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Conserved domains on  [gi|1864364209|ref|WP_176745959|]
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GBS Bsp-like repeat-containing protein, partial [Streptococcus sp. HMSC061E03]

Protein Classification

peptidase C39 family protein( domain architecture ID 10553241)

uncharacterized peptidase C39 family protein; C39 mostly contains bacteriocin-processing endopeptidases that cleaves the double-glycine leader peptide from the precursors of various bacteriocins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GBS_Bsp-like super family cl17055
GBS Bsp-like repeat; This domain is found as a repeat in a number of Streptococcus proteins ...
 2-88 1.75e-18

GBS Bsp-like repeat; This domain is found as a repeat in a number of Streptococcus proteins including some hypothetical proteins and Bsp. Bsp is a protein of group B Streptococcus (GBS) which might control cell morphology.


The actual alignment was detected with superfamily member pfam08481:

Pssm-ID: 400671  Cd Length: 89  Bit Score: 78.11  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864364209   2 IKNVNSGAGTFTVTVDQAPQGRQIKNIRVAAWSKA-HQENLYWYSATPTGMHT-EITVSANNHGNEAGNYTTHVYVDYKD 79
Cdd:pfam08481   1 VQNYNANKGTFDVTVSGVSAPSGVKSVQVPVWSEAnGQDDLKWYTATKQSDGTyKVTVNIKNHKNETGTYNVHAYVTDTN 80


                  ....*....
gi 1864364209  80 GGVEGFNLG 88
Cdd:pfam08481  81 GKQKFLGAT 89
Peptidase_C39_like super family cl00296
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ...
 127-250 1.50e-13

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.


The actual alignment was detected with superfamily member cd02549:

Pssm-ID: 469710 [Multi-domain]  Cd Length: 141  Bit Score: 66.28  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864364209 127 GCVPTSLAMtftdIL----GRTILPTTVADylyNNTDSFNKGEAGTDSDGIV-AATRNWGLKSQLVNGAGGIAEALMAGK 201
Cdd:cd02549     6 GCGPTSLAM----VLsylgVKVTKPQLAAE---GNTYDFAKDGYGTYPKPIVsAAARKYGLVVRPLTGLLALLRQLAAGH 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1864364209 202 HVLAAVGNSQFTsDPYTHELVLHGYD-NGRTYVRDPYNSGnNGWYSINYL 250
Cdd:cd02549    79 PVIVSVNLGVSI-TPSGHAMVVIGYDrKGNVYVNDPGGGR-RLVVSFDEF 126
 
Name Accession Description Interval E-value
GBS_Bsp-like pfam08481
GBS Bsp-like repeat; This domain is found as a repeat in a number of Streptococcus proteins ...
 2-88 1.75e-18

GBS Bsp-like repeat; This domain is found as a repeat in a number of Streptococcus proteins including some hypothetical proteins and Bsp. Bsp is a protein of group B Streptococcus (GBS) which might control cell morphology.


Pssm-ID: 400671  Cd Length: 89  Bit Score: 78.11  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864364209   2 IKNVNSGAGTFTVTVDQAPQGRQIKNIRVAAWSKA-HQENLYWYSATPTGMHT-EITVSANNHGNEAGNYTTHVYVDYKD 79
Cdd:pfam08481   1 VQNYNANKGTFDVTVSGVSAPSGVKSVQVPVWSEAnGQDDLKWYTATKQSDGTyKVTVNIKNHKNETGTYNVHAYVTDTN 80


                  ....*....
gi 1864364209  80 GGVEGFNLG 88
Cdd:pfam08481  81 GKQKFLGAT 89
Peptidase_C39A cd02549
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 127-250 1.50e-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 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: 66.28  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864364209 127 GCVPTSLAMtftdIL----GRTILPTTVADylyNNTDSFNKGEAGTDSDGIV-AATRNWGLKSQLVNGAGGIAEALMAGK 201
Cdd:cd02549     6 GCGPTSLAM----VLsylgVKVTKPQLAAE---GNTYDFAKDGYGTYPKPIVsAAARKYGLVVRPLTGLLALLRQLAAGH 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1864364209 202 HVLAAVGNSQFTsDPYTHELVLHGYD-NGRTYVRDPYNSGnNGWYSINYL 250
Cdd:cd02549    79 PVIVSVNLGVSI-TPSGHAMVVIGYDrKGNVYVNDPGGGR-RLVVSFDEF 126
Peptidase_C39_2 pfam13529
Peptidase_C39 like family;
105-236 2.89e-03

