NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|815845761|ref|WP_046467230|]
View 

MULTISPECIES: M15 family metallopeptidase [Staphylococcus]

Protein Classification

M15 family metallopeptidase( domain architecture ID 13000893)

M15 family metallopeptidase of the zinc-binding metallopeptidase family, which contains mostly carboxypeptidases and dipeptidases, is involved in bacterial cell wall biosynthesis and metabolism

EC:  3.4.17.-
Gene Ontology:  GO:0008233|GO:0016787|GO:0006508
PubMed:  15044722

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LD-carboxypeptidase cd14852
L,D-carboxypeptidase DacB and LdcB, and related proteins; This L,D-carboxypeptidase family ...
 54-202 6.12e-72

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: 215.96  E-value: 6.12e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761  54 LIVNKQIKLPKDFNP-------------GENPKAVRALNKMMTDAKKDNIQLYKISGFRSYQTQVQLFNNYKARDGEKAA 120
Cdd:cd14852    1 VLVNKDHPLPEDYVPedlvpyvlldnglYLRKEAAEALEEMFDAAKKDGIDLTIVSGYRSYEYQQELYNNYVARYGKEEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761 121 NKYSSKPGHSEHQTGLSFDVGAQGSDkNLYRSFGKTKEGKWIKKHAADYGFIVRYGKHKENETGYQYEPWHLRYLGKDKA 200
Cdd:cd14852   81 DRYSARPGYSEHQTGLAVDIGSTDGP-CLEESFEDTPAGKWLAENAHKYGFILRYPKGKENITGYSYEPWHFRYVGKEAA 159


                 ..
gi 815845761 201 KK 202
Cdd:cd14852  160 KK 161
 
Name Accession Description Interval E-value
LD-carboxypeptidase cd14852
L,D-carboxypeptidase DacB and LdcB, and related proteins; This L,D-carboxypeptidase family ...
 54-202 6.12e-72

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: 215.96  E-value: 6.12e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761  54 LIVNKQIKLPKDFNP-------------GENPKAVRALNKMMTDAKKDNIQLYKISGFRSYQTQVQLFNNYKARDGEKAA 120
Cdd:cd14852    1 VLVNKDHPLPEDYVPedlvpyvlldnglYLRKEAAEALEEMFDAAKKDGIDLTIVSGYRSYEYQQELYNNYVARYGKEEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761 121 NKYSSKPGHSEHQTGLSFDVGAQGSDkNLYRSFGKTKEGKWIKKHAADYGFIVRYGKHKENETGYQYEPWHLRYLGKDKA 200
Cdd:cd14852   81 DRYSARPGYSEHQTGLAVDIGSTDGP-CLEESFEDTPAGKWLAENAHKYGFILRYPKGKENITGYSYEPWHFRYVGKEAA 159


                 ..
gi 815845761 201 KK 202
Cdd:cd14852  160 KK 161
LdcB COG1876
LD-carboxypeptidase LdcB, LAS superfamily [Cell wall/membrane/envelope biogenesis];
55-215 8.56e-72

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


Pssm-ID: 441480  Cd Length: 168  Bit Score: 215.52  E-value: 8.56e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761  55 IVNKQIKLPKDF-------NPGENPKAVRALNKMMTDAKKDNIQLYKISGFRSYQTQVQLFNNYKARDGEKAANKYSSKP 127
Cdd:COG1876    1 LVNKDHPLPADDlvplpggGHRLRKEAAAAFEAMQAAAKKDGIDLVIVSGYRSYERQEALYNRKVARYGIEAALRYSAPP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761 128 GHSEHQTGLSFDVGAQGSDKNLYRSFGKTKEGKWIKKHAADYGFIVRYGKHKENETGYQYEPWHLRYLGKDKAKKVKQSG 207
Cdd:COG1876   81 GTSEHHTGLAIDIGDPDPGTDLEEEFEETPAGKWLAANAAKYGFILRYPKGKEDITGYAYEPWHWRYVGVEAAKEIFEKG 160


                 ....*...
gi 815845761 208 KSLESYLG 215
Cdd:COG1876  161 LTLEEYLG 168
LD_carboxy_LdcB NF041194
LD-carboxypeptidase LdcB/DacB;
51-216 1.66e-61

LD-carboxypeptidase LdcB/DacB;


Pssm-ID: 469098  Cd Length: 180  Bit Score: 189.94  E-value: 1.66e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761  51 DGILIVNKQIKLPKDFNPGENPKAVRALNKMMTDAKKdniQLYKIS----GFRSYQTQVQLFNNYKARDGEKAANKYSSK 126
Cdd:NF041194  15 DEIIIVNKHYPLSKDYNPGENPTAKAALLQLIADMQA---AGYPISdqysGFRSYETQTELYQNYVNQDGKEAADRYSAR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761 127 PGHSEHQTGLSFDVgaQGSDKNLYRsfgKTKEGKWIKKHAADYGFIVRYGKHKENETGYQYEPWHLRYLGKDkAKKVKQS 206
Cdd:NF041194  92 PGYSEHQTGLAFDL--IDTSGNLLE---EPKASQWLLDHAADYGFIVRYLKGKEASTGYMPESWHLRYIGKE-AKEIADS 165

