSDSGFYEatpktdlDYDIHQYTSKGKIAGFDHDLDINV 248
Cdd:cd06414  149 KydVWVAQYGNSPTYPG-------NYGMWQYTSSGSVPGISGNVDLNY 189
GH25_muramidase cd00599
Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan ...
 54-248 4.16e-17

Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.


Pssm-ID: 119373 [Multi-domain]  Cd Length: 186  Bit Score: 77.00  E-value: 4.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137  54 VIDVSGWQRPEEINyDTLSQNISGAIVRvhsgaqtskendASY-VNGVDKAFKTHITEFQKRNVPVAVYAYvaGKNVQEM 132
Cdd:cd00599    2 GIDVSSWQGSIDWN-AVKAAGIDFVFIK------------ATEgTTYVDPKFATNRARARAAGLLVGAYHF--ARPCANA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137 133 EKAAEVFYNASSPYSPSYY-WLDVEEKTMSN----MNDGVEAFRAKLESLGAKNIGIYVGVYFMEEHSIDTDKFTSV-WI 206
Cdd:cd00599   67 EAQADNFVNTVPRDPGSLPlVLDVEDTGGGCsaaaLAAWLNAFLNEVEALTGKKPIIYTSPSFWDDYLASSQLSDYPlWI 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 565865137 207 PSYGSDSGFYEATPKTdldYDIHQYTSKGKIAGFDHDLDINV 248
Cdd:cd00599  147 AHYRGEPPPAPGAWRP---WTLWQYTSSGRVPGISGPVDLNV 185
Glyco_hydro_25 pfam01183
Glycosyl hydrolases family 25;
55-239 9.34e-11

Glycosyl hydrolases family 25;


Pssm-ID: 426105  Cd Length: 180  Bit Score: 59.30  E-value: 9.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137   55 IDVSGWQrpEEINYDTLSQN-ISGAIVRVHSGAqtskendaSYVngvDKAFKTHITEFQKRNVPVAVYAYVAGKNVQEME 133
Cdd:pfam01183   1 IDVSSYQ--GDIDWQKVKASgVSFVFIKATEGT--------DYV---DPYFTTQYANARAAGLKVGAYHFARPCNSSTAA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137  134 KAAEVFY-NASSPYSPSYYW---LDVEEK---TMSNMNDGVEAFRAKLESLGAKNIGIYVGVYFMEEHSIDTD--KFTSV 204
Cdd:pfam01183  68 AQADYFLsNVQGLGLDAGTLppvLDVEVTtglTKAAATSNILRFLDRVKKQTGYKPVIYTGTSFWTNNLLYGQfiADYPL 147

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 565865137  205 WIPSYGSDsgfYEATPKTDLDYDIHQYTSKGKIAG 239
Cdd:pfam01183 148 WIASYAVT---PPKDYPGWTKWTFWQYTSSGSIPG 179
GH25_Lyc-like cd06525
Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by ...
 55-247 7.91e-10

Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.


Pssm-ID: 119385  Cd Length: 184  Bit Score: 56.92  E-value: 7.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137  55 IDVSGWQrpEEINYDTLSQN-ISGAIVRVHSGAqtskendasyvNGVDKAFKTHITEFQKRNVPVAVYAYVAGKNvqEME 133
Cdd:cd06525    3 IDISNWQ--GNINFNAVKDSgVEVVYIKATEGT-----------TFVDSYFNENYNGAKAAGLKVGFYHFLVGTS--NPE 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137 134 KAAEVFYNASSPYS----PsyyWLDVEEKTM---SNMNDGVEAFRAKLESLGAKNIGIYVGVYFMEEHSIDTDKFTSVWI 206
Cdd:cd06525   68 EQAENFYNTIKGKKmdlkP---ALDVEVNFGlskDELNDYVLRFIEEFEKLSGLKVGIYTYTSFINNNLDSRLSSYPLWI 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 565865137 207 PSYG----SDSGFYEAtpktdldYDIHQYTSKGKIAGFDHDLDIN 247
Cdd:cd06525  145 ANYGvsppSSNGIWNS-------WVGFQYSETGRVNGVSGSVDLD 182
GH25_LysA-like cd06417
LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial ...
 54-248 2.80e-04

LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis.


