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MULTISPECIES: C39 family peptidase [Acinetobacter]

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, ...
 48-199 5.47e-63

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: 195.98  E-value: 5.47e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246  48 EHVEVKPALLDQFQGIVRQAYDYSCGSAALTTLLNGYVGTRLDEQQVMNGLMKFGEtdkiIERRSFSLLDMKRFVAALGL 127
Cdd:COG3271   30 YSVPVKSLKELRFRNVVRQQYDYSCGAAALATLLNYHYGRPVSEAEVLEGMLTHGD----QRRRGFSLLDMKRYLEALGL 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491376246 128 ESGGYRGEFEDLVKQGQPAIVPISYAGFKHFVVYKAYKNGRVYVADPALGNISFDEQRFKEVWENNTLYLIN 199
Cdd:COG3271  106 RADGYRLTLDDLAQLGIPAIVLINLGGYKHFVVVKGVDDGRVLLADPALGNRSLSREEFEKMWDGNVLFVVP 177
 
Name Accession Description Interval E-value
C39G COG3271
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, ...
 48-199 5.47e-63

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: 195.98  E-value: 5.47e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246  48 EHVEVKPALLDQFQGIVRQAYDYSCGSAALTTLLNGYVGTRLDEQQVMNGLMKFGEtdkiIERRSFSLLDMKRFVAALGL 127
Cdd:COG3271   30 YSVPVKSLKELRFRNVVRQQYDYSCGAAALATLLNYHYGRPVSEAEVLEGMLTHGD----QRRRGFSLLDMKRYLEALGL 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491376246 128 ESGGYRGEFEDLVKQGQPAIVPISYAGFKHFVVYKAYKNGRVYVADPALGNISFDEQRFKEVWENNTLYLIN 199
Cdd:COG3271  106 RADGYRLTLDDLAQLGIPAIVLINLGGYKHFVVVKGVDDGRVLLADPALGNRSLSREEFEKMWDGNVLFVVP 177
Peptidase_C39G cd02423
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 62-197 7.88e-55

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: 173.22  E-value: 7.88e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246  62 GIVRQAYDYSCGSAALTTLLNGYVGTRLDEQQVMNGLMkfgetdkiIERRSFSLLDMKRFVAALGLESGGYRGEFEDLVK 141
Cdd:cd02423    2 GVVRQSYDFSCGPAALATLLRYYGGINITEQEVLKLML--------IRSEGFSMLDLKRYAEALGLKANGYRLNLDKLNA 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491376246 142 QGQPAIVPISYAGFKHFVVYKAYKNGRVYVADPALGNISFDEQRFKEVWENNTLYL 197
Cdd:cd02423   74 LQIPVIVLVNNGGYGHFVVIKGIDGDRVLVGDPALGNISMSREEFERIWTGNALFV 129
Peptidase_C39 pfam03412
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ...
 63-197 1.55e-15

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: 71.49  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246   63 IVRQAYDYSCGSAALTTLLNgYVGTRLDEQQVMNglmKFGetdkiIERRSFSLLDMKRFVAALGLESGGYRGEFEDLVKQ 142
Cdd:pfam03412   4 IVLQVDENDCGLACLAMILK-YYGSNVSLEELRE---LAG-----TPAEGTSLLGLKKAAEKLGFKAKAIKADLSELKEL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 491376246  143 GQPAIVPISyAGFKHFVVYKAYKNGRVYVADPALGNISFDEQRFKEVWENNTLYL 197
Cdd:pfam03412  75 PLPFIAHWD-GNGGHFVVVYGIKKNKVLIADPAVGKIKLSREEFEKEWTGVALLV 128
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 72-188 1.75e-09

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 58.03  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246   72 CGSAALTTLLnGYVG--TRLDEQQVMNGLMKFGEtdkiierRSFSLLDMKRfvaALGLESGGYRGEFEDLVKQGQPAIVp 149
Cdd:TIGR03796  13 CGAASLAMIL-AYYGryVPLEELREECGVSRDGS-------KASNLLKAAR---SYGLEAKGFRKELDALAELPLPYIV- 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 491376246  150 isYAGFKHFVVYKAYKNGRVYVADPALGNISFDEQRFKE 188
Cdd:TIGR03796  81 --FWNFNHFVVVEGFRGGRVYLNDPALGPRTVSLEEFDE 117
 
Name Accession Description Interval E-value
C39G COG3271
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, ...
 48-199 5.47e-63