                        170
                 ....*....|
gi 815845761 207 GKSLESYLGL 216
Cdd:NF041194 166 GLSLEEYYGF 175
VanY pfam02557
D-alanyl-D-alanine carboxypeptidase;
71-197 2.48e-52

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 426830 [Multi-domain]  Cd Length: 131  Bit Score: 165.10  E-value: 2.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761   71 NPKAVRALNKMMTDAKKDNIQLYKISGFRSYQTQVQLFNNYKARDGEKAANKYSSKPGHSEHQTGLSFDVGAQGSDKNLY 150
Cdd:pfam02557   5 RKEAAEALEELFAAAKKEGINLRAISGFRSYEYQEALFKKYVKGEGKKAILRWSAPPGTSEHHTGLAIDIGDPDNPWELE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 815845761  151 RSFGKTKEGKWIKKHAADYGFIVRYGKHKENETGYQYEPWHLRYLGK 197
Cdd:pfam02557  85 ESFEDTAAFKWLQANAHKYGFVLRYPKGKEQITGVSYEPWHWRYVGI 131
 
Name Accession Description Interval E-value
LD-carboxypeptidase cd14852
L,D-carboxypeptidase DacB and LdcB, and related proteins; This L,D-carboxypeptidase family ...
 54-202 6.12e-72

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: 215.96  E-value: 6.12e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761  54 LIVNKQIKLPKDFNP-------------GENPKAVRALNKMMTDAKKDNIQLYKISGFRSYQTQVQLFNNYKARDGEKAA 120
Cdd:cd14852    1 VLVNKDHPLPEDYVPedlvpyvlldnglYLRKEAAEALEEMFDAAKKDGIDLTIVSGYRSYEYQQELYNNYVARYGKEEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761 121 NKYSSKPGHSEHQTGLSFDVGAQGSDkNLYRSFGKTKEGKWIKKHAADYGFIVRYGKHKENETGYQYEPWHLRYLGKDKA 200
Cdd:cd14852   81 DRYSARPGYSEHQTGLAVDIGSTDGP-CLEESFEDTPAGKWLAENAHKYGFILRYPKGKENITGYSYEPWHFRYVGKEAA 159


                 ..
gi 815845761 201 KK 202
Cdd:cd14852  160 KK 161
LdcB COG1876
LD-carboxypeptidase LdcB, LAS superfamily [Cell wall/membrane/envelope biogenesis];
55-215 8.56e-72

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


Pssm-ID: 441480  Cd Length: 168  Bit Score: 215.52  E-value: 8.56e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761  55 IVNKQIKLPKDF-------NPGENPKAVRALNKMMTDAKKDNIQLYKISGFRSYQTQVQLFNNYKARDGEKAANKYSSKP 127
Cdd:COG1876    1 LVNKDHPLPADDlvplpggGHRLRKEAAAAFEAMQAAAKKDGIDLVIVSGYRSYERQEALYNRKVARYGIEAALRYSAPP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761 128 GHSEHQTGLSFDVGAQGSDKNLYRSFGKTKEGKWIKKHAADYGFIVRYGKHKENETGYQYEPWHLRYLGKDKAKKVKQSG 207
Cdd:COG1876   81 GTSEHHTGLAIDIGDPDPGTDLEEEFEETPAGKWLAANAAKYGFILRYPKGKEDITGYAYEPWHWRYVGVEAAKEIFEKG 160


                 ....*...
gi 815845761 208 KSLESYLG 215
Cdd:COG1876  161 LTLEEYLG 168
LD_carboxy_LdcB NF041194
LD-carboxypeptidase LdcB/DacB;
51-216 1.66e-61

LD-carboxypeptidase LdcB/DacB;


Pssm-ID: 469098  Cd Length: 180  Bit Score: 189.94  E-value: 1.66e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761  51 DGILIVNKQIKLPKDFNPGENPKAVRALNKMMTDAKKdniQLYKIS----GFRSYQTQVQLFNNYKARDGEKAANKYSSK 126
Cdd:NF041194  15 DEIIIVNKHYPLSKDYNPGENPTAKAALLQLIADMQA---AGYPISdqysGFRSYETQTELYQNYVNQDGKEAADRYSAR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761 127 PGHSEHQTGLSFDVgaQGSDKNLYRsfgKTKEGKWIKKHAADYGFIVRYGKHKENETGYQYEPWHLRYLGKDkAKKVKQS 206
Cdd:NF041194  92 PGYSEHQTGLAFDL--IDTSGNLLE---EPKASQWLLDHAADYGFIVRYLKGKEASTGYMPESWHLRYIGKE-AKEIADS 165

                        170
                 ....*....|
gi 815845761 207 GKSLESYLGL 216
Cdd:NF041194 166 GLSLEEYYGF 175
VanY pfam02557
D-alanyl-D-alanine carboxypeptidase;
71-197 2.48e-52

