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Conserved domains on  [gi|502822610|ref|WP_013057586|]
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MULTISPECIES: D-alanyl-D-alanine carboxypeptidase family protein [Priestia]

Protein Classification

D-alanyl-D-alanine carboxypeptidase family protein( domain architecture ID 11449003)

D-alanyl-D-alanine carboxypeptidase family protein such as Streptococcus pneumoniae L,D-carboxypeptidase Dacb and Enterococcus faecium D-alanyl-D-alanine carboxypeptidase, which removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LdcB COG1876
LD-carboxypeptidase LdcB, LAS superfamily [Cell wall/membrane/envelope biogenesis];
70-249 6.61e-77

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


:

Pssm-ID: 441480  Cd Length: 168  Bit Score: 230.15  E-value: 6.61e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610  70 LVNKKHQLPesyqPSDLVYADVPfifnekieKRMLRKPAAQALEELFRDAEKEGISLLGVSGYRSHERQKELFAFYAKRD 149
Cdd:COG1876    1 LVNKDHPLP----ADDLVPLPGG--------GHRLRKEAAAAFEAMQAAAKKDGIDLVIVSGYRSYERQEALYNRKVARY 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610 150 GEEQARTYSAYPGTSEHETGLAIDVTGGSGMCAAADCFADTPEAHWLSKNAYQYGFIIRYPEGEEQVTGYKYEPWHLRYV 229
Cdd:COG1876   69 GIEAALRYSAPPGTSEHHTGLAIDIGDPDPGTDLEEEFEETPAGKWLAANAAKYGFILRYPKGKEDITGYAYEPWHWRYV 148

                        170       180
                 ....*....|....*....|
gi 502822610 230 GKKAAASIFNQYATLETYAN 249
Cdd:COG1876  149 GVEAAKEIFEKGLTLEEYLG 168
 
Name Accession Description Interval E-value
LdcB COG1876
LD-carboxypeptidase LdcB, LAS superfamily [Cell wall/membrane/envelope biogenesis];
70-249 6.61e-77

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


Pssm-ID: 441480  Cd Length: 168  Bit Score: 230.15  E-value: 6.61e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610  70 LVNKKHQLPesyqPSDLVYADVPfifnekieKRMLRKPAAQALEELFRDAEKEGISLLGVSGYRSHERQKELFAFYAKRD 149
Cdd:COG1876    1 LVNKDHPLP----ADDLVPLPGG--------GHRLRKEAAAAFEAMQAAAKKDGIDLVIVSGYRSYERQEALYNRKVARY 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610 150 GEEQARTYSAYPGTSEHETGLAIDVTGGSGMCAAADCFADTPEAHWLSKNAYQYGFIIRYPEGEEQVTGYKYEPWHLRYV 229
Cdd:COG1876   69 GIEAALRYSAPPGTSEHHTGLAIDIGDPDPGTDLEEEFEETPAGKWLAANAAKYGFILRYPKGKEDITGYAYEPWHWRYV 148

                        170       180
                 ....*....|....*....|
gi 502822610 230 GKKAAASIFNQYATLETYAN 249
Cdd:COG1876  149 GVEAAKEIFEKGLTLEEYLG 168
LD-carboxypeptidase cd14852
L,D-carboxypeptidase DacB and LdcB, and related proteins; This L,D-carboxypeptidase family ...
 69-237 6.84e-77

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: 229.82  E-value: 6.84e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610  69 ALVNKKHQLPESYQPSDLVyadvpfIFNEKIEKRMLRKPAAQALEELFRDAEKEGISLLGVSGYRSHERQKELFAFYAKR 148
Cdd:cd14852    1 VLVNKDHPLPEDYVPEDLV------PYVLLDNGLYLRKEAAEALEEMFDAAKKDGIDLTIVSGYRSYEYQQELYNNYVAR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610 149 DGEEQARTYSAYPGTSEHETGLAIDVTGGSGmCAAADCFADTPEAHWLSKNAYQYGFIIRYPEGEEQVTGYKYEPWHLRY 228
Cdd:cd14852   75 YGKEEADRYSARPGYSEHQTGLAVDIGSTDG-PCLEESFEDTPAGKWLAENAHKYGFILRYPKGKENITGYSYEPWHFRY 153


                 ....*....
gi 502822610 229 VGKKAAASI 237
Cdd:cd14852  154 VGKEAAKKI 162
VanY pfam02557
D-alanyl-D-alanine carboxypeptidase;
104-231 6.89e-63

