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Conserved domains on  [gi|15597149|ref|NP_250643|]
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hypothetical protein PA1953 [Pseudomonas aeruginosa PAO1]

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, ...
 18-181 5.56e-70

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: 211.77  E-value: 5.56e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  18 AATLGFPALPGGGLVY-KQVQSIRERRFADLVEQKTDFSCGAAALATILEKAYGAPLDEQAVIQGMLAHADPeivRTQGF 96
Cdd:COG3271  15 AGSPAGSVLPGSGGGYsVPVKSLKELRFRNVVRQQYDYSCGAAALATLLNYHYGRPVSEAEVLEGMLTHGDQ---RRRGF 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  97 SMLDMKRYVESMGMRARGYRIEAAQLEQLKIPAIVLMEIRGYKHFVVLQRTQGEYVYVGDPALGHKRYALTEFAKGWNGI 176
Cdd:COG3271  92 SLLDMKRYLEALGLRADGYRLTLDDLAQLGIPAIVLINLGGYKHFVVVKGVDDGRVLLADPALGNRSLSREEFEKMWDGN 171


                ....*
gi 15597149 177 VFAVI 181
Cdd:COG3271 172 VLFVV 176
 
Name Accession Description Interval E-value
C39G COG3271
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, ...
 18-181 5.56e-70

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: 211.77  E-value: 5.56e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  18 AATLGFPALPGGGLVY-KQVQSIRERRFADLVEQKTDFSCGAAALATILEKAYGAPLDEQAVIQGMLAHADPeivRTQGF 96
Cdd:COG3271  15 AGSPAGSVLPGSGGGYsVPVKSLKELRFRNVVRQQYDYSCGAAALATLLNYHYGRPVSEAEVLEGMLTHGDQ---RRRGF 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  97 SMLDMKRYVESMGMRARGYRIEAAQLEQLKIPAIVLMEIRGYKHFVVLQRTQGEYVYVGDPALGHKRYALTEFAKGWNGI 176
Cdd:COG3271  92 SLLDMKRYLEALGLRADGYRLTLDDLAQLGIPAIVLINLGGYKHFVVVKGVDDGRVLLADPALGNRSLSREEFEKMWDGN 171


                ....*
gi 15597149 177 VFAVI 181
Cdd:COG3271 172 VLFVV 176
Peptidase_C39G cd02423
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 46-180 3.85e-53

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: 167.06  E-value: 3.85e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  46 DLVEQKTDFSCGAAALATILEKAYGAPLDEQAVIQGMLahadpeiVRTQGFSMLDMKRYVESMGMRARGYRIEAAQLEQL 125
Cdd:cd02423   2 GVVRQSYDFSCGPAALATLLRYYGGINITEQEVLKLML-------IRSEGFSMLDLKRYAEALGLKANGYRLNLDKLNAL 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15597149 126 KIPAIVLMEIRGYKHFVVLQRTQGEYVYVGDPALGHKRYALTEFAKGWNGIVFAV 180
Cdd:cd02423  75 QIPVIVLVNNGGYGHFVVIKGIDGDRVLVGDPALGNISMSREEFERIWTGNALFV 129
Peptidase_C39 pfam03412
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ...
 55-177 1.42e-21

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: 86.51  E-value: 1.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149    55 SCGAAALATILeKAYG--APLDEQAviqgMLAHADPEivrtqGFSMLDMKRYVESMGMRARGYRIEAAQLEQLKIPAIVL 132
Cdd:pfam03412  12 DCGLACLAMIL-KYYGsnVSLEELR----ELAGTPAE-----GTSLLGLKKAAEKLGFKAKAIKADLSELKELPLPFIAH 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 15597149   133 MEiRGYKHFVVLQRTQGEYVYVGDPALGHKRYALTEFAKGWNGIV 177
Cdd:pfam03412  82 WD-GNGGHFVVVYGIKKNKVLIADPAVGKIKLSREEFEKEWTGVA 125
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 56-177 7.57e-15

