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Conserved domains on  [gi|489156023|ref|WP_003065704|]
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MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Streptococcus]

Protein Classification

N-acetylmuramoyl-L-alanine amidase( domain architecture ID 10652594)

N-acetylmuramoyl-L-alanine amidase hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides; similar to Lactococcus phage r1t N-acetylmuramoyl-L-alanine amidase (R1tp49) and Listeria virus A511 endolysin PLY511, a probable N-acetylmuramoyl-L-alanine amidase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CwlA super family cl46750
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
167-328 2.09e-22

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


The actual alignment was detected with superfamily member COG5632:

Pssm-ID: 481090  Cd Length: 177  Bit Score: 91.96  E-value: 2.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156023 167 KPLGVIIHDTGVDNSTIESEVNYMVQNYDKegVFVHSFIDSDTILRIADEGYKAQGAG---ANANPYYIQFELTHEDSQK 243
Cdd:COG5632   23 KPKGIVIHNTANPGATAENHANYFNNNNRS--ASWHYFVDDKEIIQHIPLNENAWHAGdgtGPGNRRSIGIEICENKDGD 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156023 244 gFAEQLANAAYYTAYMLKKYDLPVTlgqedgegTIWTHEMVSLylggtdHVDPTDYWTEtandyfgTDYDIEDFVELVQA 323
Cdd:COG5632  101 -FAKAYENAAELIAYLMKKYGIPID--------NVVRHYDWSG------KNCPHGLLAN-------GGYRWDQFKADVKS 158


                 ....*
gi 489156023 324 YYNAL 328
Cdd:COG5632  159 ALNGL 163
 
Name Accession Description Interval E-value
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
167-328 2.09e-22

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


Pssm-ID: 444359  Cd Length: 177  Bit Score: 91.96  E-value: 2.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156023 167 KPLGVIIHDTGVDNSTIESEVNYMVQNYDKegVFVHSFIDSDTILRIADEGYKAQGAG---ANANPYYIQFELTHEDSQK 243
Cdd:COG5632   23 KPKGIVIHNTANPGATAENHANYFNNNNRS--ASWHYFVDDKEIIQHIPLNENAWHAGdgtGPGNRRSIGIEICENKDGD 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156023 244 gFAEQLANAAYYTAYMLKKYDLPVTlgqedgegTIWTHEMVSLylggtdHVDPTDYWTEtandyfgTDYDIEDFVELVQA 323
Cdd:COG5632  101 -FAKAYENAAELIAYLMKKYGIPID--------NVVRHYDWSG------KNCPHGLLAN-------GGYRWDQFKADVKS 158


                 ....*
gi 489156023 324 YYNAL 328
Cdd:COG5632  159 ALNGL 163
Ami_2 smart00644
Ami_2 domain;
166-296 4.89e-20

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 84.33  E-value: 4.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156023   166 GKPLGVIIHDTGVDNSTIESEVNYMvQNYDKEGVFVHSFIDSD-TILRIADEGYKAQGAG----ANANPYYIQFEL--TH 238
Cdd:smart00644   1 PPPRGIVIHHTANSNASCANEARYM-QNNHMNDIGYHFLVGGDgRVYQGVGWNYVAWHAGgahtPGYNDISIGIEFigSF 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 489156023   239 EDSQKGFAEQLANAAYYTAYMLKKYDLPVtlgqeDGEGTIWTHEMVSlylggtDHVDP 296
Cdd:smart00644  80 DSDDEPFAEALYAALDLLAKLLKGAGLPP-----DGRYRIVGHRDVA------PTEDP 126
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 167-299 6.31e-20

Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.


Pssm-ID: 133475 [Multi-domain]  Cd Length: 126  Bit Score: 83.88  E-value: 6.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156023 167 KPLGVIIHDTGVDNS-TIESEVNYMvQNYDKEG---VFVHSFIDSD-TILRIADEGYKAQGAGANANPYYIQFELTHEDS 241
Cdd:cd06583    1 PVKYVVIHHTANPNCyTAAAAVRYL-QNYHMRGwsdISYHFLVGGDgRIYQGRGWNYVGWHAGGNYNSYSIGIELIGNFD 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489156023 242 QKG-FAEQLANAAYYTAYMLKKYDLPvtlgqedGEGTIWTHEMVSLYlggtdHVDPTDY 299
Cdd:cd06583   80 GGPpTAAQLEALAELLAYLVKRYGIP-------PDYRIVGHRDVSPG-----TECPGDA 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 167-296 1.40e-10

N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.


