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Conserved domains on  [gi|517987028|ref|WP_019157236|]
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D-alanyl-D-alanine carboxypeptidase family protein [Robertmurraya massiliosenegalensis]

Protein Classification

D-alanyl-D-alanine carboxypeptidase family protein( domain architecture ID 11447584)

D-alanyl-D-alanine carboxypeptidase family protein may remove C-terminal D-alanyl residues from sugar-peptide cell wall precursors

CATH:  3.40.710.10
EC:  3.4.-.-
Gene Ontology:  GO:0008236|GO:0006508
MEROPS:  S11
SCOP:  3001604

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
1-429 2.66e-116

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


:

Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 343.74  E-value: 2.66e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028   1 MKKSFIqksivclLTFVLMigFIQKPAAAAENIDINANAVILIDAETGKILYEKNAETVLGIASMTKMMTEYLLLEAVKE 80
Cdd:COG1686    1 MKKLLL-------LALLLL--LAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  81 GKVKWDQTFTISPELSKMshddDLSNVYLRVDSAYTVEDLYSAMAIESANAATVAIAEIVAGSEANFVKLMNEKAEELGL 160
Cdd:COG1686   72 GKISLDDKVTVSEEAART----GGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGM 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 161 GDFKFVNSTGLNNrdlakhfpdvvggaeEENVMSARAVAKLAYQILKDFPEVLETSSIPEKTFAEGTKdrFVMDNWNWML 240
Cdd:COG1686  148 TNTHFVNPTGLPD---------------PGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNGRG--ITLRNTNRLL 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 241 egyrdiadrysyyqqFTYEGLDGLKTGSTNFAGFCFTGTASRDGVRYITVVMGTKSQTERFVETKKLLDFAfnnFSKEEL 320
Cdd:COG1686  211 ---------------GRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYG---FPKGEA 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 321 VPAEYVVKGTetvpvskgkedqvkvhsadaissivtpaeqenfdtvvkldkdklneegaLTAPIKKGDKIGTVTIQFkDG 400
Cdd:COG1686  273 LKAEVVLDGP-------------------------------------------------LKAPVKKGQVVGTLVVTL-DG 302
                        410       420
                 ....*....|....*....|....*....
gi 517987028 401 EAVYlssegqksmTVDLIAAENVEKANWF 429
Cdd:COG1686  303 KTIA---------EVPLVAAEDVEKAGFF 322
 
Name Accession Description Interval E-value
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
1-429 2.66e-116

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


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 343.74  E-value: 2.66e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028   1 MKKSFIqksivclLTFVLMigFIQKPAAAAENIDINANAVILIDAETGKILYEKNAETVLGIASMTKMMTEYLLLEAVKE 80
Cdd:COG1686    1 MKKLLL-------LALLLL--LAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  81 GKVKWDQTFTISPELSKMshddDLSNVYLRVDSAYTVEDLYSAMAIESANAATVAIAEIVAGSEANFVKLMNEKAEELGL 160
Cdd:COG1686   72 GKISLDDKVTVSEEAART----GGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGM 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 161 GDFKFVNSTGLNNrdlakhfpdvvggaeEENVMSARAVAKLAYQILKDFPEVLETSSIPEKTFAEGTKdrFVMDNWNWML 240
Cdd:COG1686  148 TNTHFVNPTGLPD---------------PGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNGRG--ITLRNTNRLL 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 241 egyrdiadrysyyqqFTYEGLDGLKTGSTNFAGFCFTGTASRDGVRYITVVMGTKSQTERFVETKKLLDFAfnnFSKEEL 320
Cdd:COG1686  211 ---------------GRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYG---FPKGEA 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 321 VPAEYVVKGTetvpvskgkedqvkvhsadaissivtpaeqenfdtvvkldkdklneegaLTAPIKKGDKIGTVTIQFkDG 400
Cdd:COG1686  273 LKAEVVLDGP-------------------------------------------------LKAPVKKGQVVGTLVVTL-DG 302
                        410       420
                 ....*....|....*....|....*....
gi 517987028 401 EAVYlssegqksmTVDLIAAENVEKANWF 429
Cdd:COG1686  303 KTIA---------EVPLVAAEDVEKAGFF 322
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
34-295 1.61e-81