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: 73.05  E-value: 7.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149    56 CGAAALATILEKaYGA--PLDEQAVIQGmlahadpeiVRTQGFSMLDMKRYVESMGMRARGYRIEAAQLEQLKIPAIVLM 133
Cdd:TIGR03796  13 CGAASLAMILAY-YGRyvPLEELREECG---------VSRDGSKASNLLKAARSYGLEAKGFRKELDALAELPLPYIVFW 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15597149   134 EirgYKHFVVLQRTQGEYVYVGDPALGHKRYALTEFAKGWNGIV 177
Cdd:TIGR03796  83 N---FNHFVVVEGFRGGRVYLNDPALGPRTVSLEEFDESFTGVV 123
 
Name Accession Description Interval E-value
C39G COG3271
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, ...
 18-181 5.56e-70

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: 211.77  E-value: 5.56e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  18 AATLGFPALPGGGLVY-KQVQSIRERRFADLVEQKTDFSCGAAALATILEKAYGAPLDEQAVIQGMLAHADPeivRTQGF 96
Cdd:COG3271  15 AGSPAGSVLPGSGGGYsVPVKSLKELRFRNVVRQQYDYSCGAAALATLLNYHYGRPVSEAEVLEGMLTHGDQ---RRRGF 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  97 SMLDMKRYVESMGMRARGYRIEAAQLEQLKIPAIVLMEIRGYKHFVVLQRTQGEYVYVGDPALGHKRYALTEFAKGWNGI 176
Cdd:COG3271  92 SLLDMKRYLEALGLRADGYRLTLDDLAQLGIPAIVLINLGGYKHFVVVKGVDDGRVLLADPALGNRSLSREEFEKMWDGN 171


                ....*
gi 15597149 177 VFAVI 181
Cdd:COG3271 172 VLFVV 176
Peptidase_C39G cd02423
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 46-180 3.85e-53

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: 167.06  E-value: 3.85e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  46 DLVEQKTDFSCGAAALATILEKAYGAPLDEQAVIQGMLahadpeiVRTQGFSMLDMKRYVESMGMRARGYRIEAAQLEQL 125
Cdd:cd02423   2 GVVRQSYDFSCGPAALATLLRYYGGINITEQEVLKLML-------IRSEGFSMLDLKRYAEALGLKANGYRLNLDKLNAL 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15597149 126 KIPAIVLMEIRGYKHFVVLQRTQGEYVYVGDPALGHKRYALTEFAKGWNGIVFAV 180
Cdd:cd02423  75 QIPVIVLVNNGGYGHFVVIKGIDGDRVLVGDPALGNISMSREEFERIWTGNALFV 129
Peptidase_C39B cd02418
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 47-178 2.83e-22

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: 88.42  E-value: 2.83e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  47 LVEQKTDFSCGAAALATILeKAYGAPLDEQAVIQgmLAHADpeivrTQGFSMLDMKRYVESMGMRARGYRI--EAAQLEQ 124
Cdd:cd02418   3 YVLQVDEMDCGAACLAMIA-KYYGKNYSLAKLRE--LAGTD-----REGTSLLGLVKAAEKLGFETRAVKAdmDLFELKD 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15597149 125 LKIPAIVLMEIRG-YKHFVVLQRTQGEYVYVGDPALGHKRYALTEFAKGWNGIVF 178
Cdd:cd02418  75 IPLPFIAHVIKEWkLNHYVVVYKIKKKKILIADPAVGITKISKEEFEKEWTGVAL 129
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 47-203 4.80e-22

