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Conserved domains on  [gi|87082022|gb|AAC75071|]
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D-alanyl-D-alanine carboxypeptidase DacD [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

serine-type D-Ala-D-Ala carboxypeptidase DacD( domain architecture ID 11485336)

serine-type D-Ala-D-Ala carboxypeptidase DacD 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
dacD PRK11397
serine-type D-Ala-D-Ala carboxypeptidase DacD;
1-388 0e+00

serine-type D-Ala-D-Ala carboxypeptidase DacD;


:

Pssm-ID: 183117 [Multi-domain]  Cd Length: 388  Bit Score: 854.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022    1 MKRRLIIAASLFVFNLSSGFAAENIPFSPQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80
Cdd:PRK11397   1 LKRRLIIAASLFAFNLSSAFAAENIPFSPQPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022   81 RITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLH 160
Cdd:PRK11397  81 RITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022  161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAG 240
Cdd:PRK11397 161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022  241 FNLIASAVDGQRRLIAVVMGADSAKGREEEARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLP 320
Cdd:PRK11397 241 FNLIASAVDGQRRLIAVVMGADSAKGREEQARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLP 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 87082022  321 KAEIPHIKAKYTLDGKELTAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGSMFSRLSDYFHHKA 388
Cdd:PRK11397 321 KAEIPHIKAKYVLDGKELEAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGGMFSRLSDYFHHKA 388
 
Name Accession Description Interval E-value
dacD PRK11397
serine-type D-Ala-D-Ala carboxypeptidase DacD;
1-388 0e+00

serine-type D-Ala-D-Ala carboxypeptidase DacD;


Pssm-ID: 183117 [Multi-domain]  Cd Length: 388  Bit Score: 854.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022    1 MKRRLIIAASLFVFNLSSGFAAENIPFSPQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80
Cdd:PRK11397   1 LKRRLIIAASLFAFNLSSAFAAENIPFSPQPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022   81 RITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLH 160
Cdd:PRK11397  81 RITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022  161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAG 240
Cdd:PRK11397 161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022  241 FNLIASAVDGQRRLIAVVMGADSAKGREEEARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLP 320
Cdd:PRK11397 241 FNLIASAVDGQRRLIAVVMGADSAKGREEQARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLP 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 87082022  321 KAEIPHIKAKYTLDGKELTAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGSMFSRLSDYFHHKA 388
Cdd:PRK11397 321 KAEIPHIKAKYVLDGKELEAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGGMFSRLSDYFHHKA 388
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
1-379 1.06e-139

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


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 400.75  E-value: 1.06e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022   1 MKRRLIIAASLFVFNLSSGfaaenipfSPQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80
Cdd:COG1686   1 MKKLLLLALLLLLAAAAAA--------PAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022  81 RITPDDIVTVGRDAWAkdnpvfVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLH 160
Cdd:COG1686  73 KISLDDKVTVSEEAAR------TGGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELG 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022 161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWN---GITQQNRNGLLWdKTMNVDGLKTGHTS 237
Cdd:COG1686 147 MTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLG-RYPGVDGLKTGYTD 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022 238 GAGFNLIASAVDGQRRLIAVVMGADSAKGREEEARKLLRWGqqnfttvqilhrgkkvgteriwygdkenidlgteqefwm 317
Cdd:COG1686 226 AAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYG--------------------------------------- 266

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 87082022 318 vLPKAEipHIKAKYTLDGkELTAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGSMFSR 379
Cdd:COG1686 267 -FPKGE--ALKAEVVLDG-PLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
29-262 1.55e-131

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 376.34  E-value: 1.55e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022    29 PQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAWAKDNPvfvGSSLM 108
Cdd:pfam00768   1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNP---GSSNI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022   109 FLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLHLKDTHFETVHGLDAPGQHSSAYDLAVLS 188
Cdd:pfam00768  78 FLKPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 87082022   189 RAIIHGEPEFYHMYSEKSLTW---NGITQQNRNGLLWDKTMNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGAD 262
Cdd:pfam00768 158 KALIKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
PBP4_Staph NF038258
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ...
 46-261 2.11e-30

penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), as the name is used in Staphylococcus aureus and related species from the same genus. PBP4 is not essential. It has transpeptidase activity, provides low level beta-lactam resistance, and in mutant strains can contribute to high level beta-lactam resistance.