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 251.54  E-value: 1.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028   34 DINANAVILIDAETGKILYEKNAETVLGIASMTKMMTEYLLLEAVKEGKVKWDQTFTISpELSKMSHDDDLSNVYLRVDS 113
Cdd:pfam00768   5 EIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTIS-EDAWATGNPGSSNIFLKPGS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  114 AYTVEDLYSAMAIESANAATVAIAEIVAGSEANFVKLMNEKAEELGLGDFKFVNSTGLNNrdlakhfpdvvggaeEENVM 193
Cdd:pfam00768  84 QVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDA---------------HGQYS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  194 SARAVAKLAYQILKDFPEVLETSSIPEKTFAEgtkdrfvMDNWNWMLEGyRDIADRYSYyqqftyegLDGLKTGSTNFAG 273
Cdd:pfam00768 149 SARDMAILAKALIKDLPEELSITKEKSFTFRG-------INKINQRNRN-GLLWDKTWN--------VDGLKTGYTNEAG 212
                         250       260
                  ....*....|....*....|..
gi 517987028  274 FCFTGTASRDGVRYITVVMGTK 295
Cdd:pfam00768 213 YCLVASATKGGMRLISVVMGAF 234
PBP4_Staph NF038258
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ...
13-295 1.77e-49

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: 172.47  E-value: 1.77e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  13 LLTFVLMIGFIQKPAAAAEN--IDI-------------NANAVILIdAETGKILYEKNAETVLGIASMTKMMTEYLLLEA 77
Cdd:NF038258   1 IVSLLLLSTIITPPASAAAEtpVEIanqegyqnlseqyNPEGAIVT-TQTGQILYDYHGNKKWDPASMTKLMTMYLTLEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  78 VKEGKVKWDQTFTISPELSKMSHDDDLSNVYLRVDSAYTVEDLYSAMAIESANAATVAIAEIVAGSEANFVKLMNEKAEE 157
Cdd:NF038258  80 IKKGKLSLNDKVKITSDYEKMSTLPNLSTFPLKPGQTYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 158 LGLGDFKFVNSTGLNNRdLAKHFPDVVGGAEEENVMSARAVAKLAYQILKDFPEVLETSSIPEKTfAEGTKdrfvMDNWN 237
Cdd:NF038258 160 LGMKHTHFTNPSGADNN-LLKPYAPKKYKDETKSKSTAKDMAILSQHLIKKHPKILKYTKLTADT-QHGVT----LYTTN 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 517987028 238 WMLEGyrdiadrysyyQQFTYEGLDGLKTGSTNfAGFCFTGTASRDGVRYITVVMGTK 295
Cdd:NF038258 234 LSLPG-----------QPMSLKGTDGLKTGTSD-EGYNLALTTKRDGLRINQVIMNVG 279
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
22-455 2.08e-46

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


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 165.17  E-value: 2.08e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  22 FIQKPAA-AAENI----DINANAVILIDAETGKILYEKNAETVLGIASMTKMMTEYLLLEAVKEGKVKWDQTFTI----- 91
Cdd:PRK10001  19 FLFAPTAfAAEQTveapSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVgkdaw 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  92 ---SPELSKMshdddlSNVYLRVDSAYTVEDLYSAMAIESANAATVAIAEIVAGSEANFVKLMNEKAEELGLGDFKFVNS 168
Cdd:PRK10001  99 atgNPALRGS------SVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTV 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 169 TGLnnrDLAKHFPdvvggaeeenvmSARAVAKLAYQILKDFPEvlETSSIPEKTFaegTKDRFVMDNWNWMLEGyrdiad 248
Cdd:PRK10001 173 HGL---DAPGQFS------------TARDMALLGKALIHDVPE--EYAIHKEKEF---TFNKIRQPNRNRLLWS------ 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 249 rysyyqqfTYEGLDGLKTGSTNFAGFCFTGTASRDGVRYITVVMGTKSQTERFVETKKLLDFAFNNFskEELVP----AE 324
Cdd:PRK10001 227 --------SNLNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFF--ETVTPikpdAT 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 325 YVvkgteTVPVSKGKEDQVKVHSADAISSIVTPAEQENFDTVVKLDkdklneEGALTAPIKKGDKIGTVTIQFKDgeavy 404
Cdd:PRK10001 297 FV-----TQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLT------EPQLTAPLKKGQVVGTIDFQLNG----- 360
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 517987028 405 lSSEGQKSmtvdLIAAENVEKanwfvlmmrgiGGFFGDLWGSVSSTVKGWF 455
Cdd:PRK10001 361 -KSIEQRP----LIVMENVEE-----------GGFFSRMWDFVMMKFHQWF 395
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
315-425 6.40e-14