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 426830 [Multi-domain]  Cd Length: 131  Bit Score: 165.10  E-value: 2.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761   71 NPKAVRALNKMMTDAKKDNIQLYKISGFRSYQTQVQLFNNYKARDGEKAANKYSSKPGHSEHQTGLSFDVGAQGSDKNLY 150
Cdd:pfam02557   5 RKEAAEALEELFAAAKKEGINLRAISGFRSYEYQEALFKKYVKGEGKKAILRWSAPPGTSEHHTGLAIDIGDPDNPWELE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 815845761  151 RSFGKTKEGKWIKKHAADYGFIVRYGKHKENETGYQYEPWHLRYLGK 197
Cdd:pfam02557  85 ESFEDTAAFKWLQANAHKYGFVLRYPKGKEQITGVSYEPWHWRYVGI 131
DD-dipeptidase_VanXYc cd14849
D-Ala-D-Ala dipeptidase/D-Ala-D-Ala carboxypeptidase (VanXYc) and related proteins; VanXYc ...
 71-196 1.59e-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: 119.29  E-value: 1.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761  71 NPKAVRALNKMMTDAKKDNiQLYKISGFRSYQTQVQLFNNYKARDGEKAANKYSSKPGHSEHQTGLSFDVGAQGSDKNLY 150
Cdd:cd14849    2 EKEVARQLKKLLEAIGGED-EIVPVSGYRSKEEQTAIYDDSLNENGEEFTEKYVALPGHSEHQTGLAIDLGLNKKDIDFI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 815845761 151 R-SFGKTKEGKWIKKHAADYGFIVRYGKHKENETGYQYEPWHLRYLG 196
Cdd:cd14849   81 CpSFPDSGICDLFREQAADYGFIERYPKDKEEITGISYEPWHFRYVG 127
Peptidase_M15 cd14814
Metalloproteases including zinc D-Ala-D-Ala carboxypeptidase, L-Ala-D-Glu peptidase, L, ...
 72-194 6.89e-24

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: 91.73  E-value: 6.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761  72 PKAVRALNKMMTDAKKDNIQLYKISGFRSYQTQVQLFNNYKARDGEKaanKYSSKPGHSEHQTGLSFDVGaqgsdknLYR 151
Cdd:cd14814    1 PDAAEALARMIAAAGAEGRTLTINSGYRTYAQQLRLFAAKGKGSGGR---RWAAPPGTSNHQWGLAIDLG-------DGG 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 815845761 152 SFGKTKEGKWIKKHAADYGFIVRYGKhkeNETGYQYEPWHLRY 194
Cdd:cd14814   71 GWRETQGYRWLKANAPRYGFDNPGGA---RRGGAFQEPWHWEY 110
DD-carboxypeptidase_like cd14847
Uncharacterized proteins of the MEROPS peptidase family M15, subfamily B; This family of ...
 72-195 2.41e-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: 81.08  E-value: 2.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761  72 PKAVRALNKMMTDAKKDNIQLYKISGFRSYQTQVQLFNNyKAR-------------------DGEKAAN--KYSSKPGHS 130
Cdd:cd14847    3 PDAAEAFLALQAAAAKDGFDLQIASSFRSFERQLAIWNR-KWSgerpvlddngqpldisslsPEEKIHAilRWSALPGAS 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815845761 131 EHQTGLSFDV---GAQGSDKNL------YRSFGK-TKEGKWIKKHAADYGFIVRYgkhKENETGYQYEPWHLRYL 195
Cdd:cd14847   82 RHHWGTDIDVydaNALPAGYQLqltpseYEEGGPfAKLYQWLDENAAKFGFFRPY---TQDRGGVAPEPWHLSYA 153
Peptidase_M15_like cd14846
Uncharacterized family of the peptidase family M15, subfamily B; This family of ...
 72-191 3.63e-07

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: 46.92  E-value: 3.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761  72 PKAVRALNKMMTDAKKDNIQLYKISGFRSYQTQVQLFNNYKARDG-EKAANKYSSKPGHSEHQTGLSFDVGAQGSDknly 150
Cdd:cd14846    3 PALLAALTAAATAAAADGVTLRITSGWRSPAEQQRLLDDAVRTYGsEEEARRWVAPPEDSAHVTGEAVDIGPADAA---- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 815845761 151 rsfgktkegKWIKKHAADYGfIVRYgkhkenetgYQYEPWH 191
Cdd:cd14846   79 ---------QWLERHGARYG-LCRI---------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 ...
 71-167 4.26e-07

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: 47.36  E-value: 4.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845761  71 NPKAVRALNKMMTDAKKDNIQLYKISGFRSYQTQVQLFNNYKARDGEKAANkysSKPGHSEHQTGLSFDVGAqgsDKNLY 150
Cdd:cd14845    9 HPEVRAVVKELIELAEEEGIDFRITEGYRSPARQAALYAQGRTKPGLIVTN---ARGGQSYHNYGLAVDIVP---LVNGK 82

                         90
                 ....*....|....*....
gi 815845761 151 RSFGK--TKEGKWIKKHAA 167
Cdd:cd14845   83 LSTGGadPWVSKAYQKLGE 101
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH