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Conserved domains on  [gi|1308587767|gb|PKL86966|]
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Clp protease ClpS [Ignavibacteriae bacterium HGW-Ignavibacteriae-1]

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

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List of domain hits

 Name Accession Description Interval E-value
ClpS COG2127
ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein ...
 2-90 1.96e-16

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


:

Pssm-ID: 441730  Cd Length: 94  Bit Score: 67.47  E-value: 1.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308587767  2 PAEVEEVVDDVNTDIEQPAKVILFNDEWHTFDEVINQILKAVKCTRDKAELLTLEVHNTGKACVFEGQMSDCLSVSSILE 81
Cdd:COG2127    3 PDTEPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGTREIAETKVEQVH 82


                 ....*....
gi 1308587767 82 EIALHTQIE 90
Cdd:COG2127   83 DYGLQATIE 91
 
Name Accession Description Interval E-value
ClpS COG2127
ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein ...
 2-90 1.96e-16

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


Pssm-ID: 441730  Cd Length: 94  Bit Score: 67.47  E-value: 1.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308587767  2 PAEVEEVVDDVNTDIEQPAKVILFNDEWHTFDEVINQILKAVKCTRDKAELLTLEVHNTGKACVFEGQMSDCLSVSSILE 81
Cdd:COG2127    3 PDTEPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGTREIAETKVEQVH 82


                 ....*....
gi 1308587767 82 EIALHTQIE 90
Cdd:COG2127   83 DYGLQATIE 91
ClpS pfam02617
ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent ...
 21-65 1.86e-13

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: 59.40  E-value: 1.86e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 1308587767 21 KVILFNDEWHTFDEVINQILKAVKCTRDKAELLTLEVHNTGKACV 65
Cdd:pfam02617  7 KVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVV 51
clpS PRK13019
ATP-dependent Clp protease adapter ClpS;
11-65 1.85e-07

ATP-dependent Clp protease adapter ClpS;


Pssm-ID: 183845  Cd Length: 94  Bit Score: 44.54  E-value: 1.85e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 1308587767 11 DVNTDIEQP--AKVILFNDEWHTFDEVINQILKAV-KCTRDKAELLTLEVHNTGKACV 65
Cdd:PRK13019  11 KTKPKLERYplYKVIVLNDDFNTFEHVVNCLLKAIpGMSEDRAWRLMITAHKEGSAVV 68
 
Name Accession Description Interval E-value
ClpS COG2127
ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein ...
 2-90 1.96e-16

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


Pssm-ID: 441730  Cd Length: 94  Bit Score: 67.47  E-value: 1.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308587767  2 PAEVEEVVDDVNTDIEQPAKVILFNDEWHTFDEVINQILKAVKCTRDKAELLTLEVHNTGKACVFEGQMSDCLSVSSILE 81
Cdd:COG2127    3 PDTEPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGTREIAETKVEQVH 82


                 ....*....
gi 1308587767 82 EIALHTQIE 90
Cdd:COG2127   83 DYGLQATIE 91
ClpS pfam02617
ATP-dependent Clp protease adaptor protein ClpS; In the bacterial cytosol, ATP-dependent ...
 21-65 1.86e-13

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: 59.40  E-value: 1.86e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 1308587767 21 KVILFNDEWHTFDEVINQILKAVKCTRDKAELLTLEVHNTGKACV 65
Cdd:pfam02617  7 KVILLNDDYTTMEFVVEVLQRVFGKSEEEATEIMLQVHREGRAVV 51
clpS PRK13019
ATP-dependent Clp protease adapter ClpS;
11-65 1.85e-07

ATP-dependent Clp protease adapter ClpS;


Pssm-ID: 183845  Cd Length: 94  Bit Score: 44.54  E-value: 1.85e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 1308587767 11 DVNTDIEQP--AKVILFNDEWHTFDEVINQILKAV-KCTRDKAELLTLEVHNTGKACV 65
Cdd:PRK13019  11 KTKPKLERYplYKVIVLNDDFNTFEHVVNCLLKAIpGMSEDRAWRLMITAHKEGSAVV 68
clpS PRK00033
ATP-dependent Clp protease adaptor protein ClpS; Reviewed
 6-65 2.35e-05

ATP-dependent Clp protease adaptor protein ClpS; Reviewed


Pssm-ID: 178809  Cd Length: 100  Bit Score: 39.16  E-value: 2.35e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308587767   6 EEVVDDVNTDIEQPA--KVILFNDEWHTFDEVINQILKAVKCTRDKAELLTLEVHNTGKACV 65
Cdd:PRK00033   12 ALVLEKVEPKLKPPPmyKVLLHNDDYTPMEFVVYVLQKFFGYDRERATQIMLEVHNEGKAVV 73
 
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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