1JWQ,1XOV,3CZX


Conserved Protein Domain Family
MurNAc-LAA

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cd02696: MurNAc-LAA 
Click on image for an interactive view with Cn3D
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.
Statistics
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PSSM-Id: 119407
View PSSM: cd02696
Aligned: 522 rows
Threshold Bit Score: 64.099
Threshold Setting Gi: 162449166
Created: 13-Dec-2003
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
active sitemetal binding
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Structure:1XOV_A: Listeria phage PSA Endolysin (Plypsa) bound to Zn2+ and a dipeptide (Glu-Lys); contacts at 3.5A; toggle side chains to view bound Zn2+
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1               #               #                                                        
1JWQ_A         3 VVVIDAGHGAkDSGAVGisrkNYEKTFNLAMALKVESILKqnpkLEVVLTRsddt------fleLKQRVKVAenlkaNVF 76  Paenibacillus p...
1XOV_A         4 NYSMSRGHSDkCVGAEDi---LSEIKEAEKVLNAASDELKre-gHNVKTFIdrtst---tqsanLNKIVNWHnanpaDVH 76  Listeria phage PSA
YP_001642794   5 EVIIDAGHGDhDSGAVGn--gLLEKERALKLSLYLRDELVns-gVSVAMTRasdt------flsLSARARFAndrgaKVF 75  Bacillus weihen...
AAP09173       2 KLVIDAGHGGyDSGAVGn--gLVEKNLTLQIARRVRDILTvnypITIKMTRdsdv------fisLSERANIAnafsaDYF 73  Bacillus cereus...
ZP_02329031    3 KLCLDFGHGGkDSGAVGh--gMKEKDIVLDVGLRTHKILTna-gIDVLLTRsddt------fvgLSDRARKAnswgaDLF 73  Paenibacillus l...
YP_001113616   5 IICLDPGHGGqDPGALGn--gLQEKDITLEIAKKIIQRLAay-dVTVKSTRdsdt------fvsLSQRAAYAnnvnaDYF 75  Desulfotomaculu...
YP_001210988   3 KLVLDPGHGGiDAGAVGn--gIKEKDLNLELCRRIAGKLEgy-dVEVTLTRtada------dvdVYRRCELAnslkaDYF 73  Pelotomaculum t...
YP_001717994  16 AGIYRSGHGGeEPDAVSg--dLLEKHLNLQITLELNTALRcnylVDTVLTRtvdt------tvsLYDRVRRAnaacaDLF 87  Candidatus Desu...
ABS44973       3 KIVLDPGHGGeDPGAISlengLREKDITLKIALYAKEFLLknslARVKLTRendv------fikLRERSKIAkrfkaDFF 76  Bacillus megate...
YP_001113924   3 RIVLDPGHGGaDPGAVGn--gLLEKQVTWMLANKVKEKLKrm-kAEVIIVQpscgnprstkddeLYLPPRDAnrlgaDFY 79  Desulfotomaculu...
Feature 1           #                                                                        #   
1JWQ_A        77 VSIHANSsgssasNGTETYYQrs-----aSKAFANVMHKYFAPATg-----LTDRGIRYGn-FHVIREttmPAVLLEVGY 145 Paenibacillus p...
1XOV_A        77 ISVHLNAgk---gTGVEVWYYagd---ekGRKLAVEISAKMAKALg-----LPNRGAKATkdLRFLNStkgTAVLLEVCF 145 Listeria phage PSA
YP_001642794  76 ISNHLNSsdnpsaLGYETFVFnrn--dknTNRLQDLIHTEGMKVLg-----FRDRGMKTAd-YAVLREthmPAVLTENGF 147 Bacillus weihen...
AAP09173      74 ISFHINSgg---gTGFESYIYnalsnsstAYAKQQKMHTAVNPVLtk--ygLRDRGAKKEn-YAVLREtamDAILTETAF 147 Bacillus cereus...
ZP_02329031   74 VSLHNNSgg---gYGFESFTYlkt--dskTDQFRAAVHSEVAPLF------RRDRGMKQAn-LAVLREtrmPACLLELGF 141 Paenibacillus l...
YP_001113616  76 VSIHINAgg---gTGFESFIYngev-sstTIKTRQVLHDTIMADMqk--yyMIDRGKKAAn-FAVIREtnmPAILTENLF 148 Desulfotomaculu...
YP_001210988  74 CSVHANSgg---gTGFESYVYtha--geiTESLRGVVHEKVAAYFks--agFPDRGKKRAn-FVVLREtgmPAVLLENLF 145 Pelotomaculum t...
YP_001717994  88 VSVHVNAgg---gTGFESFIHpqa--pekTRGIRRAIHTEAMSFLri--hsVTDRGMKTAg-FYVLRAtsmPAVLLETLF 159 Candidatus Desu...
ABS44973      77 VSIHVNAgg---gTGFESYIYlet--kdlTLAFQQSLHNEIINTLhhqhesIPNRGLKRAn-YAVLREtsmPAVLTENLF 150 Bacillus megate...
YP_001113924  80 LSIHVNAgg---gTGFESFVHqnsq-gkdTDKLRNVLHRQVMAYLak--ygIVDRGKKYAn-FAVLRLtnmPAVLIECLF 152 Desulfotomaculu...
Feature 1                                    
1JWQ_A       146 LSNAKEEATLFdedfQNRVAQGIADGIT 173 Paenibacillus polymyxa
1XOV_A       146 VDRKEDANAIHksgmYDKLGIAIAEGLT 173 Listeria phage PSA
YP_001642794 148 ISNASEMAHIRkddvLRKLAQGYARAIC 175 Bacillus weihenstephanensis KBAB4
AAP09173     148 IDTAFDANLLKnpqfIEDLSQAYANGIA 175 Bacillus cereus ATCC 14579
ZP_02329031  142 IDNAEDAADLArddfRDKLAVAIANGIL 169 Paenibacillus larvae subsp. larvae BRL-230010
YP_001113616 149 IDNPKDASLLKntdfINDLSTAITHGLV 176 Desulfotomaculum reducens MI-1
YP_001210988 146 LDSPRDAVRLKdssfLDGLAAAVAGGLV 173 Pelotomaculum thermopropionicum SI
YP_001717994 160 IDHPVDAQRLRdrvfIARYAHAVARGVG 187 Candidatus Desulforudis audaxviator MP104C
ABS44973     151 IERDFELLKDEm--fLKDLGEAHARGIA 176 Bacillus megaterium
YP_001113924 153 IDNAKDAVLLKdqsfIDGLANEIAYGLI 180 Desulfotomaculum reducens MI-1

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