Pssm-ID: 119379  Cd Length: 195  Bit Score: 40.89  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137  54 VIDVSGWQrpEEINYDTLSQNIsgAIVRVHSGAqtskendaSYVNgvdKAFKTHITEFQKRNVPVAVYAYVAGKNVqemE 133
Cdd:cd06417    3 GIDVSSWQ--SRIVTTVVPADF--VIVKATQGT--------GYVN---PSWRSQAAQAIAAGKLLGLYHYANGGNA---I 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137 134 KAAEVFYNASSPY-SPSYYWLDVEEKTMSNM--NDGVEAFRAKLESLGAKNIGIYVGVYFMEEHSIDTDKFTSVWIPSYG 210
Cdd:cd06417   65 AEADYFLNNIKGYvGKAVLVLDWESYQNSAWgnSAWARQWVNRVHELTGVWPMVYVSKSVTRQINWSVRADCGLWVAQYA 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 565865137 211 SD--SGF-YEATPKTDLDYD--IHQYTSKGKIAGFDHDLDINV 248
Cdd:cd06417  145 SNnpTGYqSQAGPWNAAWSGetIHQYTSNGSLNGYNGPLDLNL 187
GH25_muramidase_1 cd06413
Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) ...
 55-248 3.61e-04

Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.


Pssm-ID: 119375  Cd Length: 191  Bit Score: 40.34  E-value: 3.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137  55 IDVSGWQrpEEINYDTLS-QNISGAIVRVHSGAqtskendasyvNGVDKAFKTHITEFQKRNVPVAVYAYV----AGK-- 127
Cdd:cd06413    6 IDVSHHQ--GDIDWARVRaQGVSFAYIKATEGG-----------DHVDKRFAENWRGARAAGLPRGAYHFFtfcrSGAeq 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137 128 ------NVQEMEKA----AEVFYNASSPYSPSYYwlDVEEKtMSNMNDGVEAFRakleslGAKNIgIYVGVYFMEEHSID 197
Cdd:cd06413   73 aanfirNVPKDPGAlppvVDVEWNGNSATCPSAE--EVLAE-LQVFLDALEAHY------GKRPI-IYTTYDFYDDYLKG 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 565865137 198 TDKFTSVWIPSYgsdsgFYEATPKTDLDYDIHQYTSKGKIAGFDHDLDINV 248
Cdd:cd06413  143 EFPDYPLWIRSV-----AGHPRLYEDRPWTFWQYTNRGRVPGIEGDVDLNV 188
GH25_YegX-like cd06524
YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) ...
 55-248 5.76e-04

YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.


Pssm-ID: 119384  Cd Length: 194  Bit Score: 40.02  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137  55 IDVSGWQRP---EEINYDTLSQNISGAIVRVHSGaqtskendasyVNGVDKAFKTHITEFQKRNVPVAVYAYV-AGKNVq 130
Cdd:cd06524    3 IDVSHYQGKidwQKVKAKVKDSPVAFVFIKATEG-----------VDIVDPDFPTNWEGAKEAGIIRGAYHFYrPNSDP- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137 131 emEKAAEVFYNA-----SSPYSPSyywLDVE----EKTMSNMNDGVEAFRAKLES-LGAKNIgIYVGVYFMEEHsIDTDK 200
Cdd:cd06524   71 --KQQADNFLNTvkllgPGDLPPV---LDVEwdgrKSSAKQIQEGVLEWLDAVEKaTGVKPI-IYTNPSFWTDY-LTDSS 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 565865137 201 FTS--VWIPSYGSDSGfyEATPKTDLDYDIHQYTSKGKIAGFDHDLDINV 248
Cdd:cd06524  144 FSEypLWIADYNPRRK--KVPPNESKKWLLWQYSDSGKVPGISGAVDLNV 191
GH25_AtlA-like cd06522
AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell ...
 54-248 6.17e-04

AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain.