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 426830 [Multi-domain]  Cd Length: 131  Bit Score: 193.22  E-value: 6.89e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610  104 LRKPAAQALEELFRDAEKEGISLLGVSGYRSHERQKELFAFYAKRDGEEQARTYSAYPGTSEHETGLAIDVTGGSGMCAA 183
Cdd:pfam02557   4 LRKEAAEALEELFAAAKKEGINLRAISGFRSYEYQEALFKKYVKGEGKKAILRWSAPPGTSEHHTGLAIDIGDPDNPWEL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 502822610  184 ADCFADTPEAHWLSKNAYQYGFIIRYPEGEEQVTGYKYEPWHLRYVGK 231
Cdd:pfam02557  84 EESFEDTAAFKWLQANAHKYGFVLRYPKGKEQITGVSYEPWHWRYVGI 131
LD_carboxy_LdcB NF041194
LD-carboxypeptidase LdcB/DacB;
70-247 5.92e-44

LD-carboxypeptidase LdcB/DacB;


Pssm-ID: 469098  Cd Length: 180  Bit Score: 146.42  E-value: 5.92e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610  70 LVNKKHQLPESYQPSDlvyadvpfifnekiekrmlrKPAAQA-LEELFRDAEKEGISLLG-VSGYRSHERQKELFAFYAK 147
Cdd:NF041194  19 IVNKHYPLSKDYNPGE--------------------NPTAKAaLLQLIADMQAAGYPISDqYSGFRSYETQTELYQNYVN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610 148 RDGEEQARTYSAYPGTSEHETGLAIDVTGGSGmcaaaDCFADTPEAHWLSKNAYQYGFIIRYPEGEEQVTGYKYEPWHLR 227
Cdd:NF041194  79 QDGKEAADRYSARPGYSEHQTGLAFDLIDTSG-----NLLEEPKASQWLLDHAADYGFIVRYLKGKEASTGYMPESWHLR 153

                        170       180
                 ....*....|....*....|
gi 502822610 228 YVGKKAAAsIFNQYATLETY 247
Cdd:NF041194 154 YIGKEAKE-IADSGLSLEEY 172
 
Name Accession Description Interval E-value
LdcB COG1876
LD-carboxypeptidase LdcB, LAS superfamily [Cell wall/membrane/envelope biogenesis];
70-249 6.61e-77

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


Pssm-ID: 441480  Cd Length: 168  Bit Score: 230.15  E-value: 6.61e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610  70 LVNKKHQLPesyqPSDLVYADVPfifnekieKRMLRKPAAQALEELFRDAEKEGISLLGVSGYRSHERQKELFAFYAKRD 149
Cdd:COG1876    1 LVNKDHPLP----ADDLVPLPGG--------GHRLRKEAAAAFEAMQAAAKKDGIDLVIVSGYRSYERQEALYNRKVARY 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610 150 GEEQARTYSAYPGTSEHETGLAIDVTGGSGMCAAADCFADTPEAHWLSKNAYQYGFIIRYPEGEEQVTGYKYEPWHLRYV 229
Cdd:COG1876   69 GIEAALRYSAPPGTSEHHTGLAIDIGDPDPGTDLEEEFEETPAGKWLAANAAKYGFILRYPKGKEDITGYAYEPWHWRYV 148

                        170       180
                 ....*....|....*....|
gi 502822610 230 GKKAAASIFNQYATLETYAN 249
Cdd:COG1876  149 GVEAAKEIFEKGLTLEEYLG 168
LD-carboxypeptidase cd14852
L,D-carboxypeptidase DacB and LdcB, and related proteins; This L,D-carboxypeptidase family ...
 69-237 6.84e-77

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: 229.82  E-value: 6.84e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610  69 ALVNKKHQLPESYQPSDLVyadvpfIFNEKIEKRMLRKPAAQALEELFRDAEKEGISLLGVSGYRSHERQKELFAFYAKR 148
Cdd:cd14852    1 VLVNKDHPLPEDYVPEDLV------PYVLLDNGLYLRKEAAEALEEMFDAAKKDGIDLTIVSGYRSYEYQQELYNNYVAR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610 149 DGEEQARTYSAYPGTSEHETGLAIDVTGGSGmCAAADCFADTPEAHWLSKNAYQYGFIIRYPEGEEQVTGYKYEPWHLRY 228
Cdd:cd14852   75 YGKEEADRYSARPGYSEHQTGLAVDIGSTDG-PCLEESFEDTPAGKWLAENAHKYGFILRYPKGKENITGYSYEPWHFRY 153


                 ....*....
gi 502822610 229 VGKKAAASI 237
Cdd:cd14852  154 VGKEAAKKI 162
VanY pfam02557
D-alanyl-D-alanine carboxypeptidase;
104-231 6.89e-63

