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MULTISPECIES: co-chaperone GroES [Staphylococcus]

Protein Classification

co-chaperone GroES( domain architecture ID 10791922)

co-chaperone GroES (Cpn10) binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter

CATH:  1.10.560.10
Gene Ontology:  GO:0005524|GO:0140662
PubMed:  10049801|15944406|11340060
SCOP:  4000251

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
groES PRK00364
co-chaperonin GroES; Reviewed
 1-94 1.63e-44

co-chaperonin GroES; Reviewed


:

Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 138.71  E-value: 1.63e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392025  1 MLKPIGNRVVIEKKEQEQTTKSGIVLTDSAKEKSNEGVVIAVGLGRQLENGQRITPDVNEGDRVVFQEYAGTEIKQGNDT 80
Cdd:PRK00364  2 NLKPLGDRVLVKRLEEEEKTAGGIVLPDSAKEKPQEGEVVAVGPGRRLDNGERVPLDVKVGDKVLFGKYAGTEVKIDGEE 81

                        90
                ....*....|....
gi 488392025 81 YLILNADDILAIIE 94
Cdd:PRK00364 82 YLILRESDILAIVE 95
 
Name Accession Description Interval E-value
groES PRK00364
co-chaperonin GroES; Reviewed
 1-94 1.63e-44

co-chaperonin GroES; Reviewed


Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 138.71  E-value: 1.63e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392025  1 MLKPIGNRVVIEKKEQEQTTKSGIVLTDSAKEKSNEGVVIAVGLGRQLENGQRITPDVNEGDRVVFQEYAGTEIKQGNDT 80
Cdd:PRK00364  2 NLKPLGDRVLVKRLEEEEKTAGGIVLPDSAKEKPQEGEVVAVGPGRRLDNGERVPLDVKVGDKVLFGKYAGTEVKIDGEE 81

                        90
                ....*....|....
gi 488392025 81 YLILNADDILAIIE 94
Cdd:PRK00364 82 YLILRESDILAIVE 95
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
1-94 1.02e-43

Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440004  Cd Length: 95  Bit Score: 136.72  E-value: 1.02e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392025  1 MLKPIGNRVVIEKKEQEQTTKSGIVLTDSAKEKSNEGVVIAVGLGRQLENGQRITPDVNEGDRVVFQEYAGTEIKQGNDT 80
Cdd:COG0234   1 KIKPLGDRVLVKRIEAEEKTAGGIVLPDTAKEKPQEGEVVAVGPGKLLDNGKRVPLDVKVGDKVLFGKYAGTEVKIDGEE 80

                        90
                ....*....|....
gi 488392025 81 YLILNADDILAIIE 94
Cdd:COG0234  81 YLILRESDILAVVE 94
Cpn10 smart00883
Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding ...
 1-93 1.27e-41

Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding and subsequent assembly of some proteins. These are required for normal cell growth, and are stress-induced, acting to stabilise or protect disassembled polypeptides under heat-shock conditions. Type I chaperonins present in eubacteria, mitochondria and chloroplasts require the concerted action of 2 proteins, chaperonin 60 (cpn60) and chaperonin 10 (cpn10). The 10 kDa chaperonin (cpn10 - or groES in bacteria) exists as a ring-shaped oligomer of between six to eight identical subunits, while the 60 kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings, each ring containing 7 identical subunits. These ring structures assemble by self-stimulation in the presence of Mg2+-ATP. The central cavity of the cylindrical cpn60 tetradecamer provides as isolated environment for protein folding whilst cpn-10 binds to cpn-60 and synchronizes the release of the folded protein in an Mg2+-ATP dependent manner. The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60.


Pssm-ID: 197951  Cd Length: 93  Bit Score: 131.40  E-value: 1.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392025    1 MLKPIGNRVVIEKKEQEQTTKSGIVLTDSAKEKSNEGVVIAVGLGRQLENGQRITPDVNEGDRVVFQEYAGTEIKQGNDT 80
Cdd:smart00883  1 KIKPLGDRVLVKRIEEEEKTAGGIVIPDTAKEKPQEGEVVAVGPGKRLENGERVPLDVKVGDKVLFGKYAGTEVKLDGEE 80

                          90
                  ....*....|...
gi 488392025   81 YLILNADDILAII 93
Cdd:smart00883 81 YLILRESDILAVI 93
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 1-93 2.18e-36

Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL), an ATPase, to assist the folding and assembly of proteins and is found in eubacterial cytosol, as well as in the matrix of mitochondria and chloroplasts. It forms heptameric rings with a dome-like structure, forming a lid to the large cavity of the tetradecameric cpn60 cylinder and thereby tightly regulating release and binding of proteins to the cpn60 surface.


