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Conserved domains on  [gi|502609872|ref|WP_012846892|]
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small heat shock chaperone IbpB [Edwardsiella piscicida]

Protein Classification

heat shock chaperone IbpB( domain architecture ID 10793594)

heat shock chaperone IbpB associates with aggregated proteins, together with IbpA, 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
PRK11597 PRK11597
heat shock chaperone IbpB; Provisional
 1-146 4.16e-99

heat shock chaperone IbpB; Provisional


:

Pssm-ID: 183223  Cd Length: 142  Bit Score: 281.25  E-value: 4.16e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502609872   1 MRNYDLSPLMRQWIGFDKLANAMQTSLEPQGFPPYNIEKSDDNHYRISLALAGFRQSELDIEVEGPRLTVRGNPVKPEKP 80
Cdd:PRK11597   1 MRNYDLSPLLRQWIGFDKLANALQNAGESQSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLTVKGTPEQPEKE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502609872  81 VEYLHQGLVCKAFELSFTLAEHLTVEGAAFENGLLNIDLVRHVPEALQPQRIIIGaaqrDPAALEC 146
Cdd:PRK11597  81 VKWLHQGLVNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEAIAPQRIAIS----ERPALNS 142
 
Name Accession Description Interval E-value
PRK11597 PRK11597
heat shock chaperone IbpB; Provisional
 1-146 4.16e-99

heat shock chaperone IbpB; Provisional


Pssm-ID: 183223  Cd Length: 142  Bit Score: 281.25  E-value: 4.16e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502609872   1 MRNYDLSPLMRQWIGFDKLANAMQTSLEPQGFPPYNIEKSDDNHYRISLALAGFRQSELDIEVEGPRLTVRGNPVKPEKP 80
Cdd:PRK11597   1 MRNYDLSPLLRQWIGFDKLANALQNAGESQSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLTVKGTPEQPEKE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502609872  81 VEYLHQGLVCKAFELSFTLAEHLTVEGAAFENGLLNIDLVRHVPEALQPQRIIIGaaqrDPAALEC 146
Cdd:PRK11597  81 VKWLHQGLVNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEAIAPQRIAIS----ERPALNS 142
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 33-121 5.85e-44

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: 139.59  E-value: 5.85e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502609872  33 PPYNIEKSDDNHYRISLALAGFRQSELDIEVEGPRLTVRGNPVKPE-KPVEYLHQGLVCKAFELSFTLAEHLTVEGAAFE 111
Cdd:cd06470    1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEEnEEREYLHRGIAKRAFERSFNLADHVKVKGAELE 80

                         90
                 ....*....|
gi 502609872 112 NGLLNIDLVR 121
Cdd:cd06470   81 NGLLTIDLER 90
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 35-137 3.86e-26

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 94.83  E-value: 3.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502609872  35 YNIEKSDDnHYRISLALAGFRQSELDIEVEGPRLTVRG--NPVKPEKPVEYLHQGLVCKAFELSFTLAEHLTVEG--AAF 110
Cdd:COG0071    2 VDIEETDD-AYVITADLPGVDKEDIDVTVEGNVLTISGerKEEEEEEGENYLRRERRYGSFERSFTLPDDVDVDKieASY 80

                         90       100
                 ....*....|....*....|....*..
gi 502609872 111 ENGLLNIDLVRhvPEALQPQRIIIGAA 137
Cdd:COG0071   81 ENGVLTITLPK--AEEAKPRKIEIKAG 105
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 38-134 1.61e-17

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: 72.64  E-value: 1.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502609872   38 EKSDDNHYRISLALAGFRQSELDIEVEGPRLTVRGNPVKPEKPVEYLHQGLVCKAFELSFTLAEHLTVEG--AAFENGLL 115
Cdd:pfam00011   2 IKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEEEKEDDHGLRSERSYGSFSRKFTLPENADPDKvkASLKDGVL 81

                          90
                  ....*....|....*....
gi 502609872  116 NIDLVRHVPEAlQPQRIII 134
Cdd:pfam00011  82 TVTVPKLEPEP-KERRIQI 99
 
Name Accession Description Interval E-value
PRK11597 PRK11597
heat shock chaperone IbpB; Provisional
 1-146 4.16e-99

heat shock chaperone IbpB; Provisional


Pssm-ID: 183223  Cd Length: 142  Bit Score: 281.25  E-value: 4.16e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502609872   1 MRNYDLSPLMRQWIGFDKLANAMQTSLEPQGFPPYNIEKSDDNHYRISLALAGFRQSELDIEVEGPRLTVRGNPVKPEKP 80
Cdd:PRK11597   1 MRNYDLSPLLRQWIGFDKLANALQNAGESQSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLTVKGTPEQPEKE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502609872  81 VEYLHQGLVCKAFELSFTLAEHLTVEGAAFENGLLNIDLVRHVPEALQPQRIIIGaaqrDPAALEC 146
Cdd:PRK11597  81 VKWLHQGLVNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEAIAPQRIAIS----ERPALNS 142
PRK10743 PRK10743
heat shock chaperone IbpA;
1-134 6.27e-48

heat shock chaperone IbpA;


