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Conserved domains on  [gi|2523704672|ref|WP_286187648|]
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S24 family peptidase [Klebsiella sp. WP8-S18-ESBL-06]

Protein Classification

helix-turn-helix transcriptional regulator( domain architecture ID 11459250)

helix-turn-helix (HTH) transcriptional regulator similar to phage repressor protein CI and Pseudomonas aeruginosa HTH-type transcriptional regulator PrtR, which represses the expression of various pyocin genes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 10-140 1.49e-31

Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: prophages, transposons];


:

Pssm-ID: 442176  Cd Length: 121  Bit Score: 109.28  E-value: 1.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523704672  10 IDVLDFSVSAGPGVINsEFVEVLRSVEysvedarqmFNGRKQEQIRIINVRGDSMSGTIEPGDLLFVDISVQHFDGDGIY 89
Cdd:COG2932     1 VPLYDGEASAGGGAFN-EVEEPVDKLE---------FPGLPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDTEIRDGGIY 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2523704672  90 AFIYDDTSHVKRLQKMKD-KLLVISDNPTYRPWEpIEKEEMNKIFVFGKVIG 140
Cdd:COG2932    71 VVRTDGELLVKRLQRRPDgKLRLISDNPAYPPIE-IPPEDADEIEIIGRVVW 121
 
Name Accession Description Interval E-value
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 10-140 1.49e-31

Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: prophages, transposons];


Pssm-ID: 442176  Cd Length: 121  Bit Score: 109.28  E-value: 1.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523704672  10 IDVLDFSVSAGPGVINsEFVEVLRSVEysvedarqmFNGRKQEQIRIINVRGDSMSGTIEPGDLLFVDISVQHFDGDGIY 89
Cdd:COG2932     1 VPLYDGEASAGGGAFN-EVEEPVDKLE---------FPGLPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDTEIRDGGIY 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2523704672  90 AFIYDDTSHVKRLQKMKD-KLLVISDNPTYRPWEpIEKEEMNKIFVFGKVIG 140
Cdd:COG2932    71 VVRTDGELLVKRLQRRPDgKLRLISDNPAYPPIE-IPPEDADEIEIIGRVVW 121
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 55-136 6.73e-19

Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of single-stranded DNA within the bacterial cell. This family includes: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The LexA-like proteins contain two-domains: an N-terminal DNA binding domain and a C-terminal domain (CTD) that provides LexA dimerization as well as cleavage activity. They undergo autolysis, cleaving at an Ala-Gly or a Cys-Gly bond, separating the DNA-binding domain from the rest of the protein. In the presence of single-stranded DNA, the LexA, UmuD and MucA proteins interact with RecA, activating self cleavage, thus either derepressing transcription in the case of LexA or activating the lesion-bypass polymerase in the case of UmuD and MucA. The LexA proteins are serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases. LexA sequence homologs are found in almost all of the bacterial genomes sequenced to date, covering a large number of phyla, suggesting both, an ancient origin and a widespread distribution of lexA and the SOS response.


Pssm-ID: 119397 [Multi-domain]  Cd Length: 81  Bit Score: 75.67  E-value: 6.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523704672  55 RIINVRGDSMSGTIEPGDLLFVDISVQHFDGDgIYAFIYDDTSHVKRLQKMKD-KLLVISDNPTYRPWEpIEKEEMNKIF 133
Cdd:cd06529     1 FALRVKGDSMEPTIPDGDLVLVDPSDTPRDGD-IVVARLDGELTVKRLQRRGGgRLRLISDNPAYPPIE-IDEEELEIVG 78


                  ...
gi 2523704672 134 VFG 136
Cdd:cd06529    79 VVG 81
Peptidase_S24 pfam00717
Peptidase S24-like;
16-139 4.84e-18

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 74.55  E-value: 4.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523704672  16 SVSAG-PGVINSEFVEVLRSVEYSVEDARQMFngrkqeqirIINVRGDSMSGTIEPGDLLFVDISVQHFDGDgIYAFIYD 94
Cdd:pfam00717   5 RVAAGaPILAEEEIEGYLPLPESLLSPPGNLF---------ALRVKGDSMEPGIPDGDLVLVDPSREARNGD-IVVARLD 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2523704672  95 DTSHVKRLQKMKDKLLVISDNPTYRPWEpIEKEEMNKIfvFGKVI 139
Cdd:pfam00717  75 GEATVKRLYRDGGGIRLISLNPEYPPIE-LPAEDDVEI--IGRVV 116
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
57-139 2.17e-05