Pssm-ID: 468436 [Multi-domain]  Cd Length: 365  Bit Score: 119.70  E-value: 2.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022   46 TGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTV-GRDAWAKDNPvfvGSSLMFLKEGDRVSVRDLSRG 124
Cdd:NF038258  49 TGQILYDYHGNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKItSDYEKMSTLP---NLSTFPLKPGQTYTIKELLKQ 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022  125 LIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLHLKDTHFETVHGLD-------APGQ-------HSSAYDLAVLSRA 190
Cdd:NF038258 126 TALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGADnnllkpyAPKKykdetksKSTAKDMAILSQH 205

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 87082022  191 IIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTM---NVDGLKTGhTSGAGFNLIASAVDGQRRLIAVVMGA 261
Cdd:NF038258 206 LIKKHPKILKYTKLTADTQHGVTLYTTNLSLPGQPMslkGTDGLKTG-TSDEGYNLALTTKRDGLRINQVIMNV 278
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 282-373 3.68e-26

Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.


Pssm-ID: 198004 [Multi-domain]  Cd Length: 92  Bit Score: 100.37  E-value: 3.68e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022    282 FTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLPKAEIPHIKAKYTLDGKELTAPISAHQRVGEIELYDRDKQVA 361
Cdd:smart00936   1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVTLDGKLIG 80

                           90
                   ....*....|..
gi 87082022    362 HWPLVTLESVGE 373
Cdd:smart00936  81 EVPLVALEDVEK 92
 
Name Accession Description Interval E-value
dacD PRK11397
serine-type D-Ala-D-Ala carboxypeptidase DacD;
1-388 0e+00

serine-type D-Ala-D-Ala carboxypeptidase DacD;


Pssm-ID: 183117 [Multi-domain]  Cd Length: 388  Bit Score: 854.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022    1 MKRRLIIAASLFVFNLSSGFAAENIPFSPQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80
Cdd:PRK11397   1 LKRRLIIAASLFAFNLSSAFAAENIPFSPQPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022   81 RITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLH 160
Cdd:PRK11397  81 RITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022  161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAG 240
Cdd:PRK11397 161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022  241 FNLIASAVDGQRRLIAVVMGADSAKGREEEARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLP 320
Cdd:PRK11397 241 FNLIASAVDGQRRLIAVVMGADSAKGREEQARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLP 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 87082022  321 KAEIPHIKAKYTLDGKELTAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGSMFSRLSDYFHHKA 388
Cdd:PRK11397 321 KAEIPHIKAKYVLDGKELEAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGGMFSRLSDYFHHKA 388
PRK10793 PRK10793
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
 6-386 1.60e-155

D-alanyl-D-alanine carboxypeptidase fraction A; Provisional


Pssm-ID: 182736 [Multi-domain]  Cd Length: 403  Bit Score: 443.91  E-value: 1.60e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022    6 IIAASLFVFNLSSGFAAENIPFS---PQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRI 82
Cdd:PRK10793  13 LALTTALCTAFISAAHADDLNIKtmiPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022   83 TPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLHLK 162
Cdd:PRK10793  93 KETDLVTVGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLK 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022  163 DTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAGFN 242
Cdd:PRK10793 173 NTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYN 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022  243 LIASAVDGQRRLIAVVMGADSAKGREEEARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLPKA 322
Cdd:PRK10793 253 LVASATEGQMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRG 332

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 87082022  323 EIPHIKAKYTLDGKELTAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGSMFSRLSDY----FHH 386
Cdd:PRK10793 333 RMKDLKASYVLNTSELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYiklmFHH 400
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
3-385 2.56e-145

serine-type D-Ala-D-Ala carboxypeptidase;


