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C39 family peptidase [Methanosarcina acetivorans]

Protein Classification

C39 family peptidase( domain architecture ID 10007152)

C39 family peptidase is a cysteine peptidase which may cleave the "double-glycine" leader peptides from the precursors of various bacteriocins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C39G COG3271
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, ...
 16-198 9.69e-33

Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, secretion, and vesicular transport];


:

Pssm-ID: 442502 [Multi-domain]  Cd Length: 179  Bit Score: 117.02  E-value: 9.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689  16 FLSVAGLAILIAiGIPAGaSEIKVKCVVPENGTTMLLQVPD---VRQSTNYSCGASCFQAVVSYWGGKDMGEGQFIELVN 92
Cdd:COG3271    4 ATLLLSLLLLLA-GSPAG-SVLPGSGGGYSVPVKSLKELRFrnvVRQQYDYSCGAAALATLLNYHYGRPVSEAEVLEGML 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689  93 tTLGETDRKGTTPSGIVEGAEKMGLRAEIReNLTLDDLRdsiNKGIPVIVRLQAWKNedqtwemnasSHYMVVIGIDSKN 172
Cdd:COG3271   82 -THGDQRRRGFSLLDMKRYLEALGLRADGY-RLTLDDLA---QLGIPAIVLINLGGY----------KHFVVVKGVDDGR 146

                        170       180
                 ....*....|....*....|....*.
gi 499331689 173 VYFEDPWiLGSRgYIPHDEFVERWHT 198
Cdd:COG3271  147 VLLADPA-LGNR-SLSREEFEKMWDG 170
 
Name Accession Description Interval E-value
C39G COG3271
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, ...
 16-198 9.69e-33

Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442502 [Multi-domain]  Cd Length: 179  Bit Score: 117.02  E-value: 9.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689  16 FLSVAGLAILIAiGIPAGaSEIKVKCVVPENGTTMLLQVPD---VRQSTNYSCGASCFQAVVSYWGGKDMGEGQFIELVN 92
Cdd:COG3271    4 ATLLLSLLLLLA-GSPAG-SVLPGSGGGYSVPVKSLKELRFrnvVRQQYDYSCGAAALATLLNYHYGRPVSEAEVLEGML 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689  93 tTLGETDRKGTTPSGIVEGAEKMGLRAEIReNLTLDDLRdsiNKGIPVIVRLQAWKNedqtwemnasSHYMVVIGIDSKN 172
Cdd:COG3271   82 -THGDQRRRGFSLLDMKRYLEALGLRADGY-RLTLDDLA---QLGIPAIVLINLGGY----------KHFVVVKGVDDGR 146

                        170       180
                 ....*....|....*....|....*.
gi 499331689 173 VYFEDPWiLGSRgYIPHDEFVERWHT 198
Cdd:COG3271  147 VLLADPA-LGNR-SLSREEFEKMWDG 170
Peptidase_C39A cd02549
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 59-201 1.08e-31

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.


Pssm-ID: 239109 [Multi-domain]  Cd Length: 141  Bit Score: 112.89  E-value: 1.08e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689  59 QSTNYSCGASCFQAVVSYWGGKDMGEGQFIElVNTTLGETDRKGTTPSGIVEG-AEKMGLRAEIRENltLDDLRDSINKG 137
Cdd:cd02549    1 PQLENGCGPTSLAMVLSYLGVKVTKPQLAAE-GNTYDFAKDGYGTYPKPIVSAaARKYGLVVRPLTG--LLALLRQLAAG 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499331689 138 IPVIVRLQawknedQTWEMNASSHYMVVIGIDSK-NVYFEDPWiLGSRGYIPHDEFVERWHTFSY 201
Cdd:cd02549   78 HPVIVSVN------LGVSITPSGHAMVVIGYDRKgNVYVNDPG-GGRRLVVSFDEFEKAWKRMGG 135
Peptidase_C70 pfam12385
Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in ...
 52-194 2.63e-11

Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in actinobacteria, protobacteria and firmicutes. Papain-like cysteine proteases play a crucial role in plant-pathogen/pest interactions. On entering the host they act on non-self substrates, thereby manipulating the host to evade proteolysis. AvrRpt2 from Pseudomonas syringae pv. tomato DC3000 triggers resistance to P. syringae-2-dependent defence responses, including hypersensitive cell death, by cleaving the Arabidopsis RIN4 protein which is monitored by the cognate resistance protein RPS2.