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 41.71  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523704672  57 INVRGDSM-SGTIEPGDLLFVDISVQHFDGDGIYAFIyDDTSHVKRLQKmKDKLLVISDNPTYRPWePIEKEEmnKIFVF 135
Cdd:PRK10276   54 VKASGDSMiDAGISDGDLLIVDSAITASHGDIVIAAV-DGEFTVKKLQL-RPTVQLIPMNSAYSPI-TISSED--TLDVF 128


                  ....
gi 2523704672 136 GKVI 139
Cdd:PRK10276  129 GVVT 132
sod_Ni_protease TIGR02754
nickel-type superoxide dismutase maturation protease; Members of this protein family are ...
 59-127 1.12e-03

nickel-type superoxide dismutase maturation protease; Members of this protein family are apparent proteases encoded adjacent to the genes for a nickel-type superoxide dismutase. This family belongs to the same larger family (see pfam00717) as signal peptidase I, an unusual serine protease suggested to have a Ser/Lys catalytic dyad. [Cellular processes, Detoxification, Protein fate, Protein modification and repair]


Pssm-ID: 274282 [Multi-domain]  Cd Length: 90  Bit Score: 36.28  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523704672  59 VRGDSMSGTIEPGDLLFVDISVQHFD----GDGIYAF--IYDDTSHVKRLQKMKDK-LLVISDNPT----YRPWEPIEKE 127
Cdd:TIGR02754   3 VTGVSMSPTLPPGDRIIVVPWLKIFRvppiGNVVVVRhpLQPYGLIIKRLAAVDDNgLFLLGDNPKastdSRQLGPVPRS 82
 
Name Accession Description Interval E-value
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 10-140 1.49e-31

Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: prophages, transposons];


Pssm-ID: 442176  Cd Length: 121  Bit Score: 109.28  E-value: 1.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523704672  10 IDVLDFSVSAGPGVINsEFVEVLRSVEysvedarqmFNGRKQEQIRIINVRGDSMSGTIEPGDLLFVDISVQHFDGDGIY 89
Cdd:COG2932     1 VPLYDGEASAGGGAFN-EVEEPVDKLE---------FPGLPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDTEIRDGGIY 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2523704672  90 AFIYDDTSHVKRLQKMKD-KLLVISDNPTYRPWEpIEKEEMNKIFVFGKVIG 140
Cdd:COG2932    71 VVRTDGELLVKRLQRRPDgKLRLISDNPAYPPIE-IPPEDADEIEIIGRVVW 121
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 55-136 6.73e-19

Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of single-stranded DNA within the bacterial cell. This family includes: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The LexA-like proteins contain two-domains: an N-terminal DNA binding domain and a C-terminal domain (CTD) that provides LexA dimerization as well as cleavage activity. They undergo autolysis, cleaving at an Ala-Gly or a Cys-Gly bond, separating the DNA-binding domain from the rest of the protein. In the presence of single-stranded DNA, the LexA, UmuD and MucA proteins interact with RecA, activating self cleavage, thus either derepressing transcription in the case of LexA or activating the lesion-bypass polymerase in the case of UmuD and MucA. The LexA proteins are serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases. LexA sequence homologs are found in almost all of the bacterial genomes sequenced to date, covering a large number of phyla, suggesting both, an ancient origin and a widespread distribution of lexA and the SOS response.


Pssm-ID: 119397 [Multi-domain]  Cd Length: 81  Bit Score: 75.67  E-value: 6.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523704672  55 RIINVRGDSMSGTIEPGDLLFVDISVQHFDGDgIYAFIYDDTSHVKRLQKMKD-KLLVISDNPTYRPWEpIEKEEMNKIF 133
Cdd:cd06529     1 FALRVKGDSMEPTIPDGDLVLVDPSDTPRDGD-IVVARLDGELTVKRLQRRGGgRLRLISDNPAYPPIE-IDEEELEIVG 78


