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Conserved domains on  [gi|488944963|ref|WP_002856038|]
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MULTISPECIES: ATP-dependent Clp protease adaptor ClpS [Campylobacter]

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 ...
 14-91 5.94e-38

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: 121.80  E-value: 5.94e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488944963  14 EPKMYKVILLNDDVTTMDFVIEILMNIFHQNLEKASQTMLEIHHNGSGICGIYTQEIALSKQKKVIDAAKLANFPLQA 91
Cdd:pfam02617  2 EPPMYKVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVVGVYTYDIAETKVAQVHQLARENGFPLRC 79
 
Name Accession Description Interval E-value
ClpS pfam02617
ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent ...
 14-91 5.94e-38

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: 121.80  E-value: 5.94e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488944963  14 EPKMYKVILLNDDVTTMDFVIEILMNIFHQNLEKASQTMLEIHHNGSGICGIYTQEIALSKQKKVIDAAKLANFPLQA 91
Cdd:pfam02617  2 EPPMYKVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVVGVYTYDIAETKVAQVHQLARENGFPLRC 79
ClpS COG2127
ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein ...
 3-96 2.03e-35

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


Pssm-ID: 441730  Cd Length: 94  Bit Score: 115.62  E-value: 2.03e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488944963  3 KTQTLEQTKLSEPKMYKVILLNDDVTTMDFVIEILMNIFHQNLEKASQTMLEIHHNGSGICGIYTQEIALSKQKKVIDAA 82
Cdd:COG2127   6 EPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGTREIAETKVEQVHDYG 85

                        90
                ....*....|....
gi 488944963 83 klanfpLQAKVEEE 96
Cdd:COG2127  86 ------LQATIEPA 93
clpS PRK00033
ATP-dependent Clp protease adaptor protein ClpS; Reviewed
 1-96 4.90e-26

ATP-dependent Clp protease adaptor protein ClpS; Reviewed


Pssm-ID: 178809  Cd Length: 100  Bit Score: 92.32  E-value: 4.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488944963   1 MPKTQTLEQ--TKLSEPKMYKVILLNDDVTTMDFVIEILMNIFHQNLEKASQTMLEIHHNGSGICGIYTQEIALSKqkkv 78
Cdd:PRK00033   9 DMSALVLEKvePKLKPPPMYKVLLHNDDYTPMEFVVYVLQKFFGYDRERATQIMLEVHNEGKAVVGVCTREVAETK---- 84

                         90
                 ....*....|....*...
gi 488944963  79 idAAKLANFPLQAKVEEE 96
Cdd:PRK00033  85 --VEQVHQHGLLCTMEKD 100
 
Name Accession Description Interval E-value
ClpS pfam02617
ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent ...
 14-91 5.94e-38

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: 121.80  E-value: 5.94e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488944963  14 EPKMYKVILLNDDVTTMDFVIEILMNIFHQNLEKASQTMLEIHHNGSGICGIYTQEIALSKQKKVIDAAKLANFPLQA 91
Cdd:pfam02617  2 EPPMYKVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVVGVYTYDIAETKVAQVHQLARENGFPLRC 79
ClpS COG2127
ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein ...
 3-96 2.03e-35

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


Pssm-ID: 441730  Cd Length: 94  Bit Score: 115.62  E-value: 2.03e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488944963  3 KTQTLEQTKLSEPKMYKVILLNDDVTTMDFVIEILMNIFHQNLEKASQTMLEIHHNGSGICGIYTQEIALSKQKKVIDAA 82
Cdd:COG2127   6 EPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGTREIAETKVEQVHDYG 85

                        90
                ....*....|....
gi 488944963 83 klanfpLQAKVEEE 96
Cdd:COG2127  86 ------LQATIEPA 93
clpS PRK00033
ATP-dependent Clp protease adaptor protein ClpS; Reviewed
 1-96 4.90e-26

ATP-dependent Clp protease adaptor protein ClpS; Reviewed


Pssm-ID: 178809  Cd Length: 100  Bit Score: 92.32  E-value: 4.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488944963   1 MPKTQTLEQ--TKLSEPKMYKVILLNDDVTTMDFVIEILMNIFHQNLEKASQTMLEIHHNGSGICGIYTQEIALSKqkkv 78
Cdd:PRK00033   9 DMSALVLEKvePKLKPPPMYKVLLHNDDYTPMEFVVYVLQKFFGYDRERATQIMLEVHNEGKAVVGVCTREVAETK---- 84

                         90
                 ....*....|....*...
gi 488944963  79 idAAKLANFPLQAKVEEE 96
Cdd:PRK00033  85 --VEQVHQHGLLCTMEKD 100
clpS PRK13019
ATP-dependent Clp protease adapter ClpS;
2-82 3.95e-18

ATP-dependent Clp protease adapter ClpS;


Pssm-ID: 183845  Cd Length: 94  Bit Score: 71.89  E-value: 3.95e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488944963  2 PKTQTLEQTKLSEPKMYKVILLNDDVTTMDFVIE-ILMNIFHQNLEKASQTMLEIHHNGSGICGIYTQEIALSKQKKVID 80
Cdd:PRK13019  6 TKPKTKTKPKLERYPLYKVIVLNDDFNTFEHVVNcLLKAIPGMSEDRAWRLMITAHKEGSAVVWVGPLEQAELYHQQLTD 85


                ..
gi 488944963 81 AA 82
Cdd:PRK13019 86 AG 87
 
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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