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Conserved domains on  [gi|489502010|ref|WP_003406906|]
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MULTISPECIES: ATP-dependent Clp protease adapter ClpS [Mycobacterium]

Protein Classification

ATP-dependent Clp protease adaptor ClpS( domain architecture ID 10011103)

ATP-dependent Clp protease adaptor ClpS modulates the specificity of protein degradation by the ClpAP chaperone-protease complex; binds to the N-terminal substrate-domain of ClpA thereby redirecting degradation by ClpAP towards aggregated proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
clpS PRK00033
ATP-dependent Clp protease adaptor protein ClpS; Reviewed
 1-100 2.74e-42

ATP-dependent Clp protease adaptor protein ClpS; Reviewed


:

Pssm-ID: 178809  Cd Length: 100  Bit Score: 133.54  E-value: 2.74e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502010   1 MAVVSAPAKPGTTWQRESAPVDVTDRAWVTIVWDDPVNLMSYVTYVFQKLFGYSEPHATKLMLQVHNEGKAVVSAGSRES 80
Cdd:PRK00033   1 MGKTNDWDDMSALVLEKVEPKLKPPPMYKVLLHNDDYTPMEFVVYVLQKFFGYDRERATQIMLEVHNEGKAVVGVCTREV 80

                         90       100
                 ....*....|....*....|
gi 489502010  81 MEVDVSKLHAAGLWATMQQD 100
Cdd:PRK00033  81 AETKVEQVHQHGLLCTMEKD 100
 
Name Accession Description Interval E-value
clpS PRK00033
ATP-dependent Clp protease adaptor protein ClpS; Reviewed
 1-100 2.74e-42

ATP-dependent Clp protease adaptor protein ClpS; Reviewed


Pssm-ID: 178809  Cd Length: 100  Bit Score: 133.54  E-value: 2.74e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502010   1 MAVVSAPAKPGTTWQRESAPVDVTDRAWVTIVWDDPVNLMSYVTYVFQKLFGYSEPHATKLMLQVHNEGKAVVSAGSRES 80
Cdd:PRK00033   1 MGKTNDWDDMSALVLEKVEPKLKPPPMYKVLLHNDDYTPMEFVVYVLQKFFGYDRERATQIMLEVHNEGKAVVGVCTREV 80

                         90       100
                 ....*....|....*....|
gi 489502010  81 MEVDVSKLHAAGLWATMQQD 100
Cdd:PRK00033  81 AETKVEQVHQHGLLCTMEKD 100
ClpS COG2127
ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein ...
 10-100 6.11e-38

ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441730  Cd Length: 94  Bit Score: 122.55  E-value: 6.11e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502010  10 PGTTWQRESAPVDVTDRAWVTIVWDDPVNLMSYVTYVFQKLFGYSEPHATKLMLQVHNEGKAVVSAGSRESMEVDVSKLH 89
Cdd:COG2127    3 PDTEPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGTREIAETKVEQVH 82

                         90
                 ....*....|.
gi 489502010  90 AAGLWATMQQD 100
Cdd:COG2127   83 DYGLQATIEPA 93
ClpS pfam02617
ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent ...
 24-96 2.96e-26

ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent protein degradation is performed by several different chaperone-protease pairs, including ClpAP. ClpS directly influences the ClpAP machine by binding to the N-terminal domain of the chaperone ClpA. The degradation of ClpAP substrates, both SsrA-tagged proteins and ClpA itself, is specifically inhibited by ClpS. ClpS modifies ClpA substrate specificity, potentially redirecting degradation by ClpAP toward aggregated proteins.


Pssm-ID: 460621  Cd Length: 80  Bit Score: 92.53  E-value: 2.96e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489502010   24 TDRAWVTIVWDDPVNLMSYVTYVFQKLFGYSEPHATKLMLQVHNEGKAVVSAGSRESMEVDVSKLHAA------GLWAT 96
Cdd:pfam02617   2 EPPMYKVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVVGVYTYDIAETKVAQVHQLarengfPLRCT 80
 
Name Accession Description Interval E-value
clpS PRK00033
ATP-dependent Clp protease adaptor protein ClpS; Reviewed
 1-100 2.74e-42

ATP-dependent Clp protease adaptor protein ClpS; Reviewed


Pssm-ID: 178809  Cd Length: 100  Bit Score: 133.54  E-value: 2.74e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502010   1 MAVVSAPAKPGTTWQRESAPVDVTDRAWVTIVWDDPVNLMSYVTYVFQKLFGYSEPHATKLMLQVHNEGKAVVSAGSRES 80
Cdd:PRK00033   1 MGKTNDWDDMSALVLEKVEPKLKPPPMYKVLLHNDDYTPMEFVVYVLQKFFGYDRERATQIMLEVHNEGKAVVGVCTREV 80

                         90       100
                 ....*....|....*....|
gi 489502010  81 MEVDVSKLHAAGLWATMQQD 100
Cdd:PRK00033  81 AETKVEQVHQHGLLCTMEKD 100
ClpS COG2127
ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein ...
 10-100 6.11e-38

ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441730  Cd Length: 94  Bit Score: 122.55  E-value: 6.11e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502010  10 PGTTWQRESAPVDVTDRAWVTIVWDDPVNLMSYVTYVFQKLFGYSEPHATKLMLQVHNEGKAVVSAGSRESMEVDVSKLH 89
Cdd:COG2127    3 PDTEPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGTREIAETKVEQVH 82

                         90
                 ....*....|.
gi 489502010  90 AAGLWATMQQD 100
Cdd:COG2127   83 DYGLQATIEPA 93
ClpS pfam02617
ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent ...
 24-96 2.96e-26

ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent protein degradation is performed by several different chaperone-protease pairs, including ClpAP. ClpS directly influences the ClpAP machine by binding to the N-terminal domain of the chaperone ClpA. The degradation of ClpAP substrates, both SsrA-tagged proteins and ClpA itself, is specifically inhibited by ClpS. ClpS modifies ClpA substrate specificity, potentially redirecting degradation by ClpAP toward aggregated proteins.


Pssm-ID: 460621  Cd Length: 80  Bit Score: 92.53  E-value: 2.96e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489502010   24 TDRAWVTIVWDDPVNLMSYVTYVFQKLFGYSEPHATKLMLQVHNEGKAVVSAGSRESMEVDVSKLHAA------GLWAT 96
Cdd:pfam02617   2 EPPMYKVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVVGVYTYDIAETKVAQVHQLarengfPLRCT 80
clpS PRK13019
ATP-dependent Clp protease adapter ClpS;
10-97 2.55e-08

ATP-dependent Clp protease adapter ClpS;


Pssm-ID: 183845  Cd Length: 94  Bit Score: 47.24  E-value: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502010  10 PGTTWQRESAPVDVTDRAWVTIVWDDPVNLMSYVTYVFQK-LFGYSEPHATKLMLQVHNEGKAVVSAGSRESMEVDVSKL 88
Cdd:PRK13019   4 PATKPKTKTKPKLERYPLYKVIVLNDDFNTFEHVVNCLLKaIPGMSEDRAWRLMITAHKEGSAVVWVGPLEQAELYHQQL 83


                 ....*....
gi 489502010  89 HAAGLwaTM 97
Cdd:PRK13019  84 TDAGL--TM 90
 
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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