                  ...
gi 2523704672 134 VFG 136
Cdd:cd06529    79 VVG 81
Peptidase_S24 pfam00717
Peptidase S24-like;
16-139 4.84e-18

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 74.55  E-value: 4.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523704672  16 SVSAG-PGVINSEFVEVLRSVEYSVEDARQMFngrkqeqirIINVRGDSMSGTIEPGDLLFVDISVQHFDGDgIYAFIYD 94
Cdd:pfam00717   5 RVAAGaPILAEEEIEGYLPLPESLLSPPGNLF---------ALRVKGDSMEPGIPDGDLVLVDPSREARNGD-IVVARLD 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2523704672  95 DTSHVKRLQKMKDKLLVISDNPTYRPWEpIEKEEMNKIfvFGKVI 139
Cdd:pfam00717  75 GEATVKRLYRDGGGIRLISLNPEYPPIE-LPAEDDVEI--IGRVV 116
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 55-138 1.26e-14

The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal peptidase families. The S24 LexA protein domains include: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The S26 type I signal peptidase (SPase) family also includes mitochondrial inner membrane protease (IMP)-like members. SPases are essential membrane-bound proteases which function to cleave away the amino-terminal signal peptide from the translocated pre-protein, thus playing a crucial role in the transport of proteins across membranes in all living organisms. All members in this superfamily are unique serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases.


Pssm-ID: 119396 [Multi-domain]  Cd Length: 84  Bit Score: 64.59  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523704672  55 RIINVRGDSMSGTIEPGDLLFVDISVQHFDGDGIYAFIYDDTS-HVKRLQKM--KDKLLVISDNPTYRPWEPIEKEEMNk 131
Cdd:cd06462     1 FALRVEGDSMEPTIPDGDLVLVDKSSYEPKRGDIVVFRLPGGElTVKRVIGLpgEGHYFLLGDNPNSPDSRIDGPPELD- 79


                  ....*..
gi 2523704672 132 ifVFGKV 138
Cdd:cd06462    80 --IVGVV 84
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 59-142 2.83e-11

SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms];


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 58.39  E-value: 2.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523704672  59 VRGDSMSG-TIEPGDLLFVDISVQHFDGDgIYAFIYDDTSHVKRLQKMKDKLLVISDNPTYrpwEPIEKEEMNkIFVFGK 137
Cdd:COG1974   117 VKGDSMIDaGILDGDLVIVDRQLEAENGD-IVVALIDGEATVKRLYKEGGRVRLQPENPAY---PPIIIEGDD-VEILGV 191


                  ....*
gi 2523704672 138 VIGSM 142
Cdd:COG1974   192 VVGVI 196
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
57-139 2.17e-05

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 41.71  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523704672  57 INVRGDSM-SGTIEPGDLLFVDISVQHFDGDGIYAFIyDDTSHVKRLQKmKDKLLVISDNPTYRPWePIEKEEmnKIFVF 135
Cdd:PRK10276   54 VKASGDSMiDAGISDGDLLIVDSAITASHGDIVIAAV-DGEFTVKKLQL-RPTVQLIPMNSAYSPI-TISSED--TLDVF 128


                  ....
gi 2523704672 136 GKVI 139
Cdd:PRK10276  129 GVVT 132
sod_Ni_protease TIGR02754
nickel-type superoxide dismutase maturation protease; Members of this protein family are ...
 59-127 1.12e-03

nickel-type superoxide dismutase maturation protease; Members of this protein family are apparent proteases encoded adjacent to the genes for a nickel-type superoxide dismutase. This family belongs to the same larger family (see pfam00717) as signal peptidase I, an unusual serine protease suggested to have a Ser/Lys catalytic dyad. [Cellular processes, Detoxification, Protein fate, Protein modification and repair]


Pssm-ID: 274282 [Multi-domain]  Cd Length: 90  Bit Score: 36.28  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523704672  59 VRGDSMSGTIEPGDLLFVDISVQHFD----GDGIYAF--IYDDTSHVKRLQKMKDK-LLVISDNPT----YRPWEPIEKE 127
Cdd:TIGR02754   3 VTGVSMSPTLPPGDRIIVVPWLKIFRvppiGNVVVVRhpLQPYGLIIKRLAAVDDNgLFLLGDNPKastdSRQLGPVPRS 82
 
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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