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Conserved domains on  [gi|1069055649|gb|OEH18724|]
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D-alanyl-D-alanine dipeptidase [Enterobacter asburiae]

Protein Classification

D-alanyl-D-alanine dipeptidase( domain architecture ID 10013449)

D-alanyl-D-alanine dipeptidase catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10178 PRK10178
D-alanyl-D-alanine dipeptidase; Provisional
 1-182 4.23e-120

D-alanyl-D-alanine dipeptidase; Provisional


:

Pssm-ID: 236662  Cd Length: 184  Bit Score: 337.38  E-value: 4.23e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649   1 MPEESELIDVAKTFPTLHIDLKYATADNITGRPIYQEALCLLHTDAATALAKAISIASLAGLKLVVYDAYRPQQAQAQLW 80
Cdd:PRK10178    1 MMDTTRLVEITVAFHGVEIDLKYATADNLTGKPIYREARCLLHKDAEAALRKAVSIAQLAGLTLRIYDAYRPQQAQQVLW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649  81 DACPNPEYVVDVAIGSNHSRGTAIDVTLMDEHNAVLDMGAGFDEMHDRSHPYHPSVPPHAQRNRLLLNAIMFGGGFVGIS 160
Cdd:PRK10178   81 DACPDPQYVADLGRGSNHSRGTAIDLTLVDAHGNILDMGTGFDEMHARSHHFHPGVPPAAQRNRLLLLGIMHAAGFVHIA 160

                         170       180
                  ....*....|....*....|..
gi 1069055649 161 SEWWHFELPNAASYPLLDDRFA 182
Cdd:PRK10178  161 SEWWHYELPGAAAYPLLDDQAS 182
 
Name Accession Description Interval E-value
PRK10178 PRK10178
D-alanyl-D-alanine dipeptidase; Provisional
 1-182 4.23e-120

D-alanyl-D-alanine dipeptidase; Provisional


Pssm-ID: 236662  Cd Length: 184  Bit Score: 337.38  E-value: 4.23e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649   1 MPEESELIDVAKTFPTLHIDLKYATADNITGRPIYQEALCLLHTDAATALAKAISIASLAGLKLVVYDAYRPQQAQAQLW 80
Cdd:PRK10178    1 MMDTTRLVEITVAFHGVEIDLKYATADNLTGKPIYREARCLLHKDAEAALRKAVSIAQLAGLTLRIYDAYRPQQAQQVLW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649  81 DACPNPEYVVDVAIGSNHSRGTAIDVTLMDEHNAVLDMGAGFDEMHDRSHPYHPSVPPHAQRNRLLLNAIMFGGGFVGIS 160
Cdd:PRK10178   81 DACPDPQYVADLGRGSNHSRGTAIDLTLVDAHGNILDMGTGFDEMHARSHHFHPGVPPAAQRNRLLLLGIMHAAGFVHIA 160

                         170       180
                  ....*....|....*....|..
gi 1069055649 161 SEWWHFELPNAASYPLLDDRFA 182
Cdd:PRK10178  161 SEWWHYELPGAAAYPLLDDQAS 182
DdpX COG2173
D-alanyl-D-alanine dipeptidase [Cell wall/membrane/envelope biogenesis];
4-182 2.72e-85

D-alanyl-D-alanine dipeptidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441776  Cd Length: 207  Bit Score: 250.18  E-value: 2.72e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649   4 ESELIDVAKTFPTLHIDLKYATADNITGRPI-YQEALCLLHTDAATALAKAISIASLAGLKLVVYDAYRPQQAQAQLWDA 82
Cdd:COG2173    12 PEGLVDIADVDPGIRLDLRYATPDNFTGRPVpYGAPRCYLRRPAAEALAKAQAELAAQGLRLKIFDAYRPQSAQQHFWDA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649  83 CPNP----------------EYVVDVAIGSNHSRGTAIDVTLMDEHNAVLDMGAGFDEMHDRSHPYHPSVPPHAQRNRLL 146
Cdd:COG2173    92 LPDDlrmkypdvdkaelfvrGYVADPARGSPHSRGAAVDLTLVDATGKELDMGTGFDEFSPRSHPDYPGLTAEARANRRL 171

