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Conserved domains on  [gi|2131431918|dbj|GJK71735|]
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small heat shock protein IbpA [Citrobacter freundii]

Protein Classification

heat shock chaperone IbpA( domain architecture ID 10793461)

heat shock chaperone IbpA (also called 16 kDa heat shock protein A), associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10743 PRK10743
heat shock chaperone IbpA;
1-137 1.14e-97

heat shock chaperone IbpA;


:

Pssm-ID: 182691  Cd Length: 137  Bit Score: 276.69  E-value: 1.14e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131431918   1 MRNFDLSPLYRSAIGFDRLFNLLENNQGQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADDQ 80
Cdd:PRK10743    1 MRNFDLSPLYRSAIGFDRLFNLLENNQSQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADEQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2131431918  81 KERTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEANKPRRIEIN 137
Cdd:PRK10743   81 KERTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEIN 137
 
Name Accession Description Interval E-value
PRK10743 PRK10743
heat shock chaperone IbpA;
1-137 1.14e-97

heat shock chaperone IbpA;


Pssm-ID: 182691  Cd Length: 137  Bit Score: 276.69  E-value: 1.14e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131431918   1 MRNFDLSPLYRSAIGFDRLFNLLENNQGQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADDQ 80
Cdd:PRK10743    1 MRNFDLSPLYRSAIGFDRLFNLLENNQSQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADEQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2131431918  81 KERTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEANKPRRIEIN 137
Cdd:PRK10743   81 KERTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEIN 137
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 35-123 2.50e-45

Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins IbpA and IbpB, and similar proteins. IbpA and IbpB are 16 kDa small heat shock proteins (sHsps). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. IbpA and IbpB are produced during high-level production of various heterologous proteins, specifically human prorenin, renin and bovine insulin-like growth factor 2 (bIGF-2), and are strongly associated with inclusion bodies containing these heterologous proteins. IbpA and IbpB work as an integrated system to stabilize thermally aggregated proteins in a disaggregation competent state. The chaperone activity of IbpB is also significantly elevated as the temperature increases from normal to heat shock. The high temperature results in the disassociation of 2-3-MDa IbpB oligomers into smaller approximately 600-kDa structures. This elevated activity seen under heat shock conditions is retained for an extended period of time after the temperature is returned to normal. IbpA also forms multimers.


Pssm-ID: 107227  Cd Length: 90  Bit Score: 142.67  E-value: 2.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131431918  35 PPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHAD-DQKERTYLYQGIAERNFERKFQLAENIHVRGANLV 113
Cdd:cd06470     1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADeENEEREYLHRGIAKRAFERSFNLADHVKVKGAELE 80

                          90
                  ....*....|
gi 2131431918 114 NGLLYIDLER 123
Cdd:cd06470    81 NGLLTIDLER 90
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 39-137 3.24e-29

Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and prokaryotes but they have also now been shown to occur in cyanobacterial phages as well as their bacterial hosts.


Pssm-ID: 459629  Cd Length: 100  Bit Score: 101.92  E-value: 3.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131431918  39 VELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADDQKERTYLYQGIAERNFERKFQL---AENIHVRgANLVNG 115
Cdd:pfam00011   1 DIKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEEEKEDDHGLRSERSYGSFSRKFTLpenADPDKVK-ASLKDG 79

                          90       100
                  ....*....|....*....|..
gi 2131431918 116 LLYIDLERVIPEaNKPRRIEIN 137
Cdd:pfam00011  80 VLTVTVPKLEPE-PKERRIQIQ 100
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 37-137 7.51e-27

Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 439841  Cd Length: 105  Bit Score: 95.99  E-value: 7.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131431918  37 YNVELvDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADDQ--KERTYLYQGIAERNFERKFQLAENIHVRG--ANL 112
Cdd:COG0071     2 VDIEE-TDDAYVITADLPGVDKEDIDVTVEGNVLTISGERKEEEeeEGENYLRRERRYGSFERSFTLPDDVDVDKieASY 80