Pssm-ID: 460236 [Multi-domain]  Cd Length: 122  Bit Score: 58.14  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156023  167 KPLGVIIHDTGVDNSTiESEVNYMVQNYDK-EGVFVHSFIDSD-TILRIADEGYKAQGAGA-NANPYYIQFELTHEDSQK 243
Cdd:pfam01510   1 PIRYIVIHHTAGPSFA-GALLPYAACIARGwSDVSYHYLIDRDgTIYQLVPENGRAWHAGNgGGNDRSIGIELEGNFGGD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489156023  244 GF-AEQLANAAYYTAYMLKKYDLPVTlgqedgeGTIWTHEMVslylggTDHVDP 296
Cdd:pfam01510  80 PPtDAQYEALARLLADLCKRYGIPPD-------RRIVGHRDV------GRKTDP 120
 
Name Accession Description Interval E-value
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
167-328 2.09e-22

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


Pssm-ID: 444359  Cd Length: 177  Bit Score: 91.96  E-value: 2.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156023 167 KPLGVIIHDTGVDNSTIESEVNYMVQNYDKegVFVHSFIDSDTILRIADEGYKAQGAG---ANANPYYIQFELTHEDSQK 243
Cdd:COG5632   23 KPKGIVIHNTANPGATAENHANYFNNNNRS--ASWHYFVDDKEIIQHIPLNENAWHAGdgtGPGNRRSIGIEICENKDGD 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156023 244 gFAEQLANAAYYTAYMLKKYDLPVTlgqedgegTIWTHEMVSLylggtdHVDPTDYWTEtandyfgTDYDIEDFVELVQA 323
Cdd:COG5632  101 -FAKAYENAAELIAYLMKKYGIPID--------NVVRHYDWSG------KNCPHGLLAN-------GGYRWDQFKADVKS 158


                 ....*
gi 489156023 324 YYNAL 328
Cdd:COG5632  159 ALNGL 163
Ami_2 smart00644
Ami_2 domain;
166-296 4.89e-20

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 84.33  E-value: 4.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156023   166 GKPLGVIIHDTGVDNSTIESEVNYMvQNYDKEGVFVHSFIDSD-TILRIADEGYKAQGAG----ANANPYYIQFEL--TH 238
Cdd:smart00644   1 PPPRGIVIHHTANSNASCANEARYM-QNNHMNDIGYHFLVGGDgRVYQGVGWNYVAWHAGgahtPGYNDISIGIEFigSF 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 489156023   239 EDSQKGFAEQLANAAYYTAYMLKKYDLPVtlgqeDGEGTIWTHEMVSlylggtDHVDP 296
Cdd:smart00644  80 DSDDEPFAEALYAALDLLAKLLKGAGLPP-----DGRYRIVGHRDVA------PTEDP 126
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 167-299 6.31e-20

Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.


Pssm-ID: 133475 [Multi-domain]  Cd Length: 126  Bit Score: 83.88  E-value: 6.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156023 167 KPLGVIIHDTGVDNS-TIESEVNYMvQNYDKEG---VFVHSFIDSD-TILRIADEGYKAQGAGANANPYYIQFELTHEDS 241
Cdd:cd06583    1 PVKYVVIHHTANPNCyTAAAAVRYL-QNYHMRGwsdISYHFLVGGDgRIYQGRGWNYVGWHAGGNYNSYSIGIELIGNFD 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489156023 242 QKG-FAEQLANAAYYTAYMLKKYDLPvtlgqedGEGTIWTHEMVSLYlggtdHVDPTDY 299
Cdd:cd06583   80 GGPpTAAQLEALAELLAYLVKRYGIP-------PDYRIVGHRDVSPG-----TECPGDA 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 167-296 1.40e-10

N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.


Pssm-ID: 460236 [Multi-domain]  Cd Length: 122  Bit Score: 58.14  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156023  167 KPLGVIIHDTGVDNSTiESEVNYMVQNYDK-EGVFVHSFIDSD-TILRIADEGYKAQGAGA-NANPYYIQFELTHEDSQK 243
Cdd:pfam01510   1 PIRYIVIHHTAGPSFA-GALLPYAACIARGwSDVSYHYLIDRDgTIYQLVPENGRAWHAGNgGGNDRSIGIELEGNFGGD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489156023  244 GF-AEQLANAAYYTAYMLKKYDLPVTlgqedgeGTIWTHEMVslylggTDHVDP 296
Cdd:pfam01510  80 PPtDAQYEALARLLADLCKRYGIPPD-------RRIVGHRDV------GRKTDP 120
 
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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