NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1733551949|dbj|GER01369|]
View 

ATP-dependent Clp protease adapter protein ClpS [Iodidimonas gelatinilytica]

Protein Classification

ATP-dependent Clp protease adaptor ClpS( domain architecture ID 10005389)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ClpS COG2127
ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein ...
 13-110 8.37e-47

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


:

Pssm-ID: 441730  Cd Length: 94  Bit Score: 145.28  E-value: 8.37e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551949  13 SPSTGLLTKTQPKTKKPSMYKVLMLNDDFTPMDFVIHVLKRFFRMSSEQATRVMLHVHQKGVGVCGVFTYEIAETKANQV 92
Cdd:COG2127     2 SPDTEPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGTREIAETKVEQV 81

                          90
                  ....*....|....*...
gi 1733551949  93 VDYAqkhhhpLQCTLEKE 110
Cdd:COG2127    82 HDYG------LQATIEPA 93
 
Name Accession Description Interval E-value
ClpS COG2127
ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein ...
 13-110 8.37e-47

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


Pssm-ID: 441730  Cd Length: 94  Bit Score: 145.28  E-value: 8.37e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551949  13 SPSTGLLTKTQPKTKKPSMYKVLMLNDDFTPMDFVIHVLKRFFRMSSEQATRVMLHVHQKGVGVCGVFTYEIAETKANQV 92
Cdd:COG2127     2 SPDTEPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGTREIAETKVEQV 81

                          90
                  ....*....|....*...
gi 1733551949  93 VDYAqkhhhpLQCTLEKE 110
Cdd:COG2127    82 HDYG------LQATIEPA 93
ClpS pfam02617
ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent ...
 27-106 4.78e-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: 137.60  E-value: 4.78e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551949  27 KKPSMYKVLMLNDDFTPMDFVIHVLKRFFRMSSEQATRVMLHVHQKGVGVCGVFTYEIAETKANQVVDYAQKHHHPLQCT 106
Cdd:pfam02617   1 KEPPMYKVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVVGVYTYDIAETKVAQVHQLARENGFPLRCT 80
clpS PRK00033
ATP-dependent Clp protease adaptor protein ClpS; Reviewed
 13-110 2.85e-43

ATP-dependent Clp protease adaptor protein ClpS; Reviewed


Pssm-ID: 178809  Cd Length: 100  Bit Score: 136.62  E-value: 2.85e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551949  13 SPSTGLLTKTQPKTKKPSMYKVLMLNDDFTPMDFVIHVLKRFFRMSSEQATRVMLHVHQKGVGVCGVFTYEIAETKANQV 92
Cdd:PRK00033    9 DMSALVLEKVEPKLKPPPMYKVLLHNDDYTPMEFVVYVLQKFFGYDRERATQIMLEVHNEGKAVVGVCTREVAETKVEQV 88

                          90
                  ....*....|....*...
gi 1733551949  93 vdyaqkHHHPLQCTLEKE 110
Cdd:PRK00033   89 ------HQHGLLCTMEKD 100
 
Name Accession Description Interval E-value
ClpS COG2127
ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein ...
 13-110 8.37e-47

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


Pssm-ID: 441730  Cd Length: 94  Bit Score: 145.28  E-value: 8.37e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551949  13 SPSTGLLTKTQPKTKKPSMYKVLMLNDDFTPMDFVIHVLKRFFRMSSEQATRVMLHVHQKGVGVCGVFTYEIAETKANQV 92
Cdd:COG2127     2 SPDTEPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGTREIAETKVEQV 81

                          90
                  ....*....|....*...
gi 1733551949  93 VDYAqkhhhpLQCTLEKE 110
Cdd:COG2127    82 HDYG------LQATIEPA 93
ClpS pfam02617
ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent ...
 27-106 4.78e-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: 137.60  E-value: 4.78e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551949  27 KKPSMYKVLMLNDDFTPMDFVIHVLKRFFRMSSEQATRVMLHVHQKGVGVCGVFTYEIAETKANQVVDYAQKHHHPLQCT 106
Cdd:pfam02617   1 KEPPMYKVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVVGVYTYDIAETKVAQVHQLARENGFPLRCT 80
clpS PRK00033
ATP-dependent Clp protease adaptor protein ClpS; Reviewed
 13-110 2.85e-43

ATP-dependent Clp protease adaptor protein ClpS; Reviewed


Pssm-ID: 178809  Cd Length: 100  Bit Score: 136.62  E-value: 2.85e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551949  13 SPSTGLLTKTQPKTKKPSMYKVLMLNDDFTPMDFVIHVLKRFFRMSSEQATRVMLHVHQKGVGVCGVFTYEIAETKANQV 92
Cdd:PRK00033    9 DMSALVLEKVEPKLKPPPMYKVLLHNDDYTPMEFVVYVLQKFFGYDRERATQIMLEVHNEGKAVVGVCTREVAETKVEQV 88

                          90
                  ....*....|....*...
gi 1733551949  93 vdyaqkHHHPLQCTLEKE 110
Cdd:PRK00033   89 ------HQHGLLCTMEKD 100
clpS PRK13019
ATP-dependent Clp protease adapter ClpS;
13-94 4.40e-28

ATP-dependent Clp protease adapter ClpS;


Pssm-ID: 183845  Cd Length: 94  Bit Score: 97.70  E-value: 4.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551949  13 SPSTGLLTKTQPKTKKPSMYKVLMLNDDFTPMDFVIH-VLKRFFRMSSEQATRVMLHVHQKGVGVCGVFTYEIAETKANQ 91
Cdd:PRK13019    3 DPATKPKTKTKPKLERYPLYKVIVLNDDFNTFEHVVNcLLKAIPGMSEDRAWRLMITAHKEGSAVVWVGPLEQAELYHQQ 82


                  ...
gi 1733551949  92 VVD 94
Cdd:PRK13019   83 LTD 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH