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Conserved domains on  [gi|2057943280|tpg|DAT37945|]
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MAG TPA: Cell wall hydrolase autolysin [Bacteriophage sp.]

Protein Classification

N-acetylmuramoyl-L-alanine amidase( domain architecture ID 10119458)

N-acetylmuramoyl-L-alanine amidase hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides

CATH:  3.40.630.40
EC:  3.5.1.28
Gene Ontology:  GO:0008745|GO:0046872
PubMed:  18266855
SCOP:  4001130

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MurNAc-LAA cd02696
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ...
 3-172 2.34e-32

N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.


:

Pssm-ID: 119407 [Multi-domain]  Cd Length: 172  Bit Score: 115.72  E-value: 2.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057943280   3 INVHAGHnphGKIACGAVGL--ISESLENRRVKDLVVDELRRMGHTVYDCTVEDGTSqtnVLTRIINKCNMHSVDLDVSI 80
Cdd:cd02696     2 IVIDPGH---GGKDPGAVGNdgLKEKDINLAIALKLAKLLEAAGAKVVLTRDDDTFV---SLSERVAIANRAGADLFISI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057943280  81 HFNSASSVGANGTEVYIYDESSKAS-TYALNVLNAICS-LGFRNRGVKVNkKLGFLRRTKAPAMLIECCFVNSQRDIALY 158
Cdd:cd02696    76 HANAAPNSSARGAEVYYYSGSSEESkRLAEAIQKELVKaLGLRNRGVKQA-NLYVLRNTKMPAVLVELGFISNPEDAKLL 154

                         170
                  ....*....|....*...
gi 2057943280 159 N----PHEVAAAIVYGIT 172
Cdd:cd02696   155 NspeyQDKIAEAIAEGIL 172
 
Name Accession Description Interval E-value
MurNAc-LAA cd02696
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ...
 3-172 2.34e-32

N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.


Pssm-ID: 119407 [Multi-domain]  Cd Length: 172  Bit Score: 115.72  E-value: 2.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057943280   3 INVHAGHnphGKIACGAVGL--ISESLENRRVKDLVVDELRRMGHTVYDCTVEDGTSqtnVLTRIINKCNMHSVDLDVSI 80
Cdd:cd02696     2 IVIDPGH---GGKDPGAVGNdgLKEKDINLAIALKLAKLLEAAGAKVVLTRDDDTFV---SLSERVAIANRAGADLFISI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057943280  81 HFNSASSVGANGTEVYIYDESSKAS-TYALNVLNAICS-LGFRNRGVKVNkKLGFLRRTKAPAMLIECCFVNSQRDIALY 158
Cdd:cd02696    76 HANAAPNSSARGAEVYYYSGSSEESkRLAEAIQKELVKaLGLRNRGVKQA-NLYVLRNTKMPAVLVELGFISNPEDAKLL 154

                         170
                  ....*....|....*...
gi 2057943280 159 N----PHEVAAAIVYGIT 172
Cdd:cd02696   155 NspeyQDKIAEAIAEGIL 172
AmiC COG0860
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];
12-171 9.43e-25

N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440621  Cd Length: 204  Bit Score: 96.87  E-value: 9.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057943280  12 HGKIACGAVGL--ISESLENRRVKDLVVDELRRMGHTVYDcTVEDGTSQTnvLTRIINKCNMHSVDLDVSIHFNSASSVG 89
Cdd:COG0860    33 HGGKDPGAIGPngLKEKDVNLDIALRLAELLEAPGAKVVL-TRDDDTFVS--LSERVAIANKAKADLFISIHANAAPNPS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057943280  90 ANGTEVYIYDESS---KASTYALNVLNAICS-LGFRNRGVKvNKKLGFLRRTKAPAMLIECCFVNSQRDIALYN----PH 161
Cdd:COG0860   110 ARGAEVYYYSGSQtsaESKKLAEAIQKELVKaLGLKDRGVK-QANFYVLRETDMPAVLVELGFISNPEDEALLKspayQQ 188

                         170
                  ....*....|
gi 2057943280 162 EVAAAIVYGI 171
Cdd:COG0860   189 KLAEAIADGI 198
Amidase_3 pfam01520
N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between ...
 7-172 3.79e-24

N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.


Pssm-ID: 426303  Cd Length: 174  Bit Score: 94.62  E-value: 3.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057943280   7 AGHNPHGKIACGAVGlISESLENRRVKDLVVDELRRMGHTVYDCtveDGTSQTNVLTRIINKCNMHSVDLDVSIHFNSAS 86
Cdd:pfam01520   5 PGHGGKDPGAVGPNG-ILEKDINLKIALKLRKLLEAKGAEVILT---RDSDETVSLEERANIANSNGADLFVSIHANAFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057943280  87 SVGANGTEVYI--YDESSKAS-TYALNVLNAICS-LGFRNRGVKVNKkLGFLRRTKAPAMLIECCFVNSQRDIALYN--- 159
Cdd:pfam01520  81 NSSASGVEVYYlaKRKSSAESkRLAQSIQKELVKvLGLKNRGVKPAN-LYVLRNTKMPAVLVELGFISNPEDAKLLNspa 159

                         170
                  ....*....|....
gi 2057943280 160 -PHEVAAAIVYGIT 172
Cdd:pfam01520 160 yQQKIAEAIADGIL 173
Ami_3 smart00646
Ami_3 domain;
63-171 1.21e-12