Pssm-ID: 238197  Cd Length: 93  Bit Score: 117.99  E-value: 2.18e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392025  1 MLKPIGNRVVIEKKEQEQTTKSGIVLTDSAKEKSNEGVVIAVGLGRQLENGQRITPDVNEGDRVVFQEYAGTEIKQGNDT 80
Cdd:cd00320   1 KIKPLGDRVLVKRIEAEEKTKGGIILPDSAKEKPQEGKVVAVGPGRRNENGERVPLSVKVGDKVLFPKYAGTEVKLDGEE 80

                        90
                ....*....|...
gi 488392025 81 YLILNADDILAII 93
Cdd:cd00320  81 YLILRESDILAVI 93
Cpn10 pfam00166
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ...
 1-93 9.96e-34

Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a functional co-chaperonin that is required for the folding and assembly of Gp23, a major capsid protein, during phage morphogenesis.


Pssm-ID: 395114  Cd Length: 92  Bit Score: 111.55  E-value: 9.96e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392025   1 MLKPIGNRVVIEKKEQEQTTKSGIVLTDSAKEKSNEGVVIAVGLGRQLeNGQRITPDVNEGDRVVFQEYAGTEIKQGNDT 80
Cdd:pfam00166  1 KIKPLGDRVLVKRVEEEEKTAGGIILPDSAKEKPQQGEVVAVGPGARN-NGNDVPLEVKVGDKVLFPKYAGTEVKVDGKE 79

                         90
                 ....*....|...
gi 488392025  81 YLILNADDILAII 93
Cdd:pfam00166 80 YLILKESDILAVI 92
 
Name Accession Description Interval E-value
groES PRK00364
co-chaperonin GroES; Reviewed
 1-94 1.63e-44

co-chaperonin GroES; Reviewed


Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 138.71  E-value: 1.63e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392025  1 MLKPIGNRVVIEKKEQEQTTKSGIVLTDSAKEKSNEGVVIAVGLGRQLENGQRITPDVNEGDRVVFQEYAGTEIKQGNDT 80
Cdd:PRK00364  2 NLKPLGDRVLVKRLEEEEKTAGGIVLPDSAKEKPQEGEVVAVGPGRRLDNGERVPLDVKVGDKVLFGKYAGTEVKIDGEE 81

                        90
                ....*....|....
gi 488392025 81 YLILNADDILAIIE 94
Cdd:PRK00364 82 YLILRESDILAIVE 95
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
1-94 1.02e-43

Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440004  Cd Length: 95  Bit Score: 136.72  E-value: 1.02e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392025  1 MLKPIGNRVVIEKKEQEQTTKSGIVLTDSAKEKSNEGVVIAVGLGRQLENGQRITPDVNEGDRVVFQEYAGTEIKQGNDT 80
Cdd:COG0234   1 KIKPLGDRVLVKRIEAEEKTAGGIVLPDTAKEKPQEGEVVAVGPGKLLDNGKRVPLDVKVGDKVLFGKYAGTEVKIDGEE 80

                        90
                ....*....|....
gi 488392025 81 YLILNADDILAIIE 94
Cdd:COG0234  81 YLILRESDILAVVE 94
Cpn10 smart00883
Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding ...
 1-93 1.27e-41

Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding and subsequent assembly of some proteins. These are required for normal cell growth, and are stress-induced, acting to stabilise or protect disassembled polypeptides under heat-shock conditions. Type I chaperonins present in eubacteria, mitochondria and chloroplasts require the concerted action of 2 proteins, chaperonin 60 (cpn60) and chaperonin 10 (cpn10). The 10 kDa chaperonin (cpn10 - or groES in bacteria) exists as a ring-shaped oligomer of between six to eight identical subunits, while the 60 kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings, each ring containing 7 identical subunits. These ring structures assemble by self-stimulation in the presence of Mg2+-ATP. The central cavity of the cylindrical cpn60 tetradecamer provides as isolated environment for protein folding whilst cpn-10 binds to cpn-60 and synchronizes the release of the folded protein in an Mg2+-ATP dependent manner. The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60.