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1069055649 147 LNAIMFGGGFVGISSEWWHFELPNAASYPLLDDRFA 182
Cdd:COG2173   172 LREAMEAAGFTNYPTEWWHFDLGDEMPYPVLDFPVE 207
D-Ala-D-Ala_dipeptidase_Aad cd14840
D-Ala-D-Ala dipeptidase (includes Lactobacillus plantarum Aad peptidase); D-Ala-D-Ala ...
 20-177 8.09e-82

D-Ala-D-Ala dipeptidase (includes Lactobacillus plantarum Aad peptidase); D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine dipeptidase vanX; VanX; EC 3.4.13.22) is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci and other bacteria (both Gram-positive and Gram-negative). It is part of a gene cluster that affects cell-wall biosynthesis. The operon triggers the termination of peptidoglycan precursors by D-Ala-(R)-lactate instead of D-Ala-D-Ala dipeptides. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. This subfamily includes Lactobacillus Aad peptidase and belongs in the MEROPS peptidase family M15, subfamily D.


Pssm-ID: 350617 [Multi-domain]  Cd Length: 158  Bit Score: 239.63  E-value: 8.09e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649  20 DLKYATADNITGRPIYQEALCLLHTDAATALAKAISIASLAGLKLVVYDAYRPQQAQAQLWDACPNPEYVVDVAIGSNHS 99
Cdd:cd14840     1 DLRYATTDNFTGKKLYPSARAYLRKEAAEKLAKAQKELKKPGYRLKIFDAYRPLSVQKKLWEAVPDPRYVANPAKGSRHN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1069055649 100 RGTAIDVTLMDEHNAVLDMGAGFDEMHDRSHPYHPSVPPHAQRNRLLLNAIMFGGGFVGISSEWWHFELPNAASYPLL 177
Cdd:cd14840    81 RGAAVDLTLVDLKGGELDMGTGFDDFSERAHHDYEGLSEEALKNRLLLREVMEKAGFKPIPTEWWHFDDPDWKKYPLL 158
Peptidase_M15 pfam01427
D-ala-D-ala dipeptidase;
4-185 2.75e-75

D-ala-D-ala dipeptidase;


Pssm-ID: 279735  Cd Length: 199  Bit Score: 224.41  E-value: 2.75e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649   4 ESELIDVAKTFPTLHIDLKYATADNITGRP-IYQEALCLLHTDAATALAKAISIASLAGLKLVVYDAYRPQQAQ--AQLW 80
Cdd:pfam01427   2 SLGLVDLAQVGPDYQIDLKYATADNFTGKQlLYQAARCLAHKEPAWALAVADAYAPIAGQQLVVWDTYRPIVAQdgLQGW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649  81 DACPNPEYVVDVAIG-------------SNHSRGTAIDVTLM-DEHNAVLDMGAGFDEMHDRSHPYHPS-VPPHAQRNRL 145
Cdd:pfam01427  82 VATPEPKEVIYHQVYqiwavpnnnpltpSPHSRGAAIDLTLRrDDLGQLVDMGGEFDEMSERSHANAYQtVEPAAQRNRK 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1069055649 146 LLNAIMFGGGFVGISSEWWHFELPNAAsyplLDDRFACFP 185
Cdd:pfam01427 162 LLRAIMESGGFLRYSGEWWHFSLPDAL----YNDRHPDFQ 197
 
Name Accession Description Interval E-value
PRK10178 PRK10178
D-alanyl-D-alanine dipeptidase; Provisional
 1-182 4.23e-120

D-alanyl-D-alanine dipeptidase; Provisional


Pssm-ID: 236662  Cd Length: 184  Bit Score: 337.38  E-value: 4.23e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649   1 MPEESELIDVAKTFPTLHIDLKYATADNITGRPIYQEALCLLHTDAATALAKAISIASLAGLKLVVYDAYRPQQAQAQLW 80
Cdd:PRK10178    1 MMDTTRLVEITVAFHGVEIDLKYATADNLTGKPIYREARCLLHKDAEAALRKAVSIAQLAGLTLRIYDAYRPQQAQQVLW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649  81 DACPNPEYVVDVAIGSNHSRGTAIDVTLMDEHNAVLDMGAGFDEMHDRSHPYHPSVPPHAQRNRLLLNAIMFGGGFVGIS 160
Cdd:PRK10178   81 DACPDPQYVADLGRGSNHSRGTAIDLTLVDAHGNILDMGTGFDEMHARSHHFHPGVPPAAQRNRLLLLGIMHAAGFVHIA 160

