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Conserved domains on  [gi|1012714570|ref|WP_062817271|]
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MULTISPECIES: ATP-dependent Clp protease adapter ClpS [unclassified Alcanivorax]

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 ...
 35-113 1.66e-45

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: 141.83  E-value: 1.66e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1012714570  35 KPPSMYKVLMLNDDYTPMDFVVEILEDFFNLGREQATRVMLTVHTEGKAVCGVYPQDIAETKATQVVEYARENQHPLMC 113
Cdd:pfam02617   1 KEPPMYKVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVVGVYTYDIAETKVAQVHQLARENGFPLRC 79
 
Name Accession Description Interval E-value
ClpS pfam02617
ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent ...
 35-113 1.66e-45

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: 141.83  E-value: 1.66e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1012714570  35 KPPSMYKVLMLNDDYTPMDFVVEILEDFFNLGREQATRVMLTVHTEGKAVCGVYPQDIAETKATQVVEYARENQHPLMC 113
Cdd:pfam02617   1 KEPPMYKVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVVGVYTYDIAETKVAQVHQLARENGFPLRC 79
clpS PRK00033
ATP-dependent Clp protease adaptor protein ClpS; Reviewed
 14-118 4.46e-44

ATP-dependent Clp protease adaptor protein ClpS; Reviewed


Pssm-ID: 178809  Cd Length: 100  Bit Score: 138.93  E-value: 4.46e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012714570  14 DSPSDPDRHGDLAVEEARPKLKPPSMYKVLMLNDDYTPMDFVVEILEDFFNLGREQATRVMLTVHTEGKAVCGVYPQDIA 93
Cdd:PRK00033    2 GKTNDWDDMSALVLEKVEPKLKPPPMYKVLLHNDDYTPMEFVVYVLQKFFGYDRERATQIMLEVHNEGKAVVGVCTREVA 81

                          90       100
                  ....*....|....*....|....*
gi 1012714570  94 ETKATQVveyareNQHPLMCQVEKA 118
Cdd:PRK00033   82 ETKVEQV------HQHGLLCTMEKD 100
ClpS COG2127
ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein ...
 23-118 9.00e-44

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


Pssm-ID: 441730  Cd Length: 94  Bit Score: 137.96  E-value: 9.00e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012714570  23 GDLAVEEARPKLKPPSMYKVLMLNDDYTPMDFVVEILEDFFNLGREQATRVMLTVHTEGKAVCGVYPQDIAETKATQVVE 102
Cdd:COG2127     4 DTEPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGTREIAETKVEQVHD 83

                          90
                  ....*....|....*.
gi 1012714570 103 YArenqhpLMCQVEKA 118
Cdd:COG2127    84 YG------LQATIEPA 93
 
Name Accession Description Interval E-value
ClpS pfam02617
ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent ...
 35-113 1.66e-45

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: 141.83  E-value: 1.66e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1012714570  35 KPPSMYKVLMLNDDYTPMDFVVEILEDFFNLGREQATRVMLTVHTEGKAVCGVYPQDIAETKATQVVEYARENQHPLMC 113
Cdd:pfam02617   1 KEPPMYKVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVVGVYTYDIAETKVAQVHQLARENGFPLRC 79
clpS PRK00033
ATP-dependent Clp protease adaptor protein ClpS; Reviewed
 14-118 4.46e-44

ATP-dependent Clp protease adaptor protein ClpS; Reviewed


Pssm-ID: 178809  Cd Length: 100  Bit Score: 138.93  E-value: 4.46e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012714570  14 DSPSDPDRHGDLAVEEARPKLKPPSMYKVLMLNDDYTPMDFVVEILEDFFNLGREQATRVMLTVHTEGKAVCGVYPQDIA 93
Cdd:PRK00033    2 GKTNDWDDMSALVLEKVEPKLKPPPMYKVLLHNDDYTPMEFVVYVLQKFFGYDRERATQIMLEVHNEGKAVVGVCTREVA 81

                          90       100
                  ....*....|....*....|....*
gi 1012714570  94 ETKATQVveyareNQHPLMCQVEKA 118
Cdd:PRK00033   82 ETKVEQV------HQHGLLCTMEKD 100
ClpS COG2127
ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein ...
 23-118 9.00e-44

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


Pssm-ID: 441730  Cd Length: 94  Bit Score: 137.96  E-value: 9.00e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012714570  23 GDLAVEEARPKLKPPSMYKVLMLNDDYTPMDFVVEILEDFFNLGREQATRVMLTVHTEGKAVCGVYPQDIAETKATQVVE 102
Cdd:COG2127     4 DTEPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGTREIAETKVEQVHD 83

                          90
                  ....*....|....*.
gi 1012714570 103 YArenqhpLMCQVEKA 118
Cdd:COG2127    84 YG------LQATIEPA 93
clpS PRK13019
ATP-dependent Clp protease adapter ClpS;
27-99 3.08e-23

ATP-dependent Clp protease adapter ClpS;


Pssm-ID: 183845  Cd Length: 94  Bit Score: 85.76  E-value: 3.08e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1012714570  27 VEEARPKLKPPSMYKVLMLNDDYTPMDFVVE-ILEDFFNLGREQATRVMLTVHTEGKAVCGVYPQDIAETKATQ 99
Cdd:PRK13019    9 KTKTKPKLERYPLYKVIVLNDDFNTFEHVVNcLLKAIPGMSEDRAWRLMITAHKEGSAVVWVGPLEQAELYHQQ 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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