Pssm-ID: 403550 [Multi-domain]  Cd Length: 143  Bit Score: 59.40  E-value: 2.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689   52 LQVPDVRQSTNYSCGASCFQAVVSYWGGKDMGEGQfielVNTTLGETDRKGTTPSG--IVEGAEKMGLR--AEIRENLTL 127
Cdd:pfam12385   5 LDVPYNVQQAAMGCWAASASMIAGYRGQKPIDPSE----IAALVPGWSQYDTGLNGpeDIALAEKWGLGnvPEPPQSYSI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499331689  128 DDLRDSINKGIPVIVRlqawknedQTWEMNASSHYMVVIGIDS--KNVYFEDPWiLGSRGYIPHDEFVE 194
Cdd:pfam12385  81 DALVKLLRAYGPLWCA--------IAWPGGFVGHAIVLTGIDEdgTPVYYHDPW-SGPRREVSLASFNP 140
 
Name Accession Description Interval E-value
C39G COG3271
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, ...
 16-198 9.69e-33

Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442502 [Multi-domain]  Cd Length: 179  Bit Score: 117.02  E-value: 9.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689  16 FLSVAGLAILIAiGIPAGaSEIKVKCVVPENGTTMLLQVPD---VRQSTNYSCGASCFQAVVSYWGGKDMGEGQFIELVN 92
Cdd:COG3271    4 ATLLLSLLLLLA-GSPAG-SVLPGSGGGYSVPVKSLKELRFrnvVRQQYDYSCGAAALATLLNYHYGRPVSEAEVLEGML 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689  93 tTLGETDRKGTTPSGIVEGAEKMGLRAEIReNLTLDDLRdsiNKGIPVIVRLQAWKNedqtwemnasSHYMVVIGIDSKN 172
Cdd:COG3271   82 -THGDQRRRGFSLLDMKRYLEALGLRADGY-RLTLDDLA---QLGIPAIVLINLGGY----------KHFVVVKGVDDGR 146

                        170       180
                 ....*....|....*....|....*.
gi 499331689 173 VYFEDPWiLGSRgYIPHDEFVERWHT 198
Cdd:COG3271  147 VLLADPA-LGNR-SLSREEFEKMWDG 170
Peptidase_C39A cd02549
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 59-201 1.08e-31

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.


Pssm-ID: 239109 [Multi-domain]  Cd Length: 141  Bit Score: 112.89  E-value: 1.08e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689  59 QSTNYSCGASCFQAVVSYWGGKDMGEGQFIElVNTTLGETDRKGTTPSGIVEG-AEKMGLRAEIRENltLDDLRDSINKG 137
Cdd:cd02549    1 PQLENGCGPTSLAMVLSYLGVKVTKPQLAAE-GNTYDFAKDGYGTYPKPIVSAaARKYGLVVRPLTG--LLALLRQLAAG 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499331689 138 IPVIVRLQawknedQTWEMNASSHYMVVIGIDSK-NVYFEDPWiLGSRGYIPHDEFVERWHTFSY 201
Cdd:cd02549   78 HPVIVSVN------LGVSITPSGHAMVVIGYDRKgNVYVNDPG-GGRRLVVSFDEFEKAWKRMGG 135
Peptidase_C39G cd02423
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 57-199 8.37e-15

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature.


Pssm-ID: 239103 [Multi-domain]  Cd Length: 129  Bit Score: 68.45  E-value: 8.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689  57 VRQSTNYSCGASCFQAVVSYWGGKDMGEGQFIELVNttlgeTDRKGTTPSGIVEGAEKMGLRAEIReNLTLDDLRdsiNK 136
Cdd:cd02423    4 VRQSYDFSCGPAALATLLRYYGGINITEQEVLKLML-----IRSEGFSMLDLKRYAEALGLKANGY-RLNLDKLN---AL 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499331689 137 GIPVIVrlqaWKNEDQTwemnasSHYMVVIGIDSKNVYFEDPwilgSRGYI--PHDEFVERWHTF 199
Cdd:cd02423   75 QIPVIV----LVNNGGY------GHFVVIKGIDGDRVLVGDP----ALGNIsmSREEFERIWTGN 125
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 53-196 1.16e-13

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 69.48  E-value: 1.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689  53 QVPDVRQSTNYSCGASCFQAVVSYWgGKDMGEGQFIELVNttlgeTDRKGTTPSGIVEGAEKMGLRAEIREnLTLDDLRD 132
Cdd:COG2274    3 KVPFVLQMEAADCGLACLAMIARYY-GRPVSLEELREALG-----VSRDGLSLLGLLRAARRLGLRARGVR-LDLEELAE 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499331689 133 SInkgIPVIVRlqawknedqtWEMNassHYMVVIGIDSKNVYFEDPWIlGSRgYIPHDEFVERW 196
Cdd:COG2274   76 LP---LPAILH----------WDGN---HFVVLEGVDGDKVTIADPAT-GRR-KLSLEEFAESW 121
Peptidase_C39B cd02418
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 57-196 4.22e-12

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.