                         170       180
                  ....*....|....*....|..
gi 1069055649 161 SEWWHFELPNAASYPLLDDRFA 182
Cdd:PRK10178  161 SEWWHYELPGAAAYPLLDDQAS 182
DdpX COG2173
D-alanyl-D-alanine dipeptidase [Cell wall/membrane/envelope biogenesis];
4-182 2.72e-85

D-alanyl-D-alanine dipeptidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441776  Cd Length: 207  Bit Score: 250.18  E-value: 2.72e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649   4 ESELIDVAKTFPTLHIDLKYATADNITGRPI-YQEALCLLHTDAATALAKAISIASLAGLKLVVYDAYRPQQAQAQLWDA 82
Cdd:COG2173    12 PEGLVDIADVDPGIRLDLRYATPDNFTGRPVpYGAPRCYLRRPAAEALAKAQAELAAQGLRLKIFDAYRPQSAQQHFWDA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649  83 CPNP----------------EYVVDVAIGSNHSRGTAIDVTLMDEHNAVLDMGAGFDEMHDRSHPYHPSVPPHAQRNRLL 146
Cdd:COG2173    92 LPDDlrmkypdvdkaelfvrGYVADPARGSPHSRGAAVDLTLVDATGKELDMGTGFDEFSPRSHPDYPGLTAEARANRRL 171

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1069055649 147 LNAIMFGGGFVGISSEWWHFELPNAASYPLLDDRFA 182
Cdd:COG2173   172 LREAMEAAGFTNYPTEWWHFDLGDEMPYPVLDFPVE 207
D-Ala-D-Ala_dipeptidase_Aad cd14840
D-Ala-D-Ala dipeptidase (includes Lactobacillus plantarum Aad peptidase); D-Ala-D-Ala ...
 20-177 8.09e-82

D-Ala-D-Ala dipeptidase (includes Lactobacillus plantarum Aad peptidase); D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine dipeptidase vanX; VanX; EC 3.4.13.22) is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci and other bacteria (both Gram-positive and Gram-negative). It is part of a gene cluster that affects cell-wall biosynthesis. The operon triggers the termination of peptidoglycan precursors by D-Ala-(R)-lactate instead of D-Ala-D-Ala dipeptides. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. This subfamily includes Lactobacillus Aad peptidase and belongs in the MEROPS peptidase family M15, subfamily D.


Pssm-ID: 350617 [Multi-domain]  Cd Length: 158  Bit Score: 239.63  E-value: 8.09e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649  20 DLKYATADNITGRPIYQEALCLLHTDAATALAKAISIASLAGLKLVVYDAYRPQQAQAQLWDACPNPEYVVDVAIGSNHS 99
Cdd:cd14840     1 DLRYATTDNFTGKKLYPSARAYLRKEAAEKLAKAQKELKKPGYRLKIFDAYRPLSVQKKLWEAVPDPRYVANPAKGSRHN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1069055649 100 RGTAIDVTLMDEHNAVLDMGAGFDEMHDRSHPYHPSVPPHAQRNRLLLNAIMFGGGFVGISSEWWHFELPNAASYPLL 177
Cdd:cd14840    81 RGAAVDLTLVDLKGGELDMGTGFDDFSERAHHDYEGLSEEALKNRLLLREVMEKAGFKPIPTEWWHFDDPDWKKYPLL 158
Peptidase_M15 pfam01427
D-ala-D-ala dipeptidase;
4-185 2.75e-75

D-ala-D-ala dipeptidase;