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: 93.75  E-value: 4.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  47 LVEQKTDFSCGAAALATILeKAYGAPLDEQAVIQGMlahadpeIVRTQGFSMLDMKRYVESMGMRARGYRIEAAQLEQLK 126
Cdd:COG2274   6 FVLQMEAADCGLACLAMIA-RYYGRPVSLEELREAL-------GVSRDGLSLLGLLRAARRLGLRARGVRLDLEELAELP 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597149 127 IPAIVLMEirgYKHFVVLQRTQGEYVYVGDPALGHKRYALTEFAKGWNGIVFavigqgydrgnpLLTPPEPLTARNR 203
Cdd:COG2274  78 LPAILHWD---GNHFVVLEGVDGDKVTIADPATGRRKLSLEEFAESWTGVAL------------LLEPTPEFDKRGE 139
Peptidase_C39 pfam03412
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ...
 55-177 1.42e-21

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: 86.51  E-value: 1.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149    55 SCGAAALATILeKAYG--APLDEQAviqgMLAHADPEivrtqGFSMLDMKRYVESMGMRARGYRIEAAQLEQLKIPAIVL 132
Cdd:pfam03412  12 DCGLACLAMIL-KYYGsnVSLEELR----ELAGTPAE-----GTSLLGLKKAAEKLGFKAKAIKADLSELKELPLPFIAH 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 15597149   133 MEiRGYKHFVVLQRTQGEYVYVGDPALGHKRYALTEFAKGWNGIV 177
Cdd:pfam03412  82 WD-GNGGHFVVVYGIKKNKVLIADPAVGKIKLSREEFEKEWTGVA 125
Peptidase_C39_like cd02259
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ...
 50-177 3.36e-17

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: 74.73  E-value: 3.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  50 QKTDFSCGAAALATILeKAYGAPLDEQAVIQgmlahadPEIVRTQGFSMLDMKRYVESMGMRARGYRIEAAQLEQLKIPA 129
Cdd:cd02259   1 GGGPLDCGLACLQMLL-RYFGIPVRRDVLLN-------AQQRRQQGLSLADLVSLANKLGLTAQGVKLPLAALSRLQLPA 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15597149 130 IVLmeiRGYKHFVVLQRTQGEYVYVGDP-ALGHKRYALTEFAKGWNGIV 177
Cdd:cd02259  73 LLL---WKQGHFVILYGADKGQVLIADPlEEGPVTLSESELEERWTGHW 118
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 56-177 7.57e-15

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: 73.05  E-value: 7.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149    56 CGAAALATILEKaYGA--PLDEQAVIQGmlahadpeiVRTQGFSMLDMKRYVESMGMRARGYRIEAAQLEQLKIPAIVLM 133
Cdd:TIGR03796  13 CGAASLAMILAY-YGRyvPLEELREECG---------VSRDGSKASNLLKAARSYGLEAKGFRKELDALAELPLPYIVFW 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15597149   134 EirgYKHFVVLQRTQGEYVYVGDPALGHKRYALTEFAKGWNGIV 177
Cdd:TIGR03796  83 N---FNHFVVVEGFRGGRVYLNDPALGPRTVSLEEFDESFTGVV 123
Peptidase_C39D cd02420
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 56-177 2.04e-13

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: 64.76  E-value: 2.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  56 CGAAALATILeKAYG--APLDEQAVIQGmlahadpeiVRTQGFSMLDMKRYVESMGMRARGYRIEAAQLEQLKIPAIVLM 133
Cdd:cd02420  12 CGAASLAIIL-AYYGryVPLSELRIACG---------VSRDGSNASNLLKAAREYGLTAKGYKKDLEALREVSLPAIVFW 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15597149 134 eirGYKHFVVLQRTQGEYVYVGDPALGHKRYALTEFAKGWNGIV 177
Cdd:cd02420  82 ---NFNHFLVVEGFDKRKVFLNDPATGRRTVSLEEFDQSFTGVV 122
Peptidase_C39C cd02419
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 91-176 2.93e-13

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: 64.20  E-value: 2.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  91 VRTQGFSMLDMKRYVESMGMRARGYRIEAAQLEQLKIPAIVLMEIrgyKHFVVLQRTQGEYVYVGDPALGHKRYALTEFA 170
Cdd:cd02419  39 VSLKGATLADLIDIAQQLGLSTRALRLDLEELGQLKLPCILHWDM---NHFVVLKKVSRRRIVIHDPALGKRKLSLEEAS 115


                ....*.
gi 15597149 171 KGWNGI 176
Cdd:cd02419 116 RHFTGV 121
Peptidase_C39E cd02424
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 47-180 1.07e-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, which contains Colicin V perocessing peptidase.


