Conserved Protein Domain Family
ACD_IbpA-B_like

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cd06470: ACD_IbpA-B_like 
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.
Statistics
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PSSM-Id: 107227
View PSSM: cd06470
Aligned: 35 rows
Threshold Bit Score: 106.848
Threshold Setting Gi: 50470482
Created: 18-Mar-2008
Updated: 17-Jan-2013
Structure
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Aligned Rows:
 
putative dimer
Feature 1:putative dimer interface [polypeptide binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1          #####        # # ##                                                #          
gi 68568733   33 PPYNIEKsddnHYRITLALAGFRQEDLEIQLEgTRLSVKGTpeqpk-------eekkwLHQGLMNQPFSLSFTLAENMEV 105
gi 70724779   41 PAYNLLKns-eQHELTVSVPGYAQDELDVSVLnNQLTVRGKpnvektdeaeekegikwLHQGIRKSEFVLSFTLEHRIVI 119
gi 149908184  75 PRYNITHvgelDYQITLALAGFSLEEIDITVTaDELVITGKrqpvd-------vtstwLHQGINQADFSRKFALADHVQV 147
gi 71082886   42 PPYNIRKtgkdNYAIEVALAGFNKNDVEVEFEdNLLTVRTKqvdksed---ksddgeiIHKGISQRQFARSFTIAEDVKV 118
gi 50470482   18 PNYNLIQldkyNYELSVSVPGYKKEELEVSIInNRLNINSKskkekek---etkkinwIHQGILKNNFSISFKLEHKIKI 94
gi 84704530   36 PPYNIVRtsetDYEITLAVAGFSQDDLEIEVVdRELRVSGRrdsdqd------edreyLHQGIAGRNFDRRFRLAEHLTV 109
gi 8134501    42 PAYNLFQidehKYELILSIPGYEEKELDISVHnSQLTVQGKkqnqend---dkkikkyLHKGIIFNDFSLNFNFDHKIQV 118
gi 8134500    42 PPYDILQlkenFYKLIVSVPGYLEKNLEISTQyDQLIIIGKkeitentnekketvekiLHQEIYTGDFSLSFRLNERISV 121
gi 31982990   41 PSYDLIQknenNYQLIINTAGYKEEDLDILVHnNKLTVTGKykenin-----nkdnynGCIKGLKKYFSLSFNLDNRIKV 115
gi 183599532  43 QTYDLKQiddsHYELTVSVPGYQESDLTVSLKgGRLLVEGKreeksq-----ednekwLHRGISYGQFTLQFDLGKNVRI 117
                         90
                 ....*....|....*.
Feature 1               ##       
gi 68568733  106 SGATFVNGLLHIDLIR 121
gi 70724779  120 QQANLANGLLTLHFTY 135
gi 149908184 148 LGAEMAQGLLTINLQR 163
gi 71082886  119 NGAELKDGLLTIACER 134
gi 50470482   95 KYANLKHGILNLSFFY 110
gi 84704530  110 RGAQLENGLLTVLLAL 125
gi 8134501   119 KKAELFSGLLKINFEC 134
gi 8134500   122 MSATLDQGLLTIYFEY 137
gi 31982990  116 KQAKIILGLLTLDFEY 131
gi 183599532 118 EKADLSRGLLTVAIEY 133

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