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 417.86  E-value: 2.56e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022    3 RRLIIAASLFVF-NLSSGFAAENIPfspQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHR 81
Cdd:PRK10001   8 LRGLAAGSAFLFlFAPTAFAAEQTV---EAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022   82 ITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLHL 161
Cdd:PRK10001  85 IKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022  162 KDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAGF 241
Cdd:PRK10001 165 TNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTAGAGY 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022  242 NLIASAVDGQRRLIAVVMGADSAKGREEEARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLPK 321
Cdd:PRK10001 245 NLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIPR 324

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 87082022  322 AEIPHIKAKYTLDGKELTAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGSMFSRLSDY----FH 385
Cdd:PRK10001 325 GQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFvmmkFH 392
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
1-379 1.06e-139

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


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 400.75  E-value: 1.06e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022   1 MKRRLIIAASLFVFNLSSGfaaenipfSPQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80
Cdd:COG1686   1 MKKLLLLALLLLLAAAAAA--------PAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022  81 RITPDDIVTVGRDAWAkdnpvfVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLH 160
Cdd:COG1686  73 KISLDDKVTVSEEAAR------TGGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELG 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022 161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWN---GITQQNRNGLLWdKTMNVDGLKTGHTS 237
Cdd:COG1686 147 MTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLG-RYPGVDGLKTGYTD 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022 238 GAGFNLIASAVDGQRRLIAVVMGADSAKGREEEARKLLRWGqqnfttvqilhrgkkvgteriwygdkenidlgteqefwm 317
Cdd:COG1686 226 AAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYG--------------------------------------- 266

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 87082022 318 vLPKAEipHIKAKYTLDGkELTAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGSMFSR 379
Cdd:COG1686 267 -FPKGE--ALKAEVVLDG-PLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
29-262 1.55e-131

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 376.34  E-value: 1.55e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022    29 PQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAWAKDNPvfvGSSLM 108
Cdd:pfam00768   1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNP---GSSNI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022   109 FLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLHLKDTHFETVHGLDAPGQHSSAYDLAVLS 188
Cdd:pfam00768  78 FLKPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 87082022   189 RAIIHGEPEFYHMYSEKSLTW---NGITQQNRNGLLWDKTMNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGAD 262
Cdd:pfam00768 158 KALIKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
PBP4_Staph NF038258
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ...
 46-261 2.11e-30

penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), as the name is used in Staphylococcus aureus and related species from the same genus. PBP4 is not essential. It has transpeptidase activity, provides low level beta-lactam resistance, and in mutant strains can contribute to high level beta-lactam resistance.


Pssm-ID: 468436 [Multi-domain]  Cd Length: 365  Bit Score: 119.70  E-value: 2.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022   46 TGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTV-GRDAWAKDNPvfvGSSLMFLKEGDRVSVRDLSRG 124
Cdd:NF038258  49 TGQILYDYHGNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKItSDYEKMSTLP---NLSTFPLKPGQTYTIKELLKQ 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022  125 LIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLHLKDTHFETVHGLD-------APGQ-------HSSAYDLAVLSRA 190
Cdd:NF038258 126 TALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGADnnllkpyAPKKykdetksKSTAKDMAILSQH 205

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 87082022  191 IIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTM---NVDGLKTGhTSGAGFNLIASAVDGQRRLIAVVMGA 261
Cdd:NF038258 206 LIKKHPKILKYTKLTADTQHGVTLYTTNLSLPGQPMslkGTDGLKTG-TSDEGYNLALTTKRDGLRINQVIMNV 278
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 282-373 3.68e-26

Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.


Pssm-ID: 198004 [Multi-domain]  Cd Length: 92  Bit Score: 100.37  E-value: 3.68e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022    282 FTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLPKAEIPHIKAKYTLDGKELTAPISAHQRVGEIELYDRDKQVA 361
Cdd:smart00936   1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVTLDGKLIG 80

                           90
                   ....*....|..
gi 87082022    362 HWPLVTLESVGE 373
Cdd:smart00936  81 EVPLVALEDVEK 92
PBP5_C pfam07943
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 282-373 9.43e-23

Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.