Pssm-ID: 182691  Cd Length: 137  Bit Score: 151.50  E-value: 6.27e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502609872   1 MRNYDLSPLMRQWIGFDKLANAMQT--SLEPQGFPPYNIEKSDDNHYRISLALAGFRQSELDIEVEGPRLTVRGNPVKPE 78
Cdd:PRK10743   1 MRNFDLSPLYRSAIGFDRLFNLLENnqSQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADEQ 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502609872  79 KPVEYLHQGLVCKAFELSFTLAEHLTVEGAAFENGLLNIDLVRHVPEALQPQRIII 134
Cdd:PRK10743  81 KERTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEI 136
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 33-121 5.85e-44

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: 139.59  E-value: 5.85e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502609872  33 PPYNIEKSDDNHYRISLALAGFRQSELDIEVEGPRLTVRGNPVKPE-KPVEYLHQGLVCKAFELSFTLAEHLTVEGAAFE 111
Cdd:cd06470    1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEEnEEREYLHRGIAKRAFERSFNLADHVKVKGAELE 80

                         90
                 ....*....|
gi 502609872 112 NGLLNIDLVR 121
Cdd:cd06470   81 NGLLTIDLER 90
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 35-137 3.86e-26

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 94.83  E-value: 3.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502609872  35 YNIEKSDDnHYRISLALAGFRQSELDIEVEGPRLTVRG--NPVKPEKPVEYLHQGLVCKAFELSFTLAEHLTVEG--AAF 110
Cdd:COG0071    2 VDIEETDD-AYVITADLPGVDKEDIDVTVEGNVLTISGerKEEEEEEGENYLRRERRYGSFERSFTLPDDVDVDKieASY 80

                         90       100
                 ....*....|....*....|....*..
gi 502609872 111 ENGLLNIDLVRhvPEALQPQRIIIGAA 137
Cdd:COG0071   81 ENGVLTITLPK--AEEAKPRKIEIKAG 105
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 38-134 1.61e-17

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: 72.64  E-value: 1.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502609872   38 EKSDDNHYRISLALAGFRQSELDIEVEGPRLTVRGNPVKPEKPVEYLHQGLVCKAFELSFTLAEHLTVEG--AAFENGLL 115
Cdd:pfam00011   2 IKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEEEKEDDHGLRSERSYGSFSRKFTLPENADPDKvkASLKDGVL 81

                          90
                  ....*....|....*....
gi 502609872  116 NIDLVRHVPEAlQPQRIII 134
Cdd:pfam00011  82 TVTVPKLEPEP-KERRIQI 99
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 41-119 3.68e-15

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: 66.42  E-value: 3.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502609872  41 DDNHYRISLALAGFRQSELDIEVEGPRLTVRGN-PVKPEKPVEYLHQGLVCKAFELSFTLAEHLTVEG--AAFENGLLNI 117
Cdd:cd06464    5 TDDAYVVEADLPGFKKEDIKVEVEDGVLTISGErEEEEEEEENYLRRERSYGSFSRSFRLPEDVDPDKikASLENGVLTI 84


                 ..
gi 502609872 118 DL 119
Cdd:cd06464   85 TL 86
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 41-121 1.75e-09

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: 51.44  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502609872  41 DDNHYRISLALAGFRQSELDIEVEGPRLTVRGNpVKPEKPVEYlhqglVCKAFELSFTLAEHLTVEG--AAFENGLLNID 118
Cdd:cd00298    4 TDDEVVVTVDLPGVKKEDIKVEVEDNVLTISGK-REEEEERER-----SYGEFERSFELPEDVDPEKskASLENGVLEIT 77


                 ...
gi 502609872 119 LVR 121
Cdd:cd00298   78 LPK 80
ArsA_HSP20 pfam17886
HSP20-like domain found in ArsA; This domain is found at the C-terminus of ArsA like proteins. ...
 42-117 9.02e-03

HSP20-like domain found in ArsA; This domain is found at the C-terminus of ArsA like proteins. This domain is related to HSP20.


Pssm-ID: 436117  Cd Length: 63  Bit Score: 33.23  E-value: 9.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502609872   42 DNHYRISLALAGFRQSELDIEVEGPRLTVRGNPVKpekpveylhqglvcKAFELSFTLAEHlTVEGAAFENGLLNI 117
Cdd:pfam17886   1 DGGYVLRLRLPFVDKEDVDLSRSGDELIIKIGNFR--------------RNITLPRSLARL-EVTGAKFEDGVLRI 61
 
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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