Pssm-ID: 119382  Cd Length: 192  Bit Score: 39.66  E-value: 6.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137  54 VIDVSGWQrpEEI---NYDTL-SQNISGAIVRVHSGAqtskendaSYVNGVDKAfktHITEFQKRNVPVAVYAYVAGKNv 129
Cdd:cd06522    3 VVDVSSNN--GIMsvaDYNKLkNYGVKAVIVKLTEGT--------TYRNPYAAS---QIANAKAAGLKVSAYHYAHYTS- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137 130 qEMEKAAEVFYNASSPYS-----PSYYWLDVEEKTMSNMNDG-VEAFRAKLESLGAKNIGIYVGVYFmeehsIDTDKFTS 203
Cdd:cd06522   69 -AADAQAEARYFANTAKSlglskNTVMVADMEDSSSSGNATAnVNAFWQTMKAAGYKNTDVYTSASW-----LNSRADTS 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 565865137 204 ------VWIPSYGSDsgfYEATPKTDLDYDIHQYTSKGKIAGFDHDLDINV 248
Cdd:cd06522  143 tlgakrVWVAQYPYN---PSSNNLWNTNYGAWQWTSQAHFPGRSGGFDVSI 190
GH25_Cpl1-like cd06415
Cpl-1 lysin (also known as Cpl-9 lysozyme / muramidase) is a bacterial cell wall endolysin ...
 54-246 5.29e-03

Cpl-1 lysin (also known as Cpl-9 lysozyme / muramidase) is a bacterial cell wall endolysin encoded by the pneumococcal bacteriophage Cp-1, which cleaves the glycosidic N-acetylmuramoyl-(beta1,4)-N-acetylglucosamine bonds of the pneumococcal glycan chain, thus acting as an enzymatic antimicrobial agent (an enzybiotic) against streptococcal infections. Cpl-1 belongs to the CP family of lysozymes (CPL lysozymes) which includes the Cpl-7 lysin. Cpl-1 has a glycosyl hydrolase family 25 (GH25) catalytic domain with an irregular (beta/alpha)5-beta3 barrel and a C-terminal cell wall-anchoring module formed by six similar choline-binding repeats (ChBr's). The ChBr's facilitate the anchoring of Cpl-1 to the choline-containing teichoic acid of the pneumococcal cell wall. Other members of this domain family have an N-terminal CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain similar to that of the firmicute CHAP lysins and associated with endopeptidase activity. The Cpl-7 lysin is also included here as is LysB of Lactococcus phage, and the Mur lysin of Lactobacillus phage.


Pssm-ID: 119377  Cd Length: 196  Bit Score: 36.99  E-value: 5.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137  54 VIDVSGWQrpeeiNYDTLSQNISG---AIVRVHSGaqtskendasyVNGVDKAFKTHITEFQKRNVPVAVYAYVA-GKNV 129
Cdd:cd06415    3 GVDVASYQ-----GTDLTAYGQAGakfAIVKISEG-----------TNYVNPKASAQVSSAIANGKMTGGYHFARfGGSV 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565865137 130 QEMEKAAEVFYNASSPYSP---SYYWLDVEEKTMSNMN---DGVEAFRAKLESLGAKNIgIYVGVYFMEEHsIDTDKF-- 201
Cdd:cd06415   67 SQAKYEADYFLNSAQQAGLpkgSYLALDYEQGSGNSKAantSAILAFMDTIKDAGYKPM-LYSYKPLLLNN-VDYSQIia 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 565865137 202 ---TSVWIPSYGSdsgfYEATPKTDLDY-------DIHQYTSKGKIAGFDHDLDI 246
Cdd:cd06415  145 kypNSLWVAAYPT----YGVQDTPDFNYfpsmdgvAIWQFTSNWRGGGVDGNITL 195
 
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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