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: 67.24  E-value: 6.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028   315 FSKEELVPAEYVVKgteTVPVSKGKEDQVKVHSADAISSIVTPAEQENFDTVVKLDKDKLNeegaltAPIKKGDKIGTVT 394
Cdd:smart00936   1 FETVKLYKKGQVVG---TVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELE------APIKKGQVVGTLV 71
                           90       100       110
                   ....*....|....*....|....*....|.
gi 517987028   395 IQfkdgeavylsSEGQKSMTVDLIAAENVEK 425
Cdd:smart00936  72 VT----------LDGKLIGEVPLVALEDVEK 92
 
Name Accession Description Interval E-value
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
1-429 2.66e-116

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


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 343.74  E-value: 2.66e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028   1 MKKSFIqksivclLTFVLMigFIQKPAAAAENIDINANAVILIDAETGKILYEKNAETVLGIASMTKMMTEYLLLEAVKE 80
Cdd:COG1686    1 MKKLLL-------LALLLL--LAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  81 GKVKWDQTFTISPELSKMshddDLSNVYLRVDSAYTVEDLYSAMAIESANAATVAIAEIVAGSEANFVKLMNEKAEELGL 160
Cdd:COG1686   72 GKISLDDKVTVSEEAART----GGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGM 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 161 GDFKFVNSTGLNNrdlakhfpdvvggaeEENVMSARAVAKLAYQILKDFPEVLETSSIPEKTFAEGTKdrFVMDNWNWML 240
Cdd:COG1686  148 TNTHFVNPTGLPD---------------PGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNGRG--ITLRNTNRLL 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 241 egyrdiadrysyyqqFTYEGLDGLKTGSTNFAGFCFTGTASRDGVRYITVVMGTKSQTERFVETKKLLDFAfnnFSKEEL 320
Cdd:COG1686  211 ---------------GRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYG---FPKGEA 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 321 VPAEYVVKGTetvpvskgkedqvkvhsadaissivtpaeqenfdtvvkldkdklneegaLTAPIKKGDKIGTVTIQFkDG 400
Cdd:COG1686  273 LKAEVVLDGP-------------------------------------------------LKAPVKKGQVVGTLVVTL-DG 302
                        410       420
                 ....*....|....*....|....*....
gi 517987028 401 EAVYlssegqksmTVDLIAAENVEKANWF 429
Cdd:COG1686  303 KTIA---------EVPLVAAEDVEKAGFF 322
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
34-295 1.61e-81

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 251.54  E-value: 1.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028   34 DINANAVILIDAETGKILYEKNAETVLGIASMTKMMTEYLLLEAVKEGKVKWDQTFTISpELSKMSHDDDLSNVYLRVDS 113
Cdd:pfam00768   5 EIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTIS-EDAWATGNPGSSNIFLKPGS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  114 AYTVEDLYSAMAIESANAATVAIAEIVAGSEANFVKLMNEKAEELGLGDFKFVNSTGLNNrdlakhfpdvvggaeEENVM 193
Cdd:pfam00768  84 QVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDA---------------HGQYS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  194 SARAVAKLAYQILKDFPEVLETSSIPEKTFAEgtkdrfvMDNWNWMLEGyRDIADRYSYyqqftyegLDGLKTGSTNFAG 273
Cdd:pfam00768 149 SARDMAILAKALIKDLPEELSITKEKSFTFRG-------INKINQRNRN-GLLWDKTWN--------VDGLKTGYTNEAG 212
                         250       260
                  ....*....|....*....|..
gi 517987028  274 FCFTGTASRDGVRYITVVMGTK 295
Cdd:pfam00768 213 YCLVASATKGGMRLISVVMGAF 234
PBP4_Staph NF038258
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ...
13-295 1.77e-49

