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: 17-Jan-2013
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:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1               #               #                                                        
1JWQ_A         3 VVVIDAGHGAkDSGAVGisrkNYEKTFNLAMALKVESILKqnpkLEVVLTRsddt------fleLKQRVKVAenlkaNVF 76
1XOV_A         4 NYSMSRGHSDkCVGAEDi---LSEIKEAEKVLNAASDELKre-gHNVKTFIdrtst---tqsanLNKIVNWHnanpaDVH 76
gi 163937908   5 EVIIDAGHGDhDSGAVGn--gLLEKERALKLSLYLRDELVns-gVSVAMTRasdt------flsLSARARFAndrgaKVF 75
gi 29895892    2 KLVIDAGHGGyDSGAVGn--gLVEKNLTLQIARRVRDILTvnypITIKMTRdsdv------fisLSERANIAnafsaDYF 73
gi 167463942   3 KLCLDFGHGGkDSGAVGh--gMKEKDIVLDVGLRTHKILTna-gIDVLLTRsddt------fvgLSDRARKAnswgaDLF 73
gi 134300120   5 IICLDPGHGGqDPGALGn--gLQEKDITLEIAKKIIQRLAay-dVTVKSTRdsdt------fvsLSQRAAYAnnvnaDYF 75
gi 147676773   3 KLVLDPGHGGiDAGAVGn--gIKEKDLNLELCRRIAGKLEgy-dVEVTLTRtada------dvdVYRRCELAnslkaDYF 73
gi 169832012  16 AGIYRSGHGGeEPDAVSg--dLLEKHLNLQITLELNTALRcnylVDTVLTRtvdt------tvsLYDRVRRAnaacaDLF 87
gi 152941017   3 KIVLDPGHGGeDPGAISlengLREKDITLKIALYAKEFLLknslARVKLTRendv------fikLRERSKIAkrfkaDFF 76
gi 134300428   3 RIVLDPGHGGaDPGAVGn--gLLEKQVTWMLANKVKEKLKrm-kAEVIIVQpscgnprstkddeLYLPPRDAnrlgaDFY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1           #                                                                        #   
1JWQ_A        77 VSIHANSsgssasNGTETYYQrs-----aSKAFANVMHKYFAPATg-----LTDRGIRYGn-FHVIREttmPAVLLEVGY 145
1XOV_A        77 ISVHLNAgk---gTGVEVWYYagd---ekGRKLAVEISAKMAKALg-----LPNRGAKATkdLRFLNStkgTAVLLEVCF 145
gi 163937908  76 ISNHLNSsdnpsaLGYETFVFnrn--dknTNRLQDLIHTEGMKVLg-----FRDRGMKTAd-YAVLREthmPAVLTENGF 147
gi 29895892   74 ISFHINSgg---gTGFESYIYnalsnsstAYAKQQKMHTAVNPVLtk--ygLRDRGAKKEn-YAVLREtamDAILTETAF 147
gi 167463942  74 VSLHNNSgg---gYGFESFTYlkt--dskTDQFRAAVHSEVAPLF------RRDRGMKQAn-LAVLREtrmPACLLELGF 141
gi 134300120  76 VSIHINAgg---gTGFESFIYngev-sstTIKTRQVLHDTIMADMqk--yyMIDRGKKAAn-FAVIREtnmPAILTENLF 148
gi 147676773  74 CSVHANSgg---gTGFESYVYtha--geiTESLRGVVHEKVAAYFks--agFPDRGKKRAn-FVVLREtgmPAVLLENLF 145
gi 169832012  88 VSVHVNAgg---gTGFESFIHpqa--pekTRGIRRAIHTEAMSFLri--hsVTDRGMKTAg-FYVLRAtsmPAVLLETLF 159
gi 152941017  77 VSIHVNAgg---gTGFESYIYlet--kdlTLAFQQSLHNEIINTLhhqhesIPNRGLKRAn-YAVLREtsmPAVLTENLF 150
gi 134300428  80 LSIHVNAgg---gTGFESFVHqnsq-gkdTDKLRNVLHRQVMAYLak--ygIVDRGKKYAn-FAVLRLtnmPAVLIECLF 152
                        170       180
                 ....*....|....*....|....*...
Feature 1                                    
1JWQ_A       146 LSNAKEEATLFdedfQNRVAQGIADGIT 173
1XOV_A       146 VDRKEDANAIHksgmYDKLGIAIAEGLT 173
gi 163937908 148 ISNASEMAHIRkddvLRKLAQGYARAIC 175
gi 29895892  148 IDTAFDANLLKnpqfIEDLSQAYANGIA 175
gi 167463942 142 IDNAEDAADLArddfRDKLAVAIANGIL 169
gi 134300120 149 IDNPKDASLLKntdfINDLSTAITHGLV 176
gi 147676773 146 LDSPRDAVRLKdssfLDGLAAAVAGGLV 173
gi 169832012 160 IDHPVDAQRLRdrvfIARYAHAVARGVG 187
gi 152941017 151 IERDFELLKDEm--fLKDLGEAHARGIA 176
gi 134300428 153 IDNAKDAVLLKdqsfIDGLANEIAYGLI 180

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