Pssm-ID: 239099 [Multi-domain]  Cd Length: 136  Bit Score: 61.46  E-value: 4.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689  57 VRQSTNYSCGASCFQAVVSYWGgKDMGEGQFIELVNTtlgetDRKGTTPSGIVEGAEKMGLRAE-IRENLtldDLRDSIN 135
Cdd:cd02418    4 VLQVDEMDCGAACLAMIAKYYG-KNYSLAKLRELAGT-----DREGTSLLGLVKAAEKLGFETRaVKADM---DLFELKD 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499331689 136 KGIPVIVRLQawKNEDQtwemnasSHYMVVIGIDSKNVYFEDPwilgSRG--YIPHDEFVERW 196
Cdd:cd02418   75 IPLPFIAHVI--KEWKL-------NHYVVVYKIKKKKILIADP----AVGitKISKEEFEKEW 124
Peptidase_C70 pfam12385
Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in ...
 52-194 2.63e-11

Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in actinobacteria, protobacteria and firmicutes. Papain-like cysteine proteases play a crucial role in plant-pathogen/pest interactions. On entering the host they act on non-self substrates, thereby manipulating the host to evade proteolysis. AvrRpt2 from Pseudomonas syringae pv. tomato DC3000 triggers resistance to P. syringae-2-dependent defence responses, including hypersensitive cell death, by cleaving the Arabidopsis RIN4 protein which is monitored by the cognate resistance protein RPS2.


Pssm-ID: 403550 [Multi-domain]  Cd Length: 143  Bit Score: 59.40  E-value: 2.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689   52 LQVPDVRQSTNYSCGASCFQAVVSYWGGKDMGEGQfielVNTTLGETDRKGTTPSG--IVEGAEKMGLR--AEIRENLTL 127
Cdd:pfam12385   5 LDVPYNVQQAAMGCWAASASMIAGYRGQKPIDPSE----IAALVPGWSQYDTGLNGpeDIALAEKWGLGnvPEPPQSYSI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499331689  128 DDLRDSINKGIPVIVRlqawknedQTWEMNASSHYMVVIGIDS--KNVYFEDPWiLGSRGYIPHDEFVE 194
Cdd:pfam12385  81 DALVKLLRAYGPLWCA--------IAWPGGFVGHAIVLTGIDEdgTPVYYHDPW-SGPRREVSLASFNP 140
Peptidase_C39_2 pfam13529
Peptidase_C39 like family;
53-178 3.78e-11

Peptidase_C39 like family;


Pssm-ID: 379241 [Multi-domain]  Cd Length: 139  Bit Score: 59.00  E-value: 3.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689   53 QVPDVRQSTN--YSCGASCFQAVVSYWG--------GKDMGEGQFIELVNTTLGETDRK---GTTPSGIVEGAEKMGLRA 119
Cdd:pfam13529   1 DVPYYNQLDElpNGCGPTSLAMVLSYLGitvtqdelAKEIGTNPDGNPNTGFVGNPYDKsgyGVYNPPIVALAEKYGLKV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499331689  120 EIRENLTLDDLRDSINKGIPVIVRLQAWKNEDQTWEmnASSHYMVVIGIDSKN--VYFEDP 178
Cdd:pfam13529  81 TDITGSSFDEVIRLLDAGIPVVVSTTTFGPLNYYFT--SSGHLVVIVGYDDKGdyVYVNDP 139
Peptidase_C39 pfam03412
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ...
 54-196 3.00e-10

Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as precursor peptides containing N-terminal extensions (leader peptides) which are cleaved off during maturation. Most non-lantibiotics and also some lantibiotics have leader peptides of the so-called double-glycine type. These leader peptides share consensus sequences and also a common processing site with two conserved glycine residues in positions -1 and -2. The double- glycine-type leader peptides are unrelated to the N-terminal signal sequences which direct proteins across the cytoplasmic membrane via the sec pathway. Their processing sites are also different from typical signal peptidase cleavage sites, suggesting that a different processing enzyme is involved. Peptide bacteriocins are exported across the cytoplasmic membrane by a dedicated ATP-binding cassette (ABC) transporter. The ABC transporter is the maturation protease and its proteolytic domain resides in the N-terminal part of the protein. This peptidase domain is found in a wide range of ABC transporters, however the presumed catalytic cysteine and histidine are not conserved in all members of this family.


