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Conserved domains on  [gi|490364893|ref|WP_004244558|]
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MULTISPECIES: ATP-dependent Clp protease adapter ClpS [Enterobacterales]

Protein Classification

ATP-dependent Clp protease adaptor ClpS( domain architecture ID 10495739)

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 pfam02617
ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent ...
 21-100 1.17e-46

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: 144.14  E-value: 1.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364893   21 EPPAMYKVILNNDDYTPMDFVVEVLTMYFFLNEEKATQIMLDVHHKGKGVCGVYSADIAETKVAQVNQYARENGHPLLCT 100
Cdd:pfam02617   1 KEPPMYKVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVVGVYTYDIAETKVAQVHQLARENGFPLRCT 80
 
Name Accession Description Interval E-value
ClpS pfam02617
ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent ...
 21-100 1.17e-46

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: 144.14  E-value: 1.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364893   21 EPPAMYKVILNNDDYTPMDFVVEVLTMYFFLNEEKATQIMLDVHHKGKGVCGVYSADIAETKVAQVNQYARENGHPLLCT 100
Cdd:pfam02617   1 KEPPMYKVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVVGVYTYDIAETKVAQVHQLARENGFPLRCT 80
clpS PRK00033
ATP-dependent Clp protease adaptor protein ClpS; Reviewed
 14-104 1.58e-42

ATP-dependent Clp protease adaptor protein ClpS; Reviewed


Pssm-ID: 178809  Cd Length: 100  Bit Score: 134.31  E-value: 1.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364893  14 EKVSQLNEPPAMYKVILNNDDYTPMDFVVEVLTMYFFLNEEKATQIMLDVHHKGKGVCGVYSADIAETKVAQVNQyaren 93
Cdd:PRK00033  16 EKVEPKLKPPPMYKVLLHNDDYTPMEFVVYVLQKFFGYDRERATQIMLEVHNEGKAVVGVCTREVAETKVEQVHQ----- 90

                         90
                 ....*....|.
gi 490364893  94 gHPLLCTLEKA 104
Cdd:PRK00033  91 -HGLLCTMEKD 100
ClpS COG2127
ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein ...
 8-104 5.36e-42

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


Pssm-ID: 441730  Cd Length: 94  Bit Score: 132.95  E-value: 5.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364893   8 TETTLGEKVSQLNEPPAMYKVILNNDDYTPMDFVVEVLTMYFFLNEEKATQIMLDVHHKGKGVCGVYSADIAETKVAQVN 87
Cdd:COG2127    3 PDTEPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGTREIAETKVEQVH 82

                         90
                 ....*....|....*..
gi 490364893  88 QYArenghpLLCTLEKA 104
Cdd:COG2127   83 DYG------LQATIEPA 93
 
Name Accession Description Interval E-value
ClpS pfam02617
ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent ...
 21-100 1.17e-46

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: 144.14  E-value: 1.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364893   21 EPPAMYKVILNNDDYTPMDFVVEVLTMYFFLNEEKATQIMLDVHHKGKGVCGVYSADIAETKVAQVNQYARENGHPLLCT 100
Cdd:pfam02617   1 KEPPMYKVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVVGVYTYDIAETKVAQVHQLARENGFPLRCT 80
clpS PRK00033
ATP-dependent Clp protease adaptor protein ClpS; Reviewed
 14-104 1.58e-42

ATP-dependent Clp protease adaptor protein ClpS; Reviewed


Pssm-ID: 178809  Cd Length: 100  Bit Score: 134.31  E-value: 1.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364893  14 EKVSQLNEPPAMYKVILNNDDYTPMDFVVEVLTMYFFLNEEKATQIMLDVHHKGKGVCGVYSADIAETKVAQVNQyaren 93
Cdd:PRK00033  16 EKVEPKLKPPPMYKVLLHNDDYTPMEFVVYVLQKFFGYDRERATQIMLEVHNEGKAVVGVCTREVAETKVEQVHQ----- 90

                         90
                 ....*....|.
gi 490364893  94 gHPLLCTLEKA 104
Cdd:PRK00033  91 -HGLLCTMEKD 100
ClpS COG2127
ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein ...
 8-104 5.36e-42

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


Pssm-ID: 441730  Cd Length: 94  Bit Score: 132.95  E-value: 5.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364893   8 TETTLGEKVSQLNEPPAMYKVILNNDDYTPMDFVVEVLTMYFFLNEEKATQIMLDVHHKGKGVCGVYSADIAETKVAQVN 87
Cdd:COG2127    3 PDTEPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGTREIAETKVEQVH 82

                         90
                 ....*....|....*..
gi 490364893  88 QYArenghpLLCTLEKA 104
Cdd:COG2127   83 DYG------LQATIEPA 93
clpS PRK13019
ATP-dependent Clp protease adapter ClpS;
21-85 5.14e-16

ATP-dependent Clp protease adapter ClpS;


Pssm-ID: 183845  Cd Length: 94  Bit Score: 66.88  E-value: 5.14e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490364893  21 EPPAMYKVILNNDDYTPMDFVVEVLTMYFF-LNEEKATQIMLDVHHKGKGVCGVYSADIAETKVAQ 85
Cdd:PRK13019  17 ERYPLYKVIVLNDDFNTFEHVVNCLLKAIPgMSEDRAWRLMITAHKEGSAVVWVGPLEQAELYHQQ 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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