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: 195.98  E-value: 5.47e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246  48 EHVEVKPALLDQFQGIVRQAYDYSCGSAALTTLLNGYVGTRLDEQQVMNGLMKFGEtdkiIERRSFSLLDMKRFVAALGL 127
Cdd:COG3271   30 YSVPVKSLKELRFRNVVRQQYDYSCGAAALATLLNYHYGRPVSEAEVLEGMLTHGD----QRRRGFSLLDMKRYLEALGL 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491376246 128 ESGGYRGEFEDLVKQGQPAIVPISYAGFKHFVVYKAYKNGRVYVADPALGNISFDEQRFKEVWENNTLYLIN 199
Cdd:COG3271  106 RADGYRLTLDDLAQLGIPAIVLINLGGYKHFVVVKGVDDGRVLLADPALGNRSLSREEFEKMWDGNVLFVVP 177
Peptidase_C39G cd02423
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 62-197 7.88e-55

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: 173.22  E-value: 7.88e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246  62 GIVRQAYDYSCGSAALTTLLNGYVGTRLDEQQVMNGLMkfgetdkiIERRSFSLLDMKRFVAALGLESGGYRGEFEDLVK 141
Cdd:cd02423    2 GVVRQSYDFSCGPAALATLLRYYGGINITEQEVLKLML--------IRSEGFSMLDLKRYAEALGLKANGYRLNLDKLNA 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491376246 142 QGQPAIVPISYAGFKHFVVYKAYKNGRVYVADPALGNISFDEQRFKEVWENNTLYL 197
Cdd:cd02423   74 LQIPVIVLVNNGGYGHFVVIKGIDGDRVLVGDPALGNISMSREEFERIWTGNALFV 129
Peptidase_C39 pfam03412
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ...
 63-197 1.55e-15

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: 71.49  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246   63 IVRQAYDYSCGSAALTTLLNgYVGTRLDEQQVMNglmKFGetdkiIERRSFSLLDMKRFVAALGLESGGYRGEFEDLVKQ 142
Cdd:pfam03412   4 IVLQVDENDCGLACLAMILK-YYGSNVSLEELRE---LAG-----TPAEGTSLLGLKKAAEKLGFKAKAIKADLSELKEL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 491376246  143 GQPAIVPISyAGFKHFVVYKAYKNGRVYVADPALGNISFDEQRFKEVWENNTLYL 197
Cdd:pfam03412  75 PLPFIAHWD-GNGGHFVVVYGIKKNKVLIADPAVGKIKLSREEFEKEWTGVALLV 128
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 64-197 5.92e-12

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: 65.63  E-value: 5.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246  64 VRQAYDYSCGSAALTTLLnGYVGTRLDEQQVMNGLmkfgetdkIIERRSFSLLDMKRFVAALGLESGGYRGEFEDLVKQG 143
Cdd:COG2274    7 VLQMEAADCGLACLAMIA-RYYGRPVSLEELREAL--------GVSRDGLSLLGLLRAARRLGLRARGVRLDLEELAELP 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491376246 144 QPAIVpisYAGFKHFVVYKAYKNGRVYVADPALGNISFDEQRFKEVWENNTLYL 197
Cdd:COG2274   78 LPAIL---HWDGNHFVVLEGVDGDKVTIADPATGRRKLSLEEFAESWTGVALLL 128
Peptidase_C39_like cd02259
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ...
 66-198 8.35e-12

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: 60.86  E-value: 8.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246  66 QAYDYSCGSAALTTLLNgYVGTRLDEQQVMNglmkfgetDKIIERRSFSLLDMKRFVAALGLESGGYRGEFEDLVKQGQP 145
Cdd:cd02259    1 GGGPLDCGLACLQMLLR-YFGIPVRRDVLLN--------AQQRRQQGLSLADLVSLANKLGLTAQGVKLPLAALSRLQLP 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491376246 146 AIVPISYagfKHFVVYKAYKNGRVYVADP-ALGNISFDEQRFKEVWENNTLYLI 198
Cdd:cd02259   72 ALLLWKQ---GHFVILYGADKGQVLIADPlEEGPVTLSESELEERWTGHWVLLL 122
Peptidase_C39E cd02424
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 63-193 8.45e-11

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, which contains Colicin V perocessing peptidase.


Pssm-ID: 239104 [Multi-domain]  Cd Length: 129  Bit Score: 58.50  E-value: 8.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246  63 IVRQAYDYSCGSAALTTLLNGYVGTR--LDEQQVMNGLMKFGetdkiierrsFSLLDMKRFVAALGLESGGYRGEFEDLV 140
Cdd:cd02424    3 IIKQTDLNDCGIAVIQMLYNHYYKKKydLNELKIKANLKKNG----------LSIYDLENLAKKFGLETESYQGSFLEFL 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491376246 141 KQGQPAIVPISYAGFKHFVVYKAYKNGRVYVADPALGNISFDEQRFKEVWENN 193
Cdd:cd02424   73 ELKNKFIILLKSNGLNHFVIVKKIKKNKFIVLDPKKGKYKITYKEFEKIFNNI 125
Peptidase_C39B cd02418
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 72-197 5.75e-10