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 426830 [Multi-domain]  Cd Length: 131  Bit Score: 193.22  E-value: 6.89e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610  104 LRKPAAQALEELFRDAEKEGISLLGVSGYRSHERQKELFAFYAKRDGEEQARTYSAYPGTSEHETGLAIDVTGGSGMCAA 183
Cdd:pfam02557   4 LRKEAAEALEELFAAAKKEGINLRAISGFRSYEYQEALFKKYVKGEGKKAILRWSAPPGTSEHHTGLAIDIGDPDNPWEL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 502822610  184 ADCFADTPEAHWLSKNAYQYGFIIRYPEGEEQVTGYKYEPWHLRYVGK 231
Cdd:pfam02557  84 EESFEDTAAFKWLQANAHKYGFVLRYPKGKEQITGVSYEPWHWRYVGI 131
LD_carboxy_LdcB NF041194
LD-carboxypeptidase LdcB/DacB;
70-247 5.92e-44

LD-carboxypeptidase LdcB/DacB;


Pssm-ID: 469098  Cd Length: 180  Bit Score: 146.42  E-value: 5.92e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610  70 LVNKKHQLPESYQPSDlvyadvpfifnekiekrmlrKPAAQA-LEELFRDAEKEGISLLG-VSGYRSHERQKELFAFYAK 147
Cdd:NF041194  19 IVNKHYPLSKDYNPGE--------------------NPTAKAaLLQLIADMQAAGYPISDqYSGFRSYETQTELYQNYVN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610 148 RDGEEQARTYSAYPGTSEHETGLAIDVTGGSGmcaaaDCFADTPEAHWLSKNAYQYGFIIRYPEGEEQVTGYKYEPWHLR 227
Cdd:NF041194  79 QDGKEAADRYSARPGYSEHQTGLAFDLIDTSG-----NLLEEPKASQWLLDHAADYGFIVRYLKGKEASTGYMPESWHLR 153

                        170       180
                 ....*....|....*....|
gi 502822610 228 YVGKKAAAsIFNQYATLETY 247
Cdd:NF041194 154 YIGKEAKE-IADSGLSLEEY 172
DD-dipeptidase_VanXYc cd14849
D-Ala-D-Ala dipeptidase/D-Ala-D-Ala carboxypeptidase (VanXYc) and related proteins; VanXYc ...
 104-230 3.48e-34

D-Ala-D-Ala dipeptidase/D-Ala-D-Ala carboxypeptidase (VanXYc) and related proteins; VanXYc peptidase (also known as vanXY(C) peptidase, D-alanyl-D-alanine carboxypeptidase D,D-dipeptidase/D,D-carboxypeptidase, vancomycin resistance D,D-dipeptidase) is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci. Some of the vancomycin resistance operons encode VanXY D,D-carboxypeptidase which hydrolyzes both, dipeptide (D-Ala-D-Ala) or pentapeptide (UDP-MurNac-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala). It is a bifunctional enzyme that catalyzes D,D-peptidase and D,D-carboxypeptidase activities. VanXY has higher sequence similarity to VanY than with VanX and hydrolyzes D,D-dipeptides such as D-Ala-D-Ala, whereas VanY is inactive against this substrate; thus having a less restrictive active site to accommodate larger substrates such as UDP-MurNAc-pentapeptide[Ala]. This family belongs to the MEROPS family M15, subfamily B, and includes the D,D-dipeptidases VanXYg and VanXYe.


Pssm-ID: 350623 [Multi-domain]  Cd Length: 127  Bit Score: 119.68  E-value: 3.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610 104 LRKPAAQALEELFRDAEKEGiSLLGVSGYRSHERQKELFAFYAKRDGEEQARTYSAYPGTSEHETGLAIDVTGGSG---- 179
Cdd:cd14849    1 LEKEVARQLKKLLEAIGGED-EIVPVSGYRSKEEQTAIYDDSLNENGEEFTEKYVALPGHSEHQTGLAIDLGLNKKdidf 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 502822610 180 MCAAadcFADTPEAHWLSKNAYQYGFIIRYPEGEEQVTGYKYEPWHLRYVG 230
Cdd:cd14849   80 ICPS---FPDSGICDLFREQAADYGFIERYPKDKEEITGISYEPWHFRYVG 127
Peptidase_M15 cd14814
Metalloproteases including zinc D-Ala-D-Ala carboxypeptidase, L-Ala-D-Glu peptidase, L, ...
 106-229 5.23e-29

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: 105.60  E-value: 5.23e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610 106 KPAAQALEELFRDAEKEGISLLGVSGYRSHERQKELFAFYAKRDGEeqaRTYSAYPGTSEHETGLAIDVTGGSGmcaaad 185
Cdd:cd14814    1 PDAAEALARMIAAAGAEGRTLTINSGYRTYAQQLRLFAAKGKGSGG---RRWAAPPGTSNHQWGLAIDLGDGGG------ 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 502822610 186 cFADTPEAHWLSKNAYQYGFiiRYPEGEEQVtGYKYEPWHLRYV 229
Cdd:cd14814   72 -WRETQGYRWLKANAPRYGF--DNPGGARRG-GAFQEPWHWEYV 111
DD-carboxypeptidase_like cd14847
Uncharacterized proteins of the MEROPS peptidase family M15, subfamily B; This family of ...
 104-228 6.32e-19

Uncharacterized proteins of the MEROPS peptidase family M15, subfamily B; This family of uncharacterized proteins similar to D-Ala-D-Ala carboxypeptidase pdcA (Myxococcus-type) are zinc-binding enzymes that belong to the peptidase M15 subfamily B. The enzyme D-Ala-D-Ala carbozypeptidase catalyzes carboxypeptidation reactions involved in bacterial cell wall metabolism.