                          90       100
                  ....*....|....*....|....*
gi 2131431918 113 VNGLLYIDLERviPEANKPRRIEIN 137
Cdd:COG0071    81 ENGVLTITLPK--AEEAKPRKIEIK 103
 
Name Accession Description Interval E-value
PRK10743 PRK10743
heat shock chaperone IbpA;
1-137 1.14e-97

heat shock chaperone IbpA;


Pssm-ID: 182691  Cd Length: 137  Bit Score: 276.69  E-value: 1.14e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131431918   1 MRNFDLSPLYRSAIGFDRLFNLLENNQGQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADDQ 80
Cdd:PRK10743    1 MRNFDLSPLYRSAIGFDRLFNLLENNQSQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADEQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2131431918  81 KERTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEANKPRRIEIN 137
Cdd:PRK10743   81 KERTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEIN 137
PRK11597 PRK11597
heat shock chaperone IbpB; Provisional
 1-136 2.13e-49

heat shock chaperone IbpB; Provisional


Pssm-ID: 183223  Cd Length: 142  Bit Score: 154.52  E-value: 2.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131431918   1 MRNFDLSPLYRSAIGFDRLFNLLENNQgqSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADDQ 80
Cdd:PRK11597    1 MRNYDLSPLLRQWIGFDKLANALQNAG--ESQSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLTVKGTPEQPE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2131431918  81 KERTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEANKPRRIEI 136
Cdd:PRK11597   79 KEVKWLHQGLVNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEAIAPQRIAI 134
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 35-123 2.50e-45

Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins IbpA and IbpB, and similar proteins. IbpA and IbpB are 16 kDa small heat shock proteins (sHsps). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. IbpA and IbpB are produced during high-level production of various heterologous proteins, specifically human prorenin, renin and bovine insulin-like growth factor 2 (bIGF-2), and are strongly associated with inclusion bodies containing these heterologous proteins. IbpA and IbpB work as an integrated system to stabilize thermally aggregated proteins in a disaggregation competent state. The chaperone activity of IbpB is also significantly elevated as the temperature increases from normal to heat shock. The high temperature results in the disassociation of 2-3-MDa IbpB oligomers into smaller approximately 600-kDa structures. This elevated activity seen under heat shock conditions is retained for an extended period of time after the temperature is returned to normal. IbpA also forms multimers.


Pssm-ID: 107227  Cd Length: 90  Bit Score: 142.67  E-value: 2.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131431918  35 PPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHAD-DQKERTYLYQGIAERNFERKFQLAENIHVRGANLV 113
Cdd:cd06470     1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADeENEEREYLHRGIAKRAFERSFNLADHVKVKGAELE 80

                          90
                  ....*....|
gi 2131431918 114 NGLLYIDLER 123
Cdd:cd06470    81 NGLLTIDLER 90
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 39-137 3.24e-29

Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and prokaryotes but they have also now been shown to occur in cyanobacterial phages as well as their bacterial hosts.


Pssm-ID: 459629  Cd Length: 100  Bit Score: 101.92  E-value: 3.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131431918  39 VELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADDQKERTYLYQGIAERNFERKFQL---AENIHVRgANLVNG 115
Cdd:pfam00011   1 DIKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEEEKEDDHGLRSERSYGSFSRKFTLpenADPDKVK-ASLKDG 79

                          90       100
                  ....*....|....*....|..
gi 2131431918 116 LLYIDLERVIPEaNKPRRIEIN 137
Cdd:pfam00011  80 VLTVTVPKLEPE-PKERRIQIQ 100
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 37-137 7.51e-27

Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 439841  Cd Length: 105  Bit Score: 95.99  E-value: 7.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131431918  37 YNVELvDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADDQ--KERTYLYQGIAERNFERKFQLAENIHVRG--ANL 112
Cdd:COG0071     2 VDIEE-TDDAYVITADLPGVDKEDIDVTVEGNVLTISGERKEEEeeEGENYLRRERRYGSFERSFTLPDDVDVDKieASY 80

                          90       100
                  ....*....|....*....|....*
gi 2131431918 113 VNGLLYIDLERviPEANKPRRIEIN 137
Cdd:COG0071    81 ENGVLTITLPK--AEEAKPRKIEIK 103
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 43-123 1.25e-16

Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps.