Pssm-ID: 367483 [Multi-domain]  Cd Length: 133  Bit Score: 56.46  E-value: 3.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689   54 VPDVRQSTNYSCGASCFQAVVSYWGgkdmgegqfielVNTTLGE------TDRKGTTPSGIVEGAEKMGLRAE-IRenLT 126
Cdd:pfam03412   2 YKIVLQVDENDCGLACLAMILKYYG------------SNVSLEElrelagTPAEGTSLLGLKKAAEKLGFKAKaIK--AD 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499331689  127 LDDLRDSInkgIPVIVRlqaWKNEDQtwemnassHYMVVIGIDSKNVYFEDPwilgSRG--YIPHDEFVERW 196
Cdd:pfam03412  68 LSELKELP---LPFIAH---WDGNGG--------HFVVVYGIKKNKVLIADP----AVGkiKLSREEFEKEW 121
YvpB COG4990
Predicted cysteine peptidase, C39 family [General function prediction only];
37-196 5.21e-10

Predicted cysteine peptidase, C39 family [General function prediction only];


Pssm-ID: 444014 [Multi-domain]  Cd Length: 303  Bit Score: 58.28  E-value: 5.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689  37 IKVKCVVPENGTTMLLQVPDVRQSTNYSCG------ASCFQavvsyWGGKDMGEGQFIELVNTTLGETDRKGTTP----- 105
Cdd:COG4990  101 MKKIIYPKPNPDSVLLNVPYISQLPELPTGcevtslAMLLN-----YYGIDVTKDELAEYLPKVPLPYNGYGGNPnkgfv 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689 106 --------------SGIVEGAEK-MGLRAEIRENLTLDDLRDSINKGIPVIV---RLQAWKNEDQTWEMN--------AS 159
Cdd:COG4990  176 gdpygsdpgygvyaPPIAQLAKKyLPGKAVDLTGASFEDILDELASGNPVIVwttLDFSPPSAFRSWTTPdgktfdftAN 255

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 499331689 160 SHYMVVIGIDSKNVYFEDPWilGSRGYIPHD--EFVERW 196
Cdd:COG4990  256 EHAVVVTGYDDEGVYVNDPL--GGNKYVKYSrsLFERSW 292
Peptidase_C39_like cd02259
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ...
 59-196 1.02e-09

Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in all sub-families.


Pssm-ID: 239073 [Multi-domain]  Cd Length: 122  Bit Score: 54.70  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689  59 QSTNYSCGASCFQAVVSYWGgkdmgeGQFIELVNTTLGETDRKGTTPSGIVEGAEKMGLRAEIREnLTLDDLRdsiNKGI 138
Cdd:cd02259    1 GGGPLDCGLACLQMLLRYFG------IPVRRDVLLNAQQRRQQGLSLADLVSLANKLGLTAQGVK-LPLAALS---RLQL 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499331689 139 PVIVRLqaWKNedqtwemnassHYMVVIGIDSKNVYFEDPWILGSRgYIPHDEFVERW 196
Cdd:cd02259   71 PALLLW--KQG-----------HFVILYGADKGQVLIADPLEEGPV-TLSESELEERW 114
Peptidase_C39C cd02419
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 54-192 6.05e-04

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.


Pssm-ID: 239100 [Multi-domain]  Cd Length: 127  Bit Score: 38.78  E-value: 6.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689  54 VPDVRQSTNYSCGASCFQAVVSYWGgkdmgegqfielVNTTLGE------TDRKGTTPSGIVEGAEKMGLRAE-IRENLT 126
Cdd:cd02419    1 LPVILQTEAAECGLACLAMIASYHG------------HHVDLASlrqrfpVSLKGATLADLIDIAQQLGLSTRaLRLDLE 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499331689 127 -LDDLRdsinkgIPVIVRlqawknedqtWEMNassHYMVVIGIDSKNVYFEDPwILGSRgYIPHDEF 192
Cdd:cd02419   69 eLGQLK------LPCILH----------WDMN---HFVVLKKVSRRRIVIHDP-ALGKR-KLSLEEA 114
Peptidase_C39F cd02425
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 54-194 5.59e-03

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.


Pssm-ID: 239105 [Multi-domain]  Cd Length: 126  Bit Score: 35.70  E-value: 5.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331689  54 VPDVRQSTNYSCGASCFQAVVSYWGGKdmgegqfIELvnTTLGETD---RKGTTPSGIVEGAEKMGLRAeirENLTLDDL 130
Cdd:cd02425    1 VKPILQNNQTECGLACYAMILNYFGYK-------VSL--NELREKYelgRDGLSLSYLKQLLEEYGFKC---KVYKISFK 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499331689 131 RDSINKGIPVIVrlqAWKNedqtwemnasSHYMVVIGIDSKNVYFEDPWIlgSRGYIPHDEFVE 194
Cdd:cd02425   69 KNLYPLKLPVII---FWNN----------NHFVVLEKIKKNKVTIVDPAI--GRIKISIDEFLE 117
 
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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