Pssm-ID: 197951  Cd Length: 93  Bit Score: 131.40  E-value: 1.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392025    1 MLKPIGNRVVIEKKEQEQTTKSGIVLTDSAKEKSNEGVVIAVGLGRQLENGQRITPDVNEGDRVVFQEYAGTEIKQGNDT 80
Cdd:smart00883  1 KIKPLGDRVLVKRIEEEEKTAGGIVIPDTAKEKPQEGEVVAVGPGKRLENGERVPLDVKVGDKVLFGKYAGTEVKLDGEE 80

                          90
                  ....*....|...
gi 488392025   81 YLILNADDILAII 93
Cdd:smart00883 81 YLILRESDILAVI 93
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 1-93 2.18e-36

Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL), an ATPase, to assist the folding and assembly of proteins and is found in eubacterial cytosol, as well as in the matrix of mitochondria and chloroplasts. It forms heptameric rings with a dome-like structure, forming a lid to the large cavity of the tetradecameric cpn60 cylinder and thereby tightly regulating release and binding of proteins to the cpn60 surface.


Pssm-ID: 238197  Cd Length: 93  Bit Score: 117.99  E-value: 2.18e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392025  1 MLKPIGNRVVIEKKEQEQTTKSGIVLTDSAKEKSNEGVVIAVGLGRQLENGQRITPDVNEGDRVVFQEYAGTEIKQGNDT 80
Cdd:cd00320   1 KIKPLGDRVLVKRIEAEEKTKGGIILPDSAKEKPQEGKVVAVGPGRRNENGERVPLSVKVGDKVLFPKYAGTEVKLDGEE 80

                        90
                ....*....|...
gi 488392025 81 YLILNADDILAII 93
Cdd:cd00320  81 YLILRESDILAVI 93
Cpn10 pfam00166
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ...
 1-93 9.96e-34

Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a functional co-chaperonin that is required for the folding and assembly of Gp23, a major capsid protein, during phage morphogenesis.


Pssm-ID: 395114  Cd Length: 92  Bit Score: 111.55  E-value: 9.96e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392025   1 MLKPIGNRVVIEKKEQEQTTKSGIVLTDSAKEKSNEGVVIAVGLGRQLeNGQRITPDVNEGDRVVFQEYAGTEIKQGNDT 80
Cdd:pfam00166  1 KIKPLGDRVLVKRVEEEEKTAGGIILPDSAKEKPQQGEVVAVGPGARN-NGNDVPLEVKVGDKVLFPKYAGTEVKVDGKE 79

                         90
                 ....*....|...
gi 488392025  81 YLILNADDILAII 93
Cdd:pfam00166 80 YLILKESDILAVI 92
groES PRK14533
co-chaperonin GroES; Provisional
 2-94 2.05e-18

co-chaperonin GroES; Provisional


Pssm-ID: 184730  Cd Length: 91  Bit Score: 72.59  E-value: 2.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392025  2 LKPIGNRVVIEKKEQEQTTKSGIVLTDSAKEKSNEGVVIAVGLGRQLENgqritPDVNEGDRVVFQEYAGTEIKQGNDTY 81
Cdd:PRK14533  3 VIPLGERLLIKPIKEEKKTEGGIVLPDSAKEKPMKAEVVAVGKLDDEED-----FDIKVGDKVIFSKYAGTEIKIDDEDY 77

                        90
                ....*....|...
gi 488392025 82 LILNADDILAIIE 94
Cdd:PRK14533 78 IIIDVNDILAKIE 90
PTZ00414 PTZ00414
10 kDa heat shock protein; Provisional
 2-94 2.46e-13

10 kDa heat shock protein; Provisional


Pssm-ID: 173604  Cd Length: 100  Bit Score: 60.01  E-value: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392025   2 LKPIGNRVVIEKKEQEQTTKSGIVLTDSAKEKSNEGVVIAVGLGrqlenGQRITPDVNEGDRVVFQEYAGTEIKQGNDTY 81
Cdd:PTZ00414  12 LQPLGQRVLVKRTLAAKQTKAGVLIPEQVAGKVNEGTVVAVAAA-----TKDWTPTVKVGDTVLLPEFGGSSVKVEGEEF 86

                         90
                 ....*....|...
gi 488392025  82 LILNADDILAIIE 94
Cdd:PTZ00414  87 FLYNEDSLLGVLQ 99
 
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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