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Conserved domains on  [gi|497575260|ref|WP_009889444|]
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N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile]

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, ...
2-174 2.77e-29

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: 108.78  E-value: 2.77e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575260   2 KICITVGHSILKSGAcTSADGVvNEYQYNKSLAPVLADTFRKEGHKadVIICPEKqfkTKAEEKTYKIPRVNSGGYDLLI 81
Cdd:cd02696    1 TIVIDPGHGGKDPGA-VGNDGL-KEKDINLAIALKLAKLLEAAGAK--VVLTRDD---DTFVSLSERVAIANRAGADLFI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575260  82 ELHLNAS-DGQGKGSEVLYYSN---KGLEYATRICNKLG--TVFRNRRAKlDKGLYILNSSNPTAVLIESFFCDNKEDYE 155
Cdd:cd02696   74 SIHANAApNSSARGAEVYYYSGsseESKRLAEAIQKELVkaLGLRNRGVK-QANLYVLRNTKMPAVLVELGFISNPEDAK 152
                        170       180
                 ....*....|....*....|
gi 497575260 156 K-AKKLGHEGIAKLIVEGVL 174
Cdd:cd02696  153 LlNSPEYQDKIAEAIAEGIL 172
 
Name Accession Description Interval E-value
MurNAc-LAA cd02696
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ...
2-174 2.77e-29

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: 108.78  E-value: 2.77e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575260   2 KICITVGHSILKSGAcTSADGVvNEYQYNKSLAPVLADTFRKEGHKadVIICPEKqfkTKAEEKTYKIPRVNSGGYDLLI 81
Cdd:cd02696    1 TIVIDPGHGGKDPGA-VGNDGL-KEKDINLAIALKLAKLLEAAGAK--VVLTRDD---DTFVSLSERVAIANRAGADLFI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575260  82 ELHLNAS-DGQGKGSEVLYYSN---KGLEYATRICNKLG--TVFRNRRAKlDKGLYILNSSNPTAVLIESFFCDNKEDYE 155
Cdd:cd02696   74 SIHANAApNSSARGAEVYYYSGsseESKRLAEAIQKELVkaLGLRNRGVK-QANLYVLRNTKMPAVLVELGFISNPEDAK 152
                        170       180
                 ....*....|....*....|
gi 497575260 156 K-AKKLGHEGIAKLIVEGVL 174
Cdd:cd02696  153 LlNSPEYQDKIAEAIAEGIL 172
Amidase_3 pfam01520
N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between ...
3-175 7.60e-19

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: 81.52  E-value: 7.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575260    3 ICITVGHSILKSGACtsADGVVNEYQYNKSLAPVLADTFRKEGHKadVIICPEKQFKTKAEEKTYKIprvNSGGYDLLIE 82
Cdd:pfam01520   1 IVIDPGHGGKDPGAV--GPNGILEKDINLKIALKLRKLLEAKGAE--VILTRDSDETVSLEERANIA---NSNGADLFVS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575260   83 LHLNASDGQG-KGSEVLY-----YSNKGLEYATRICNKLGTV--FRNRRAKLDkGLYILNSSNPTAVLIESFFCDNKEDY 154
Cdd:pfam01520  74 IHANAFPNSSaSGVEVYYlakrkSSAESKRLAQSIQKELVKVlgLKNRGVKPA-NLYVLRNTKMPAVLVELGFISNPEDA 152
                         170       180
                  ....*....|....*....|..
gi 497575260  155 EKAKKL-GHEGIAKLIVEGVLN 175
Cdd:pfam01520 153 KLLNSPaYQQKIAEAIADGILN 174
 
Name Accession Description Interval E-value
MurNAc-LAA cd02696
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ...
2-174 2.77e-29

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: 108.78  E-value: 2.77e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575260   2 KICITVGHSILKSGAcTSADGVvNEYQYNKSLAPVLADTFRKEGHKadVIICPEKqfkTKAEEKTYKIPRVNSGGYDLLI 81
Cdd:cd02696    1 TIVIDPGHGGKDPGA-VGNDGL-KEKDINLAIALKLAKLLEAAGAK--VVLTRDD---DTFVSLSERVAIANRAGADLFI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575260  82 ELHLNAS-DGQGKGSEVLYYSN---KGLEYATRICNKLG--TVFRNRRAKlDKGLYILNSSNPTAVLIESFFCDNKEDYE 155
Cdd:cd02696   74 SIHANAApNSSARGAEVYYYSGsseESKRLAEAIQKELVkaLGLRNRGVK-QANLYVLRNTKMPAVLVELGFISNPEDAK 152
                        170       180
                 ....*....|....*....|
gi 497575260 156 K-AKKLGHEGIAKLIVEGVL 174
Cdd:cd02696  153 LlNSPEYQDKIAEAIAEGIL 172
Amidase_3 pfam01520
N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between ...
3-175 7.60e-19

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: 81.52  E-value: 7.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575260    3 ICITVGHSILKSGACtsADGVVNEYQYNKSLAPVLADTFRKEGHKadVIICPEKQFKTKAEEKTYKIprvNSGGYDLLIE 82
Cdd:pfam01520   1 IVIDPGHGGKDPGAV--GPNGILEKDINLKIALKLRKLLEAKGAE--VILTRDSDETVSLEERANIA---NSNGADLFVS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575260   83 LHLNASDGQG-KGSEVLY-----YSNKGLEYATRICNKLGTV--FRNRRAKLDkGLYILNSSNPTAVLIESFFCDNKEDY 154
Cdd:pfam01520  74 IHANAFPNSSaSGVEVYYlakrkSSAESKRLAQSIQKELVKVlgLKNRGVKPA-NLYVLRNTKMPAVLVELGFISNPEDA 152
                         170       180
                  ....*....|....*....|..
gi 497575260  155 EKAKKL-GHEGIAKLIVEGVLN 175
Cdd:pfam01520 153 KLLNSPaYQQKIAEAIADGILN 174
 
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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