Pssm-ID: 107221  Cd Length: 88  Bit Score: 69.51  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131431918  43 DENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADDQKER-TYLYQGIAERNFERKFQLAENIHVRG--ANLVNGLLYI 119
Cdd:cd06464     5 TDDAYVVEADLPGFKKEDIKVEVEDGVLTISGEREEEEEEEeNYLRRERSYGSFSRSFRLPEDVDPDKikASLENGVLTI 84


                  ....
gi 2131431918 120 DLER 123
Cdd:cd06464    85 TLPK 88
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 43-123 4.00e-11

This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small heat shock proteins (sHsps) and a similar domain found in p23-like proteins. sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is this ACD. sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps. p23 is a cochaperone of the Hsp90 chaperoning pathway. It binds Hsp90 and participates in the folding of a number of Hsp90 clients including the progesterone receptor. p23 also has a passive chaperoning activity. p23 in addition may act as the cytosolic prostaglandin E2 synthase. Included in this family is the p23-like C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1) and the p23-like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR).


Pssm-ID: 107219  Cd Length: 80  Bit Score: 55.29  E-value: 4.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131431918  43 DENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADDQKertylyQGIAERNFERKFQLAENIHVRG--ANLVNGLLYID 120
Cdd:cd00298     4 TDDEVVVTVDLPGVKKEDIKVEVEDNVLTISGKREEEEE------RERSYGEFERSFELPEDVDPEKskASLENGVLEIT 77


                  ...
gi 2131431918 121 LER 123
Cdd:cd00298    78 LPK 80
metazoan_ACD cd06526
Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins ...
 43-106 1.01e-07

Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps.


Pssm-ID: 107247  Cd Length: 83  Bit Score: 46.36  E-value: 1.01e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131431918  43 DENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADDQKERTYLYqgiaeRNFERKFQLAENIH 106
Cdd:cd06526     5 DDEKFQVTLDVKGFKPEELKVKVSDNKLVVEGKHEEREDEHGYVS-----REFTRRYQLPEGVD 63
ACD_HspB8_like cd06480
Alpha-crystallin domain (ACD) found in mammalian 21.6 KDa small heat shock protein (sHsp) ...
 47-101 6.04e-04

Alpha-crystallin domain (ACD) found in mammalian 21.6 KDa small heat shock protein (sHsp) HspB8, also denoted as Hsp22 in humans, and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. A chaperone complex formed of HspB8 and Bag3 stimulates degradation of protein complexes by macroautophagy. HspB8 also forms complexes with Hsp27 (HspB1), MKBP (HspB2), HspB3, alphaB-crystallin (HspB5), Hsp20 (HspB6), and cvHsp (HspB7). These latter interactions may depend on phosphorylation of the respective partner sHsp. HspB8 may participate in the regulation of cell proliferation, cardiac hypertrophy, apoptosis, and carcinogenesis. Point mutations in HspB8 have been correlated with the development of several congenital neurological diseases, including Charcot Marie tooth disease and distal motor neuropathy type II.


Pssm-ID: 107235  Cd Length: 91  Bit Score: 36.85  E-value: 6.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2131431918  47 YRIAIAVAGFAESELEITAQDNLLVVKGAHADDQKErtylyQGIAERNFERKFQL 101
Cdd:cd06480    17 WKVCVNVHSFKPEELTVKTKDGFVEVSGKHEEQQKE-----GGIVSKNFTKKIQL 66
 
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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