Pssm-ID: 239104 [Multi-domain]  Cd Length: 129  Bit Score: 57.35  E-value: 1.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  47 LVEQKTDFSCGAAALATILEKAYGAP--LDEQaVIQGMLAHadpeivrtQGFSMLDMKRYVESMGMRARGYRIEAAQLEQ 124
Cdd:cd02424   3 IIKQTDLNDCGIAVIQMLYNHYYKKKydLNEL-KIKANLKK--------NGLSIYDLENLAKKFGLETESYQGSFLEFLE 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597149 125 LKIPAIVLMEIRGYKHFVVLQRTQGEYVYVGDPALGHKRYALTEFAKGWNGIVFAV 180
Cdd:cd02424  74 LKNKFIILLKSNGLNHFVIVKKIKKNKFIVLDPKKGKYKITYKEFEKIFNNIIITV 129
Peptidase_C39F cd02425
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 47-177 9.17e-09

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: 51.88  E-value: 9.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  47 LVEQKTDFSCGAAALATILeKAYG--APLDEqaVIQGMLAHADpeivrtqGFSMLDMKRYVESMGMRARGYRIEAAQ-LE 123
Cdd:cd02425   3 PILQNNQTECGLACYAMIL-NYFGykVSLNE--LREKYELGRD-------GLSLSYLKQLLEEYGFKCKVYKISFKKnLY 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15597149 124 QLKIPAIVLMEIRgykHFVVLQRTQGEYVYVGDPALGHKRYALTEFAKGWNGIV 177
Cdd:cd02425  73 PLKLPVIIFWNNN---HFVVLEKIKKNKVTIVDPAIGRIKISIDEFLENFSGYI 123
Peptidase_C39A cd02549
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 56-174 3.12e-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 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: 48.17  E-value: 3.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  56 CGAAALATILEkAYGAPldeqaVIQGMLAHADPEIV---RTQGFSMLDMKRY-VESMGMRARGYRIEAAQLEQLK--IPA 129
Cdd:cd02549   7 CGPTSLAMVLS-YLGVK-----VTKPQLAAEGNTYDfakDGYGTYPKPIVSAaARKYGLVVRPLTGLLALLRQLAagHPV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15597149 130 IVLME----IRGYKHFVVL---QRTQgeYVYVGDPALG-HKRYALTEFAKGWN 174
Cdd:cd02549  81 IVSVNlgvsITPSGHAMVVigyDRKG--NVYVNDPGGGrRLVVSFDEFEKAWK 131
Peptidase_C39_likeA cd02417
A sub-family of peptidase C39 which contains Cyclolysin and Hemolysin processing peptidases. ...
 82-175 1.36e-03

A sub-family of peptidase C39 which contains Cyclolysin and Hemolysin processing peptidases. 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 this sub-family.


Pssm-ID: 239098 [Multi-domain]  Cd Length: 121  Bit Score: 37.61  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597149  82 MLAH-----ADPEIVR------TQGFSMLDMKRYVESMGMRARGYRIEAAQLEQLKIPAIVLmeIRGYKHFVVLQRTQGE 150
Cdd:cd02417  14 LLARyhgiaADPEQLRhefglaGEPFNSTELLLAAKSLGLKAKAVRQPVERLARLPLPALAW--DDDGGHFILAKLDGQK 91

                        90       100
                ....*....|....*....|....*..
gi 15597149 151 YVyVGDPAlGHK--RYALTEFAKGWNG 175
Cdd:cd02417  92 YL-IQDPI-SQRpeVLSREEFEARWSG 116
 
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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