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Conserved domains on  [gi|1393193103|gb|AWN54916|]
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ATP-dependent Clp protease adapter ClpS [Methylobacterium sp. 17Sr1-1]

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
 22-127 2.89e-48

ATP-dependent Clp protease adaptor protein ClpS; Reviewed


:

Pssm-ID: 178809  Cd Length: 100  Bit Score: 149.72  E-value: 2.89e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393193103  22 PGNGNGDGRSGTAVITRTKPRTKRPNLYRVLLLNDDYTPMEFVVHVVERFFNKSREDATRIMLHVHQNGVGECGIFTYEV 101
Cdd:PRK00033    1 MGKTNDWDDMSALVLEKVEPKLKPPPMYKVLLHNDDYTPMEFVVYVLQKFFGYDRERATQIMLEVHNEGKAVVGVCTREV 80

                          90       100
                  ....*....|....*....|....*.
gi 1393193103 102 AETKVTQVmdfarkHQHPLQCVMEKK 127
Cdd:PRK00033   81 AETKVEQV------HQHGLLCTMEKD 100
 
Name Accession Description Interval E-value
clpS PRK00033
ATP-dependent Clp protease adaptor protein ClpS; Reviewed
 22-127 2.89e-48

ATP-dependent Clp protease adaptor protein ClpS; Reviewed


Pssm-ID: 178809  Cd Length: 100  Bit Score: 149.72  E-value: 2.89e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393193103  22 PGNGNGDGRSGTAVITRTKPRTKRPNLYRVLLLNDDYTPMEFVVHVVERFFNKSREDATRIMLHVHQNGVGECGIFTYEV 101
Cdd:PRK00033    1 MGKTNDWDDMSALVLEKVEPKLKPPPMYKVLLHNDDYTPMEFVVYVLQKFFGYDRERATQIMLEVHNEGKAVVGVCTREV 80

                          90       100
                  ....*....|....*....|....*.
gi 1393193103 102 AETKVTQVmdfarkHQHPLQCVMEKK 127
Cdd:PRK00033   81 AETKVEQV------HQHGLLCTMEKD 100
ClpS COG2127
ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein ...
 31-126 1.32e-44

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


Pssm-ID: 441730  Cd Length: 94  Bit Score: 140.27  E-value: 1.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393193103  31 SGTAVITRTKPRTKRPNLYRVLLLNDDYTPMEFVVHVVERFFNKSREDATRIMLHVHQNGVGECGIFTYEVAETKVTQVM 110
Cdd:COG2127     3 PDTEPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGTREIAETKVEQVH 82

                          90
                  ....*....|....*.
gi 1393193103 111 DFArkhqhpLQCVMEK 126
Cdd:COG2127    83 DYG------LQATIEP 92
ClpS pfam02617
ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent ...
 44-122 1.42e-44

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: 139.91  E-value: 1.42e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393193103  44 KRPNLYRVLLLNDDYTPMEFVVHVVERFFNKSREDATRIMLHVHQNGVGECGIFTYEVAETKVTQVMDFARKHQHPLQC 122
Cdd:pfam02617   1 KEPPMYKVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVVGVYTYDIAETKVAQVHQLARENGFPLRC 79
 
Name Accession Description Interval E-value
clpS PRK00033
ATP-dependent Clp protease adaptor protein ClpS; Reviewed
 22-127 2.89e-48

ATP-dependent Clp protease adaptor protein ClpS; Reviewed


Pssm-ID: 178809  Cd Length: 100  Bit Score: 149.72  E-value: 2.89e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393193103  22 PGNGNGDGRSGTAVITRTKPRTKRPNLYRVLLLNDDYTPMEFVVHVVERFFNKSREDATRIMLHVHQNGVGECGIFTYEV 101
Cdd:PRK00033    1 MGKTNDWDDMSALVLEKVEPKLKPPPMYKVLLHNDDYTPMEFVVYVLQKFFGYDRERATQIMLEVHNEGKAVVGVCTREV 80

                          90       100
                  ....*....|....*....|....*.
gi 1393193103 102 AETKVTQVmdfarkHQHPLQCVMEKK 127
Cdd:PRK00033   81 AETKVEQV------HQHGLLCTMEKD 100
ClpS COG2127
ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein ...
 31-126 1.32e-44

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


Pssm-ID: 441730  Cd Length: 94  Bit Score: 140.27  E-value: 1.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393193103  31 SGTAVITRTKPRTKRPNLYRVLLLNDDYTPMEFVVHVVERFFNKSREDATRIMLHVHQNGVGECGIFTYEVAETKVTQVM 110
Cdd:COG2127     3 PDTEPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGTREIAETKVEQVH 82

                          90
                  ....*....|....*.
gi 1393193103 111 DFArkhqhpLQCVMEK 126
Cdd:COG2127    83 DYG------LQATIEP 92
ClpS pfam02617
ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent ...
 44-122 1.42e-44

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: 139.91  E-value: 1.42e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393193103  44 KRPNLYRVLLLNDDYTPMEFVVHVVERFFNKSREDATRIMLHVHQNGVGECGIFTYEVAETKVTQVMDFARKHQHPLQC 122
Cdd:pfam02617   1 KEPPMYKVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVVGVYTYDIAETKVAQVHQLARENGFPLRC 79
clpS PRK13019
ATP-dependent Clp protease adapter ClpS;
32-111 5.97e-20

ATP-dependent Clp protease adapter ClpS;


Pssm-ID: 183845  Cd Length: 94  Bit Score: 78.05  E-value: 5.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393193103  32 GTAVITRTKPRTKRPNLYRVLLLNDDYTPMEFVVHVVERF-FNKSREDATRIMLHVHQNGVGECGIFTYEVAETKVTQVM 110
Cdd:PRK13019    5 ATKPKTKTKPKLERYPLYKVIVLNDDFNTFEHVVNCLLKAiPGMSEDRAWRLMITAHKEGSAVVWVGPLEQAELYHQQLT 84


                  .
gi 1393193103 111 D 111
Cdd:PRK13019   85 D 85
 
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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