Peptidase_C39 like family;


Pssm-ID: 379241 [Multi-domain]  Cd Length: 139  Bit Score: 37.04  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864364209 105 YYSQRDPRWAGkwygvsnvdqsgCVPTSLAMTFtDILGRTILPTTVAD-YLYNNTDSFNKGEAGT----DSDG-----IV 174
Cdd:pfam13529   4 YYNQLDELPNG------------CGPTSLAMVL-SYLGITVTQDELAKeIGTNPDGNPNTGFVGNpydkSGYGvynppIV 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864364209 175 AATRNWGLKSQLVNGA--GGIAEALMAGKHVLAAVGNSQFTSDPYT---HELVLHGYD--NGRTYVRDP 236
Cdd:pfam13529  71 ALAEKYGLKVTDITGSsfDEVIRLLDAGIPVVVSTTTFGPLNYYFTssgHLVVIVGYDdkGDYVYVNDP 139
 
Name Accession Description Interval E-value
GBS_Bsp-like pfam08481
GBS Bsp-like repeat; This domain is found as a repeat in a number of Streptococcus proteins ...
 2-88 1.75e-18

GBS Bsp-like repeat; This domain is found as a repeat in a number of Streptococcus proteins including some hypothetical proteins and Bsp. Bsp is a protein of group B Streptococcus (GBS) which might control cell morphology.


Pssm-ID: 400671  Cd Length: 89  Bit Score: 78.11  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864364209   2 IKNVNSGAGTFTVTVDQAPQGRQIKNIRVAAWSKA-HQENLYWYSATPTGMHT-EITVSANNHGNEAGNYTTHVYVDYKD 79
Cdd:pfam08481   1 VQNYNANKGTFDVTVSGVSAPSGVKSVQVPVWSEAnGQDDLKWYTATKQSDGTyKVTVNIKNHKNETGTYNVHAYVTDTN 80


                  ....*....
gi 1864364209  80 GGVEGFNLG 88
Cdd:pfam08481  81 GKQKFLGAT 89
Peptidase_C39A cd02549
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 127-250 1.50e-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 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: 66.28  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864364209 127 GCVPTSLAMtftdIL----GRTILPTTVADylyNNTDSFNKGEAGTDSDGIV-AATRNWGLKSQLVNGAGGIAEALMAGK 201
Cdd:cd02549     6 GCGPTSLAM----VLsylgVKVTKPQLAAE---GNTYDFAKDGYGTYPKPIVsAAARKYGLVVRPLTGLLALLRQLAAGH 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1864364209 202 HVLAAVGNSQFTsDPYTHELVLHGYD-NGRTYVRDPYNSGnNGWYSINYL 250
Cdd:cd02549    79 PVIVSVNLGVSI-TPSGHAMVVIGYDrKGNVYVNDPGGGR-RLVVSFDEF 126
Peptidase_C39_2 pfam13529
Peptidase_C39 like family;
105-236 2.89e-03

Peptidase_C39 like family;


Pssm-ID: 379241 [Multi-domain]  Cd Length: 139  Bit Score: 37.04  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864364209 105 YYSQRDPRWAGkwygvsnvdqsgCVPTSLAMTFtDILGRTILPTTVAD-YLYNNTDSFNKGEAGT----DSDG-----IV 174
Cdd:pfam13529   4 YYNQLDELPNG------------CGPTSLAMVL-SYLGITVTQDELAKeIGTNPDGNPNTGFVGNpydkSGYGvynppIV 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864364209 175 AATRNWGLKSQLVNGA--GGIAEALMAGKHVLAAVGNSQFTSDPYT---HELVLHGYD--NGRTYVRDP 236
Cdd:pfam13529  71 ALAEKYGLKVTDITGSsfDEVIRLLDAGIPVVVSTTTFGPLNYYFTssgHLVVIVGYDdkGDYVYVNDP 139
 
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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