Pssm-ID: 429749 [Multi-domain]  Cd Length: 91  Bit Score: 91.12  E-value: 9.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022   282 FTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLPKAEIPHIKAKYTLDgKELTAPISAHQRVGEIELYDRDKQVA 361
Cdd:pfam07943   1 FETKKLYKKGDVVKKVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLK-KPLEAPIKKGQVVGKLEVYLDGKLIG 79

                          90
                  ....*....|..
gi 87082022   362 HWPLVTLESVGE 373
Cdd:pfam07943  80 EVPLVAKEDVEE 91
pbpG PRK11669
D-alanyl-D-alanine endopeptidase; Provisional
 1-261 8.74e-18

D-alanyl-D-alanine endopeptidase; Provisional


Pssm-ID: 236952  Cd Length: 306  Bit Score: 83.19  E-value: 8.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022    1 MKRRLIIAASLFVFN----LSSGFAAEN-IPFSPQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVdr 75
Cdd:PRK11669   1 MKFRVSLLSLLLLLAgvpfAPQAVAKTAaATTASQPQEIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVV-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022   76 aIDSHrITPDDIVTVGrdawAKDNPVFVGsslMF--LKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMN 153
Cdd:PRK11669  79 -LDAK-LPLDEKLKVD----ISQTPEMKG---VYsrVRLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMN 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022  154 NYAEKLHLKDTHFETVHGLdAPGQHSSAYDLAVLSRAiihgePEFYHMYSEKSLT----------WNGITQQNRNGLLWD 223
Cdd:PRK11669 150 AKAKALGMTNTRYVEPTGL-SIHNVSTARDLTKLLIA-----SKQYPLIGQLSTTrektatfrkpNYTLPFRNTNHLVYR 223

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 87082022  224 KTMNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGA 261
Cdd:PRK11669 224 DNWNIQLTKTGFTNAAGHCLVMRTVINNRPVALVVLDA 261
PenP COG2367
Beta-lactamase class A [Defense mechanisms];
38-195 2.88e-07

Beta-lactamase class A [Defense mechanisms];


Pssm-ID: 441934 [Multi-domain]  Cd Length: 276  Bit Score: 51.44  E-value: 2.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022  38 SWVLMDYTTGQILTAgNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAWAKDNPVfvgssLMFLKEGDRVS 117
Cdd:COG2367  36 GVYVLDLDTGETVGI-NADERFPAASTFKLPVLAAVLRQVDAGKLSLDERVTLTPEDLVGGSGI-----LQKLPDGTGLT 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022 118 VRDLSRGLIVDSGNDACVALADYIaGGQRqfvemMNNYAEKLHLKDTHFE-TVHGL-DAPGQH---SSAYDLAVLSRAII 192
Cdd:COG2367 110 LRELAELMITVSDNTATNLLLRLL-GPDA-----VNAFLRSLGLTDTRLDrKEPDLnELPGDGrntTTPRDMARLLAALY 183


                ...
gi 87082022 193 HGE 195
Cdd:COG2367 184 RGE 186
Beta-lactamase2 pfam13354
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ...
 38-195 2.77e-06

Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is closely related to Beta-lactamase, pfam00144, the serine beta-lactamase-like superfamily, which contains the distantly related pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.


Pssm-ID: 463854 [Multi-domain]  Cd Length: 215  Bit Score: 47.65  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022    38 SWVLMDYTTGQILtAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDawakdnpVFVGSSLMF--LKEGDR 115
Cdd:pfam13354   1 GIYVRDLDTGEEL-GINGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTAE-------DKVGGSGILqyLPDGSQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87082022   116 VSVRDLSRGLIVDSGNDACVALADYIAggqrqfVEMMNNYAEKLHLKDTHFE----TVHGLDAPGQH-SSAYDLAVLSRA 190
Cdd:pfam13354  73 LSLRDLLTLMIAVSDNTATNLLIDRLG------LEAVNARLRALGLRDTRLRrklpDLRAADKGGTNtTTARDMAKLLEA 146


                  ....*
gi 87082022   191 IIHGE 195
Cdd:pfam13354 147 LYRGE 151
 
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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