Pssm-ID: 279735  Cd Length: 199  Bit Score: 224.41  E-value: 2.75e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649   4 ESELIDVAKTFPTLHIDLKYATADNITGRP-IYQEALCLLHTDAATALAKAISIASLAGLKLVVYDAYRPQQAQ--AQLW 80
Cdd:pfam01427   2 SLGLVDLAQVGPDYQIDLKYATADNFTGKQlLYQAARCLAHKEPAWALAVADAYAPIAGQQLVVWDTYRPIVAQdgLQGW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649  81 DACPNPEYVVDVAIG-------------SNHSRGTAIDVTLM-DEHNAVLDMGAGFDEMHDRSHPYHPS-VPPHAQRNRL 145
Cdd:pfam01427  82 VATPEPKEVIYHQVYqiwavpnnnpltpSPHSRGAAIDLTLRrDDLGQLVDMGGEFDEMSERSHANAYQtVEPAAQRNRK 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1069055649 146 LLNAIMFGGGFVGISSEWWHFELPNAAsyplLDDRFACFP 185
Cdd:pfam01427 162 LLRAIMESGGFLRYSGEWWHFSLPDAL----YNDRHPDFQ 197
D-Ala-D-Ala_dipeptidase_VanX cd14817
D-Ala-D-Ala dipeptidase VanX; D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine ...
 5-175 1.89e-55

D-Ala-D-Ala dipeptidase VanX; D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine dipeptidase vanX; VanX; EC 3.4.13.22) is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci and other bacteria (both Gram-positive and Gram-negative). It is part of a gene cluster that affects cell-wall biosynthesis. The operon triggers the termination of peptidoglycan precursors by D-Ala-(R)-lactate instead of D-Ala-D-Ala dipeptides. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. It belongs in the MEROPS peptidase family M15, subfamily D.


Pssm-ID: 350616  Cd Length: 199  Bit Score: 174.22  E-value: 1.89e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649   5 SELIDVAKTFPTLHIDLKYATADNITGRPI--YQEALCLLHTDAATALAKAISIASLAGLKLVVYDAYRPQQAQAQLWDA 82
Cdd:cd14817     1 AGFVYLADVIPDIVQDIRYAGSDNFVGRPIdgYEAPRCILTREAAEALAKVQAELAKQGLGLKVYDCYRPQRAVDHFVRW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649  83 CPNPE---------YVVD---------VAIGSNHSRGTAIDVTLMD-EHNAVLDMGAGFDEMHDRSHPYHPSVPPHAQRN 143
Cdd:cd14817    81 AKDPDdtrmkaefyPDVDkkdlfelgyIAEKSGHSRGSTVDLTLVDlDTGEELDMGTPFDFFDPLSHTDSPGITAQQRAN 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1069055649 144 RLLLNAIMFGGGFVGISSEWWHFELPNaASYP 175
Cdd:cd14817   161 RLLLRSLMEKHGFKPYPKEWWHFTLKD-EPYP 191
D-Ala-D-Ala_dipeptidase cd17880
D-Ala-D-Ala_dipeptidase; This family contains D-Ala-D-Ala dipeptidase enzymes which include ...
 44-169 1.70e-35

D-Ala-D-Ala_dipeptidase; This family contains D-Ala-D-Ala dipeptidase enzymes which include D-alanyl-D-alanine dipeptidase vanX and Aad, among others. VanX is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci and other bacteria (both Gram-positive and Gram-negative). It is part of a gene cluster that affects cell-wall biosynthesis. The operon triggers the termination of peptidoglycan precursors by D-Ala-(R)-lactate instead of D-Ala-D-Ala dipeptides. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. It fasmily includes Lactobacillus Aad peptidase and belongs in the MEROPS peptidase family M15, subfamily D.


Pssm-ID: 350625 [Multi-domain]  Cd Length: 110  Bit Score: 120.52  E-value: 1.70e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649  44 TDAATALAKAISIASLAGLKLVVYDAYRPQQAQAQLWDACPNPE------------------YVVDVAIGSNHSRGTAID 105
Cdd:cd17880     1 TGVLKRLDKARLTAADIGWELLVFDAYRPIAAQQFMVQHTFAPIvardglqgqhqvyqiwavPNNNVLTPSPHSRGAAID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069055649 106 VTLmdehnavldmgagfdemhdrshpyhpsvpphaqrNRLLLNAIMFGGGFVGISSEWWHFELP 169
Cdd:cd17880    81 LTL----------------------------------RRELLNTIMESGGFLRHSGEWWHFSLG 110
D-Ala-D-Ala_dipeptidase_like cd14843
D-Ala-D-Ala dipeptidase, includes uncharacterized enzymes; This subfamily of D-Ala-D-Ala ...
 41-170 4.10e-23