Pssm-ID: 350622  Cd Length: 162  Bit Score: 80.70  E-value: 6.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610 104 LRKPAAQALEELFRDAEKEGISLLGVSGYRSHERQKELF--AFYAKR---------------DGEEQAR---TYSAYPGT 163
Cdd:cd14847    1 LHPDAAEAFLALQAAAAKDGFDLQIASSFRSFERQLAIWnrKWSGERpvlddngqpldisslSPEEKIHailRWSALPGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610 164 SEHETGLAIDV------------------TGGSGMCAaadcfadtPEAHWLSKNAYQYGFIIRYpegEEQVTGYKYEPWH 225
Cdd:cd14847   81 SRHHWGTDIDVydanalpagyqlqltpseYEEGGPFA--------KLYQWLDENAAKFGFFRPY---TQDRGGVAPEPWH 149


                 ...
gi 502822610 226 LRY 228
Cdd:cd14847  150 LSY 152
Peptidase_M15_like cd14846
Uncharacterized family of the peptidase family M15, subfamily B; This family of ...
 109-225 1.49e-10

Uncharacterized family of the peptidase family M15, subfamily B; This family of uncharacterized proteins, similar to endolysin lys (Clavibacter phage CMP1) and VanYn peptidase, are zinc-binding enzymes that belong to the peptidase M15 subfamily B, involved in bacterial cell wall metabolism.


Pssm-ID: 350621  Cd Length: 104  Bit Score: 56.55  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610 109 AQALEELFRDAEKEGISLLGVSGYRSHERQKELFAFYAKRDG-EEQARTYSAYPGTSEHETGLAIDVTGGSGMcaaadcf 187
Cdd:cd14846    6 LAALTAAATAAAADGVTLRITSGWRSPAEQQRLLDDAVRTYGsEEEARRWVAPPEDSAHVTGEAVDIGPADAA------- 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 502822610 188 adtpeaHWLSKNAYQYGFIirypegeeQVtgYKYEPWH 225
Cdd:cd14846   79 ------QWLERHGARYGLC--------RI--YANEWWH 100
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 ...
 109-174 2.76e-09

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: 53.91  E-value: 2.76e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502822610 109 AQALEELFRDAEKEGISLLGVSGYRSHERQKELFAfyAKRDGEEQARTYsAYPGTSEHETGLAIDV 174
Cdd:cd14845   13 RAVVKELIELAEEEGIDFRITEGYRSPARQAALYA--QGRTKPGLIVTN-ARGGQSYHNYGLAVDI 75
D-Ala-D-Ala_dipeptidase_like cd14843
D-Ala-D-Ala dipeptidase, includes uncharacterized enzymes; This subfamily of D-Ala-D-Ala ...
 110-175 3.44e-05

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: 43.05  E-value: 3.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610 110 QALEELfrdaeKEGISLLGVSGYRSHERQKELFAFYAKR-----------DGEEQARTYSAYPGTSE-----HETGLAID 173
Cdd:cd14843   11 QAQSLL-----PKGLRLLIFDGYRPLAVQKFLFERYYQKirkrhpgrspeELIEEVRKFVAPPSKDPltpppHSTGGAVD 85


                 ..
gi 502822610 174 VT 175
Cdd:cd14843   86 LT 87
D-Ala-D-Ala_dipeptidase_Aad cd14840
D-Ala-D-Ala dipeptidase (includes Lactobacillus plantarum Aad peptidase); D-Ala-D-Ala ...
 85-175 6.91e-03

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: 36.25  E-value: 6.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822610  85 DLVYADVPFIFNEKIEKRM---LRKPAAQALEELFRDAEKEGISLLGVSGYRSHERQKELFAFYAKRDgeeqartYSAYP 161
Cdd:cd14840    1 DLRYATTDNFTGKKLYPSArayLRKEAAEKLAKAQKELKKPGYRLKIFDAYRPLSVQKKLWEAVPDPR-------YVANP 73

                         90
                 ....*....|....*
gi 502822610 162 GT-SEHETGLAIDVT 175
Cdd:cd14840   74 AKgSRHNRGAAVDLT 88
 
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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