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: 172.47  E-value: 1.77e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  13 LLTFVLMIGFIQKPAAAAEN--IDI-------------NANAVILIdAETGKILYEKNAETVLGIASMTKMMTEYLLLEA 77
Cdd:NF038258   1 IVSLLLLSTIITPPASAAAEtpVEIanqegyqnlseqyNPEGAIVT-TQTGQILYDYHGNKKWDPASMTKLMTMYLTLEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  78 VKEGKVKWDQTFTISPELSKMSHDDDLSNVYLRVDSAYTVEDLYSAMAIESANAATVAIAEIVAGSEANFVKLMNEKAEE 157
Cdd:NF038258  80 IKKGKLSLNDKVKITSDYEKMSTLPNLSTFPLKPGQTYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 158 LGLGDFKFVNSTGLNNRdLAKHFPDVVGGAEEENVMSARAVAKLAYQILKDFPEVLETSSIPEKTfAEGTKdrfvMDNWN 237
Cdd:NF038258 160 LGMKHTHFTNPSGADNN-LLKPYAPKKYKDETKSKSTAKDMAILSQHLIKKHPKILKYTKLTADT-QHGVT----LYTTN 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 517987028 238 WMLEGyrdiadrysyyQQFTYEGLDGLKTGSTNfAGFCFTGTASRDGVRYITVVMGTK 295
Cdd:NF038258 234 LSLPG-----------QPMSLKGTDGLKTGTSD-EGYNLALTTKRDGLRINQVIMNVG 279
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
22-455 2.08e-46

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


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 165.17  E-value: 2.08e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  22 FIQKPAA-AAENI----DINANAVILIDAETGKILYEKNAETVLGIASMTKMMTEYLLLEAVKEGKVKWDQTFTI----- 91
Cdd:PRK10001  19 FLFAPTAfAAEQTveapSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVgkdaw 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  92 ---SPELSKMshdddlSNVYLRVDSAYTVEDLYSAMAIESANAATVAIAEIVAGSEANFVKLMNEKAEELGLGDFKFVNS 168
Cdd:PRK10001  99 atgNPALRGS------SVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTV 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 169 TGLnnrDLAKHFPdvvggaeeenvmSARAVAKLAYQILKDFPEvlETSSIPEKTFaegTKDRFVMDNWNWMLEGyrdiad 248
Cdd:PRK10001 173 HGL---DAPGQFS------------TARDMALLGKALIHDVPE--EYAIHKEKEF---TFNKIRQPNRNRLLWS------ 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 249 rysyyqqfTYEGLDGLKTGSTNFAGFCFTGTASRDGVRYITVVMGTKSQTERFVETKKLLDFAFNNFskEELVP----AE 324
Cdd:PRK10001 227 --------SNLNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFF--ETVTPikpdAT 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 325 YVvkgteTVPVSKGKEDQVKVHSADAISSIVTPAEQENFDTVVKLDkdklneEGALTAPIKKGDKIGTVTIQFKDgeavy 404
Cdd:PRK10001 297 FV-----TQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLT------EPQLTAPLKKGQVVGTIDFQLNG----- 360
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 517987028 405 lSSEGQKSmtvdLIAAENVEKanwfvlmmrgiGGFFGDLWGSVSSTVKGWF 455
Cdd:PRK10001 361 -KSIEQRP----LIVMENVEE-----------GGFFSRMWDFVMMKFHQWF 395
dacD PRK11397
serine-type D-Ala-D-Ala carboxypeptidase DacD;
13-429 2.75e-34

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


Pssm-ID: 183117 [Multi-domain]  Cd Length: 388  Bit Score: 132.25  E-value: 2.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  13 LLTFVLMIGFIQKPAAAAENID-------INANAVILIDAETGKILYEKNAETVLGIASMTKMMTEYLLLEAVKEGKVKW 85
Cdd:PRK11397   5 LIIAASLFAFNLSSAFAAENIPfspqppaIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  86 DQTFTISPELSKMSHD--DDLSNVYLRVDSAYTVEDLYSAMAIESANAATVAIAEIVAGSEANFVKLMNEKAEELGLGDf 163
Cdd:PRK11397  85 DDIVTVGRDAWAKDNPvfVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLHLKD- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 164 kfvnstglnnrdlaKHFPDVVGGAEEENVMSARAVAKLAYQILKDFPEVLETSSipEKTFaegtkdrfvmdNWNWMLEGY 243
Cdd:PRK11397 164 --------------THFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYS--EKSL-----------TWNGITQQN 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 244 RD--IADRYSYyqqftyegLDGLKTGSTNFAGFCFTGTASRDGVRYITVVMGTKSQTERFVETKKLLDFAFNNFSKEELV 321
Cdd:PRK11397 217 RNglLWDKTMN--------VDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGADSAKGREEQARKLLRWGQQNFTTVQIL 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 322 PAEYVVkGTETvpVSKGKEDQVKVHSADAISSIVTPAEQENFDTVVKLDKDKlneegaLTAPIKKGDKIGtvTIQFKDGE 401
Cdd:PRK11397 289 HRGKKV-GTER--IWYGDKENIALGTEQDFWMVLPKAEIPHIKAKYVLDGKE------LEAPISAHQRVG--EIELYDRD 357
                        410       420
                 ....*....|....*....|....*...
gi 517987028 402 AVYLSsegqksmtVDLIAAENVEKANWF 429
Cdd:PRK11397 358 KQVAH--------WPLVTLESVGEGGMF 377
PRK10793 PRK10793
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
34-403 5.53e-33