D-Ala-D-Ala dipeptidase, includes uncharacterized enzymes; This subfamily of D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine dipeptidase vanX; VanX; EC 3.4.13.22) also includes several uncharacterized proteins. This is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci and other bacteria (both Gram-positive and Gram-negative). It is part of a gene cluster that affects cell-wall biosynthesis. The operon triggers the termination of peptidoglycan precursors by D-Ala-(R)-lactate instead of D-Ala-D-Ala dipeptides. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. It belongs in the MEROPS peptidase family M15, subfamily D.


Pssm-ID: 350618 [Multi-domain]  Cd Length: 160  Bit Score: 90.04  E-value: 4.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649  41 LLHtdAATALAKaisiaslaGLKLVVYDAYRPQQAQAQLWDAC--------PNP----------EYVVDVAIGSN----H 98
Cdd:cd14843     9 LLQ--AQSLLPK--------GLRLLIFDGYRPLAVQKFLFERYyqkirkrhPGRspeelieevrKFVAPPSKDPLtpppH 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1069055649  99 SRGTAIDVTLMDEHNAVLDMGAGFDEMHDRSHPYH------PSVPPHAQRNRLLLNAIMFGGGFVGISSEWWHFELPN 170
Cdd:cd14843    79 STGGAVDLTLADEDGKELDMGGPIDDDTEASEAYEealtdsTGISEEARNNRRLLYDAMESAGFVNYPTEWWHFSYGD 156
Peptidase_M15 cd14814
Metalloproteases including zinc D-Ala-D-Ala carboxypeptidase, L-Ala-D-Glu peptidase, L, ...
 44-169 1.42e-13

Metalloproteases including zinc D-Ala-D-Ala carboxypeptidase, L-Ala-D-Glu peptidase, L,D-carboxypeptidase, bacteriophage endolysins, and related proteins; This family summarizes zinc-binding metallopeptidases which are mostly carboxypeptidases and dipeptidases, and includes zinc-dependent D-Ala-D-Ala carboxypeptidases, VanX, L-Ala-D-Glu peptidase, L,D-carboxypeptidase and bacteriophage endolysins, amongst other family members. These peptidases belong to MEROPS family M15 which are involved in bacterial cell wall biosynthesis and metabolism.


Pssm-ID: 350615 [Multi-domain]  Cd Length: 111  Bit Score: 64.00  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649  44 TDAATALAKAISIASLAGLKLVVYDAYRPQQAQAQLWDACPNPEYVVDVA---IGSNHSRGTAIDVTLMDEHNAvldmGA 120
Cdd:cd14814     1 PDAAEALARMIAAAGAEGRTLTINSGYRTYAQQLRLFAAKGKGSGGRRWAappGTSNHQWGLAIDLGDGGGWRE----TQ 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1069055649 121 GFDEMHDRSHPYHPSVPPhaqrnrlllnaimfGGGFVGISSEWWHFELP 169
Cdd:cd14814    77 GYRWLKANAPRYGFDNPG--------------GARRGGAFQEPWHWEYV 111
LdcB COG1876
LD-carboxypeptidase LdcB, LAS superfamily [Cell wall/membrane/envelope biogenesis];
10-167 1.04e-05

LD-carboxypeptidase LdcB, LAS superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441480  Cd Length: 168  Bit Score: 43.72  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649  10 VAKTFPTLHIDLKYATADNItgrpiyqealcLLHTDAATALAKAISIASLAGLKLVVYDAYRPQQAQAQLWDACPNpEYV 89
Cdd:COG1876     2 VNKDHPLPADDLVPLPGGGH-----------RLRKEAAAAFEAMQAAAKKDGIDLVIVSGYRSYERQEALYNRKVA-RYG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649  90 VDVAIG-------SNHSRGTAIDVTLMDEHnavLDMGAGFDEmhdrshpyhpsvppHAQRNRLLLNAIMFggGFV----- 157
Cdd:COG1876    70 IEAALRysappgtSEHHTGLAIDIGDPDPG---TDLEEEFEE--------------TPAGKWLAANAAKY--GFIlrypk 130