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: 56.06  E-value: 5.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246  72 CGSAALTTLLNGYvGTRLDeqqvMNGLMKFGETDkiieRRSFSLLDMKRFVAALGLESGGYRGEFEDLVKQGQ--PAIVP 149
Cdd:cd02418   12 CGAACLAMIAKYY-GKNYS----LAKLRELAGTD----REGTSLLGLVKAAEKLGFETRAVKADMDLFELKDIplPFIAH 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 491376246 150 ISYAG-FKHFVVYKAYKNGRVYVADPALGNISFDEQRFKEVWENNTLYL 197
Cdd:cd02418   83 VIKEWkLNHYVVVYKIKKKKILIADPAVGITKISKEEFEKEWTGVALFL 131
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 72-188 1.75e-09

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 58.03  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246   72 CGSAALTTLLnGYVG--TRLDEQQVMNGLMKFGEtdkiierRSFSLLDMKRfvaALGLESGGYRGEFEDLVKQGQPAIVp 149
Cdd:TIGR03796  13 CGAASLAMIL-AYYGryVPLEELREECGVSRDGS-------KASNLLKAAR---SYGLEAKGFRKELDALAELPLPYIV- 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 491376246  150 isYAGFKHFVVYKAYKNGRVYVADPALGNISFDEQRFKE 188
Cdd:TIGR03796  81 --FWNFNHFVVVEGFRGGRVYLNDPALGPRTVSLEEFDE 117
Peptidase_C39D cd02420
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 72-186 4.93e-07

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: 239101 [Multi-domain]  Cd Length: 125  Bit Score: 47.81  E-value: 4.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246  72 CGSAALTTLLnGYVGTR--LDEQQVMNGLMKFGETDKIIER--RSFslldmkrfvaalGLESGGYRGEFEDLVKQGQPAI 147
Cdd:cd02420   12 CGAASLAIIL-AYYGRYvpLSELRIACGVSRDGSNASNLLKaaREY------------GLTAKGYKKDLEALREVSLPAI 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 491376246 148 VpisYAGFKHFVVYKAYKNGRVYVADPALGNISFDEQRF 186
Cdd:cd02420   79 V---FWNFNHFLVVEGFDKRKVFLNDPATGRRTVSLEEF 114
Peptidase_C39C cd02419
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 72-183 2.26e-06

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: 45.71  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246  72 CGSAALTtLLNGYVGTRLDeqqvMNGL-MKFgetdkIIERRSFSLLDMKRFVAALGLESGGYRGEFEDLVKQGQPAIVpi 150
Cdd:cd02419   12 CGLACLA-MIASYHGHHVD----LASLrQRF-----PVSLKGATLADLIDIAQQLGLSTRALRLDLEELGQLKLPCIL-- 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 491376246 151 sYAGFKHFVVYKAYKNGRVYVADPALG--NISFDE 183
Cdd:cd02419   80 -HWDMNHFVVLKKVSRRRIVIHDPALGkrKLSLEE 113
Peptidase_C39F cd02425
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 63-196 1.08e-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: 239105 [Multi-domain]  Cd Length: 126  Bit Score: 41.10  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246  63 IVRQAYDYSCGSAALTTLLNGYVGT------RLDEQQVMNGLmkfgetdkiierrsfSLLDMKRFVAALGLESGGYRGEF 136
Cdd:cd02425    3 PILQNNQTECGLACYAMILNYFGYKvslnelREKYELGRDGL---------------SLSYLKQLLEEYGFKCKVYKISF 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491376246 137 -EDLVKQGQPAIVpisYAGFKHFVVYKAYKNGRVYVADPALGNISFDEQRFKEVWENNTLY 196
Cdd:cd02425   68 kKNLYPLKLPVII---FWNNNHFVVLEKIKKNKVTIVDPAIGRIKISIDEFLENFSGYILT 125
Peptidase_C39A cd02549
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 69-190 1.74e-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 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: 40.85  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376246  69 DYSCGSAALTTLLNGYvGTRLDEQQVMNglmKFGETDKIIERRSFSLLDMkrfvAALGLESGGYRGEF-------EDLVK 141
Cdd:cd02549    4 ENGCGPTSLAMVLSYL-GVKVTKPQLAA---EGNTYDFAKDGYGTYPKPI----VSAAARKYGLVVRPltgllalLRQLA 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491376246 142 QGQPAIVPISYAGF----KHFVVYKAY-KNGRVYVADPA---LGNISFDEqrFKEVW 190
Cdd:cd02549   76 AGHPVIVSVNLGVSitpsGHAMVVIGYdRKGNVYVNDPGggrRLVVSFDE--FEKAW 130
 
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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