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


Pssm-ID: 182736 [Multi-domain]  Cd Length: 403  Bit Score: 128.82  E-value: 5.53e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  34 DINANAVILIDAETGKILYEKNAETVLGIASMTKMMTEYLLLEAVKEGKVKWDQTFTISPELSKMSHDD--DLSNVYLRV 111
Cdd:PRK10793  43 QIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTVGNDAWATGNPVfkGSSLMFLKP 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 112 DSAYTVEDLYSAMAIESANAATVAIAEIVAGSEANFVKLMNekaeelglgdfKFVNSTGLNNrdlaKHFPDVVGGAEEEN 191
Cdd:PRK10793 123 GMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMN-----------SYVNALGLKN----THFQTVHGLDADGQ 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 192 VMSARAVAKLAYQILKDFPEvlETSSIPEKTFaegTKDRFVMDNWNWMLEGyrdiadrysyyqqfTYEGLDGLKTGSTNF 271
Cdd:PRK10793 188 YSSARDMALIGQALIRDVPN--EYAIYKEKEF---TFNGIRQLNRNGLLWD--------------NSLNVDGIKTGHTDK 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 272 AGFCFTGTASRDGVRYITVVMGTKSQTERFVETKKLLDFAFNNFskeELVPAEYVVKGTETVPVSKGKEDQVKVHSADAI 351
Cdd:PRK10793 249 AGYNLVASATEGQMRLISAVMGGRTFKGRETESKKLLTWGFRFF---ETVNPLKVGKEFASEPVWFGDSDRASLGVDKDV 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517987028 352 SSIVTPAEQENFDTVVKLDKDKLNeegaltAPIKKGDKIGTVTIQFkDGEAV 403
Cdd:PRK10793 326 YLTIPRGRMKDLKASYVLNTSELH------APLQKNQVVGTINFQL-DGKTI 370
pbpG PRK11669
D-alanyl-D-alanine endopeptidase; Provisional
6-275 1.22e-20

D-alanyl-D-alanine endopeptidase; Provisional


Pssm-ID: 236952  Cd Length: 306  Bit Score: 92.05  E-value: 1.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028   6 IQKSIVCLLTFVLMIGFI-------QKPAAAAENIDINANAVILIDAETGKILYEKNAETVLGIASMTKMMTEYLLLEAv 78
Cdd:PRK11669   3 FRVSLLSLLLLLAGVPFApqavaktAAATTASQPQEIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVVLDA- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  79 kegKVKWDQTFTIspelsKMSHDDDLSNVYLRV--DSAYTVEDLYSAMAIESANAATVAIAEIVAGSEANFVKLMNEKAE 156
Cdd:PRK11669  82 ---KLPLDEKLKV-----DISQTPEMKGVYSRVrlNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 157 ELGLGDFKFVNSTGLNnrdlakhfpdvvggaeEENVMSARAVAKLaYQILKDFPEVLETSSIPEKT--FAEGT------- 227
Cdd:PRK11669 154 ALGMTNTRYVEPTGLS----------------IHNVSTARDLTKL-LIASKQYPLIGQLSTTREKTatFRKPNytlpfrn 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 517987028 228 KDRFVM-DNWNwmlegyrdIadrysyyqQFTyegldglKTGSTNFAGFC 275
Cdd:PRK11669 217 TNHLVYrDNWN--------I--------QLT-------KTGFTNAAGHC 242
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
315-425 6.40e-14

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: 67.24  E-value: 6.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028   315 FSKEELVPAEYVVKgteTVPVSKGKEDQVKVHSADAISSIVTPAEQENFDTVVKLDKDKLNeegaltAPIKKGDKIGTVT 394
Cdd:smart00936   1 FETVKLYKKGQVVG---TVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELE------APIKKGQVVGTLV 71
                           90       100       110
                   ....*....|....*....|....*....|.
gi 517987028   395 IQfkdgeavylsSEGQKSMTVDLIAAENVEK 425
Cdd:smart00936  72 VT----------LDGKLIGEVPLVALEDVEK 92
PBP5_C pfam07943
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
315-425 3.22e-11