                         170
                  ....*....|....*.
gi 1069055649 158 ------GISSEWWHFE 167
Cdd:COG1876   131 gkeditGYAYEPWHWR 146
L-Ala-D-Glu_peptidase_like cd14845
L-Ala-D-Glu peptidase, also known as L-alanyl-D-glutamate endopeptidase; This L-Ala-D-Glu ...
 41-110 1.06e-05

L-Ala-D-Glu peptidase, also known as L-alanyl-D-glutamate endopeptidase; This L-Ala-D-Glu peptidase family includes L-alanyl-D-glutamate peptidase (bacteriophage T5) (also known as L-alanoyl-D-glutamate endopeptidase), and Ply118 and Ply500 L-Ala-D-Glu peptidase. Bacteriophage endolysin degrades the peptidoglycan of the bacterial host from within, leading to cell lysis and release of progeny virions. The bacteriophage endolysin Ply118 cleaves between L-Ala and D-Glu residues of Listeria cell wall peptidoglycan. This family belongs to the MEROPS peptidase M15 subfamily C.


Pssm-ID: 350620 [Multi-domain]  Cd Length: 126  Bit Score: 43.12  E-value: 1.06e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1069055649  41 LLHTDAATALAKAISIASLAGLKLVVYDAYRPQQAQAQLWDACPN-PEYVVDVAIG--SNHSRGTAIDVTLMD 110
Cdd:cd14845     7 GLHPEVRAVVKELIELAEEEGIDFRITEGYRSPARQAALYAQGRTkPGLIVTNARGgqSYHNYGLAVDIVPLV 79
VanY pfam02557
D-alanyl-D-alanine carboxypeptidase;
41-107 1.23e-05

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 426830 [Multi-domain]  Cd Length: 131  Bit Score: 42.99  E-value: 1.23e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1069055649  41 LLHTDAATALAKAISIASLAGLKLVVYDAYRPQQAQAQLW------DACPNPEYVVDVAIGSNHSRGTAIDVT 107
Cdd:pfam02557   3 YLRKEAAEALEELFAAAKKEGINLRAISGFRSYEYQEALFkkyvkgEGKKAILRWSAPPGTSEHHTGLAIDIG 75
LD-carboxypeptidase cd14852
L,D-carboxypeptidase DacB and LdcB, and related proteins; This L,D-carboxypeptidase family ...
 41-119 3.80e-04

L,D-carboxypeptidase DacB and LdcB, and related proteins; This L,D-carboxypeptidase family includes LdcB LD-Carboxypeptidase from Streptococcus pneumoniae, Bacillus anthracis, and Bacillus subtilis, and L,D-carboxypeptidase DacB from Streptococcus pneumonia and Lactococcus lactis. These enzymes are active against cell-wall-derived tetrapeptides and synthetic tetrapeptides lacking the sugar moiety but are inactive against tetrapeptides terminating in L-alanine. L,D-carboxypeptidase DacB plays a key role in the remodeling of S. pneumoniae peptidoglycan during cell division. It adopts a zinc-dependent carboxypeptidase fold and acts as an L,D-carboxypeptidase towards the tetrapeptide L-Ala-D-iGln-L-Lys-D-Ala of the peptidoglycan stem. This family also includes vanY D-Ala-D-Ala carboxypeptidase which is vancomycin-inducible and penicillin-resistant. VanY hydrolyzes depsipeptide- and D-alanyl-D-alanine-containing peptidoglycan precursors; it is insensitive to beta-lactams. All these enzymes belong to the MEROPS family M15 subfamily B.


Pssm-ID: 350624  Cd Length: 162  Bit Score: 39.15  E-value: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055649  41 LLHTDAATALAKAISIASLAGLKLVVYDAYRPQQAQAQLWD---ACPNPEY---VVDVAIGSNHSRGTAIDVTLMDEHNA 114
Cdd:cd14852    29 YLRKEAAEALEEMFDAAKKDGIDLTIVSGYRSYEYQQELYNnyvARYGKEEadrYSARPGYSEHQTGLAVDIGSTDGPCL 108


                  ....*
gi 1069055649 115 VLDMG 119
Cdd:cd14852   109 EESFE 113
 
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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