1HI9


Conserved Protein Domain Family
DAP_dppA

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cd00281: DAP_dppA 
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Peptidase M55, D-aminopeptidase dipeptide-binding protein family
M55 Peptidase, D-Aminopeptidase dipeptide-binding protein (dppA; DAP dppA; EC 3.4.11.-) domain: Peptide transport systems are found in many bacterial species and generally function to accumulate intact peptides in the cell, where they are hydrolyzed. The dipeptide-binding protein (dppA) of Bacillus subtilis belongs to the dipeptide ABC transport (dpp) operon expressed early during sporulation. It is a binuclear zinc-dependent, D-specific aminopeptidase. The biologically active enzyme is a homodecamer with active sites buried in its channel. These self-compartmentalizing proteases are characterized by a SXDXEG motif. D-Ala-D-Ala and D-Ala-Gly-Gly are the preferred substrates. Bacillus subtilis dppA is thought to function as an adaptation to nutrient deficiency; hydrolysis of its substrate releases D-Ala which can be used subsequently as metabolic fuel. This family also contains a number of uncharacterized putative peptidases.
Links
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Statistics
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PSSM-Id: 176449
View PSSM: cd00281
Aligned: 3 rows
Threshold Bit Score: 390.416
Threshold Setting Gi: 217076353
Created: 25-Jan-2002
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 5 residues -Click on image for an interactive view with Cn3D
Feature 1:metal binding site [ion binding site]
Evidence:
  • Structure:1HI9: Bacillus subtilis D-Aminopeptidase DppA binds two Zn(II) ions; contacts at 4.0A
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1               # #                                                 #                    
1HI9_A         1 MKLYMSVDMEGisglpddtfvdsgkrnyergRLIMTEEANYCIAEAFnsgcTEVLVNDSHskmnNLMVEklh--peADLI 78  Bacillus subtilis
YP_002334069   1 MKIYVSIDFEGlggvtqwsd---veygvkfkQNYLMEQLKAFLRATDg---NYVLLVDSHamgdNILWEitkefenVELI 74  Thermosipho afr...
Q2JK39         1 MKVYISADIEGiagishwdeatigqpgyeafREQMTRAVIAACEGSLaagaTQITVKDAHdsgrNLIPErlp--epVQLI 78  Synechococcus s...
Feature 1                                  #                              #                      
1HI9_A        79 SG-DVKPFSMveglddtfRGALFlGYHARast-pgvMSHSmif-gvrHFYINdrpvgELGLNAYVAGyyDVPVlMVAGDd 155 Bacillus subtilis
YP_002334069  75 SG-GLRKNYMmsgldesfDRVVFfGYHAGvgtryavMDHSyssssiyNIWINgqkmnEALINAAYAGlyNVPVaMIVGD- 152 Thermosipho afr...
Q2JK39        79 RGwSGHPYCMvqeldrsyDALLLiGYHARagsaanpLAHTytt-evsQIRLNgqaiaEFHLVSLTAAyeGVPVvFVAGDa 157 Synechococcus s...
Feature 1                                                                                        
1HI9_A       156 RAAKEAEElipnVTTAAvKQTISRsAVKCLspAKRGRLLTEKTAFALQnk---dkVKPLTPpdrpVLSIEFaNYGQAEWA 232 Bacillus subtilis
YP_002334069 153 DKLKGQVFd--dVFFVEtKESLGRfSAKHKsmKKVLKEIEETTRRMLQvpr--ekFKVYKFdtpvELVVEFtDTARADLV 228 Thermosipho afr...
Q2JK39       158 EVCAEAKAydaqIETVVtHKGMGQ-SVIAPhpQQVLRAIRQGVEGSLRrlpayrpRPLPDHf---QLEVDYkDPARAYRK 233 Synechococcus s...
Feature 1                                        
1HI9_A       233 NLmpgTEIKTgttTVQFQAkdmlEAYQAMLVM 264 Bacillus subtilis
YP_002334069 229 EMlplVERVNg-rSVKLVHedyqVIFDAILSM 259 Thermosipho africanus TCF52B
Q2JK39       234 SFypgCRWIAd-sTVRLEVsewfEVLRALEFI 264 Synechococcus sp. JA-2-3B'a(2-13)

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