Ami_3 domain;


Pssm-ID: 214762  Cd Length: 113  Bit Score: 62.31  E-value: 1.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057943280   63 TRIINKCNmhsVDLDVSIHFNSASSVGANGTEVYIYDeSSKASTYALNVLNAICS-----LGFRNRGVKVNkKLGFLRRT 137
Cdd:smart00646   1 ANIANAAK---ADLFVSIHANAGGASAARGFEVYYYS-DKGAIRESRALASIIQKslrknTGLRDRGVKEA-NFAVLRET 75

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2057943280  138 KAPAMLIECCFV-NSQRDIALYNPH---EVAAAIVYGI 171
Cdd:smart00646  76 NMPAVLVELGFItNPSDARKLKSAAyqqKLARAIAKGI 113
 
Name Accession Description Interval E-value
MurNAc-LAA cd02696
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ...
 3-172 2.34e-32

N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.


Pssm-ID: 119407 [Multi-domain]  Cd Length: 172  Bit Score: 115.72  E-value: 2.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057943280   3 INVHAGHnphGKIACGAVGL--ISESLENRRVKDLVVDELRRMGHTVYDCTVEDGTSqtnVLTRIINKCNMHSVDLDVSI 80
Cdd:cd02696     2 IVIDPGH---GGKDPGAVGNdgLKEKDINLAIALKLAKLLEAAGAKVVLTRDDDTFV---SLSERVAIANRAGADLFISI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057943280  81 HFNSASSVGANGTEVYIYDESSKAS-TYALNVLNAICS-LGFRNRGVKVNkKLGFLRRTKAPAMLIECCFVNSQRDIALY 158
Cdd:cd02696    76 HANAAPNSSARGAEVYYYSGSSEESkRLAEAIQKELVKaLGLRNRGVKQA-NLYVLRNTKMPAVLVELGFISNPEDAKLL 154

                         170
                  ....*....|....*...
gi 2057943280 159 N----PHEVAAAIVYGIT 172
Cdd:cd02696   155 NspeyQDKIAEAIAEGIL 172
AmiC COG0860
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];
12-171 9.43e-25

N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440621  Cd Length: 204  Bit Score: 96.87  E-value: 9.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057943280  12 HGKIACGAVGL--ISESLENRRVKDLVVDELRRMGHTVYDcTVEDGTSQTnvLTRIINKCNMHSVDLDVSIHFNSASSVG 89
Cdd:COG0860    33 HGGKDPGAIGPngLKEKDVNLDIALRLAELLEAPGAKVVL-TRDDDTFVS--LSERVAIANKAKADLFISIHANAAPNPS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057943280  90 ANGTEVYIYDESS---KASTYALNVLNAICS-LGFRNRGVKvNKKLGFLRRTKAPAMLIECCFVNSQRDIALYN----PH 161
Cdd:COG0860   110 ARGAEVYYYSGSQtsaESKKLAEAIQKELVKaLGLKDRGVK-QANFYVLRETDMPAVLVELGFISNPEDEALLKspayQQ 188

                         170
                  ....*....|
gi 2057943280 162 EVAAAIVYGI 171
Cdd:COG0860   189 KLAEAIADGI 198
Amidase_3 pfam01520
N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between ...
 7-172 3.79e-24

N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.


Pssm-ID: 426303  Cd Length: 174  Bit Score: 94.62  E-value: 3.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057943280   7 AGHNPHGKIACGAVGlISESLENRRVKDLVVDELRRMGHTVYDCtveDGTSQTNVLTRIINKCNMHSVDLDVSIHFNSAS 86
Cdd:pfam01520   5 PGHGGKDPGAVGPNG-ILEKDINLKIALKLRKLLEAKGAEVILT---RDSDETVSLEERANIANSNGADLFVSIHANAFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057943280  87 SVGANGTEVYI--YDESSKAS-TYALNVLNAICS-LGFRNRGVKVNKkLGFLRRTKAPAMLIECCFVNSQRDIALYN--- 159
Cdd:pfam01520  81 NSSASGVEVYYlaKRKSSAESkRLAQSIQKELVKvLGLKNRGVKPAN-LYVLRNTKMPAVLVELGFISNPEDAKLLNspa 159

                         170
                  ....*....|....
gi 2057943280 160 -PHEVAAAIVYGIT 172
Cdd:pfam01520 160 yQQKIAEAIADGIL 173
Ami_3 smart00646
Ami_3 domain;
63-171 1.21e-12

Ami_3 domain;


Pssm-ID: 214762  Cd Length: 113  Bit Score: 62.31  E-value: 1.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057943280   63 TRIINKCNmhsVDLDVSIHFNSASSVGANGTEVYIYDeSSKASTYALNVLNAICS-----LGFRNRGVKVNkKLGFLRRT 137
Cdd:smart00646   1 ANIANAAK---ADLFVSIHANAGGASAARGFEVYYYS-DKGAIRESRALASIIQKslrknTGLRDRGVKEA-NFAVLRET 75

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2057943280  138 KAPAMLIECCFV-NSQRDIALYNPH---EVAAAIVYGI 171
Cdd:smart00646  76 NMPAVLVELGFItNPSDARKLKSAAyqqKLARAIAKGI 113
 
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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