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: 59.53  E-value: 3.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  315 FSKEELVPAEYVVKgteTVPVSKGKEDQVKVHSADAISSIVTPAEQENFDTVVKLDKDklneegaLTAPIKKGDKIGTVT 394
Cdd:pfam07943   1 FETKKLYKKGDVVK---KVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKKP-------LEAPIKKGQVVGKLE 70
                          90       100       110
                  ....*....|....*....|....*....|.
gi 517987028  395 IQFkdgeavylssEGQKSMTVDLIAAENVEK 425
Cdd:pfam07943  71 VYL----------DGKLIGEVPLVAKEDVEE 91
PenP COG2367
Beta-lactamase class A [Defense mechanisms];
13-208 5.96e-11

Beta-lactamase class A [Defense mechanisms];


Pssm-ID: 441934 [Multi-domain]  Cd Length: 276  Bit Score: 62.99  E-value: 5.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  13 LLTFVLMIGFIQKPAAAAENiDINANA--------VILIDAETGKiLYEKNAETVLGIASMTKMMTEYLLLEAVKEGKVK 84
Cdd:COG2367    3 LLALLLLAAAAAAPASALEA-ELAALEaalggrvgVYVLDLDTGE-TVGINADERFPAASTFKLPVLAAVLRQVDAGKLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  85 WDQTFTISPELsKMSHDDDLSnvYLRVDSAYTVEDLYSAMAIESANAATVAIAEIVaGSEAnfvklMNEKAEELGLGDFK 164
Cdd:COG2367   81 LDERVTLTPED-LVGGSGILQ--KLPDGTGLTLRELAELMITVSDNTATNLLLRLL-GPDA-----VNAFLRSLGLTDTR 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 517987028 165 FVNSTGLNNRDLakhfpdvvggAEEENVMSARAVAKLAYQILKD 208
Cdd:COG2367  152 LDRKEPDLNELP----------GDGRNTTTPRDMARLLAALYRG 185
Beta-lactamase2 pfam13354
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ...
44-201 1.32e-10

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: 60.75  E-value: 1.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028   44 DAETGKiLYEKNAETVLGIASMTKMMTEYLLLEAVKEGKVKWDQTFTISPELsKMSHDDDLSnvYLRVDSAYTVEDLYSA 123
Cdd:pfam13354   6 DLDTGE-ELGINGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTAED-KVGGSGILQ--YLPDGSQLSLRDLLTL 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517987028  124 MAIESANAATVAIAEIVAGSEanfvklMNEKAEELGLgdfkfvNSTGLNNRDLAKHFPDvvggAEEENVMSARAVAKL 201
Cdd:pfam13354  82 MIAVSDNTATNLLIDRLGLEA------VNARLRALGL------RDTRLRRKLPDLRAAD----KGGTNTTTARDMAKL 143
AmpC COG1680
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];
27-245 1.05e-04

CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];


Pssm-ID: 441286 [Multi-domain]  Cd Length: 355  Bit Score: 44.29  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  27 AAAAENIDINANAVILIDAetGKILYEK-------------NAETVLGIASMTKMMTEYLLLEAVKEGKVKWDQtfTIS- 92
Cdd:COG1680   24 DAALAEGGIPGAAVAVVRD--GKVVYEKaygvadletgrpvTPDTLFRIASVTKSFTATAVLQLVEEGKLDLDD--PVSk 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028  93 --PELSK-------------MSH----DDDLSNVY--LRVDSAYTVEDLYSAMA---IESA--------NAATVAIAEIV 140
Cdd:COG1680  100 ylPEFKLpddakrditvrhlLTHtsglPDYEPDPYdaADVARPYTPDDLLARLAalpLLFEpgtrfsysNLGYDLLGEII 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517987028 141 AG-SEANFVKLMNEK-AEELGLGDFKFVNSTGLNNRDLAKHFPDvvGGAEEEN------------VMSARAVAKLAYQIL 206
Cdd:COG1680  180 ERvTGQPLEDYLRERiFEPLGMTDTGFGLPDAEAARLAPGYEAD--GEVHDAPawlgavagagglFSTARDLARFGQALL 257
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 517987028 207 KDfPEVLETSSIPEKTFAEGTKDRFVMDNWN------WMLEGYRD 245
Cdd:COG1680  258 NG-GEWDGKRLLSPETLAEMTTPQVPSGDAGggyglgWWLNDDGG 301
 
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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