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Conserved domains on  [gi|15598322|ref|NP_251816|]
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heat-shock protein IbpA [Pseudomonas aeruginosa PAO1]

Protein Classification

Hsp20 family protein( domain architecture ID 10158133)

small heat shock (Hsp20) family protein is a molecular chaperone that suppresses protein aggregation and protects against cell stress

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 37-126 1.25e-50

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: 156.54  E-value: 1.25e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598322  37 PPYNVEKHGDDEYRIVIAAAGFQEEDLDLQVERGVLTVSGGKREKSTDNVTYLHQGIAQRAFKLSFRLADHIEVKAASLA 116
Cdd:cd06470   1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEENEEREYLHRGIAKRAFERSFNLADHVKVKGAELE 80

                        90
                ....*....|
gi 15598322 117 NGLLNIDLVR 126
Cdd:cd06470  81 NGLLTIDLER 90
 
Name Accession Description Interval E-value
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 37-126 1.25e-50

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: 156.54  E-value: 1.25e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598322  37 PPYNVEKHGDDEYRIVIAAAGFQEEDLDLQVERGVLTVSGGKREKSTDNVTYLHQGIAQRAFKLSFRLADHIEVKAASLA 116
Cdd:cd06470   1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEENEEREYLHRGIAKRAFERSFNLADHVKVKGAELE 80

                        90
                ....*....|
gi 15598322 117 NGLLNIDLVR 126
Cdd:cd06470  81 NGLLTIDLER 90
PRK11597 PRK11597
heat shock chaperone IbpB; Provisional
 1-147 5.33e-48

heat shock chaperone IbpB; Provisional


Pssm-ID: 183223  Cd Length: 142  Bit Score: 151.44  E-value: 5.33e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598322    1 MSNaFSLAPLFRHSVGFDRFndlfESALRNEAGS-TYPPYNVEKHGDDEYRIVIAAAGFQEEDLDLQVERGVLTVSGgKR 79
Cdd:PRK11597   1 MRN-YDLSPLLRQWIGFDKL----ANALQNAGESqSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLTVKG-TP 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598322   80 EKSTDNVTYLHQGIAQRAFKLSFRLADHIEVKAASLANGLLNIDLVRLVPEEAKPKRIAInGQRPALD 147
Cdd:PRK11597  75 EQPEKEVKWLHQGLVNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEAIAPQRIAI-SERPALN 141
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 39-142 1.03e-32

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 111.40  E-value: 1.03e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598322  39 YNVEKHgDDEYRIVIAAAGFQEEDLDLQVERGVLTVSGGKR-EKSTDNVTYLHQGIAQRAFKLSFRLADHIEVKA--ASL 115
Cdd:COG0071   2 VDIEET-DDAYVITADLPGVDKEDIDVTVEGNVLTISGERKeEEEEEGENYLRRERRYGSFERSFTLPDDVDVDKieASY 80

                        90       100
                ....*....|....*....|....*..
gi 15598322 116 ANGLLNIDLVRlvPEEAKPKRIAINGQ 142
Cdd:COG0071  81 ENGVLTITLPK--AEEAKPRKIEIKAG 105
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 41-140 7.54e-20

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: 78.42  E-value: 7.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598322    41 VEKHGDDEYRIVIAAAGFQEEDLDLQVERGVLTVSgGKREKSTDNVTYLHQGIAQRAFKLSFRL---ADHIEVKaASLAN 117
Cdd:pfam00011   1 DIKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVK-GEHEEEKEDDHGLRSERSYGSFSRKFTLpenADPDKVK-ASLKD 78

                          90       100
                  ....*....|....*....|...
gi 15598322   118 GLLNIDLVRLVPeEAKPKRIAIN 140
Cdd:pfam00011  79 GVLTVTVPKLEP-EPKERRIQIQ 100
 
Name Accession Description Interval E-value
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 37-126 1.25e-50

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: 156.54  E-value: 1.25e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598322  37 PPYNVEKHGDDEYRIVIAAAGFQEEDLDLQVERGVLTVSGGKREKSTDNVTYLHQGIAQRAFKLSFRLADHIEVKAASLA 116
Cdd:cd06470   1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEENEEREYLHRGIAKRAFERSFNLADHVKVKGAELE 80

                        90
                ....*....|
gi 15598322 117 NGLLNIDLVR 126
Cdd:cd06470  81 NGLLTIDLER 90
PRK11597 PRK11597
heat shock chaperone IbpB; Provisional
 1-147 5.33e-48

heat shock chaperone IbpB; Provisional


Pssm-ID: 183223  Cd Length: 142  Bit Score: 151.44  E-value: 5.33e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598322    1 MSNaFSLAPLFRHSVGFDRFndlfESALRNEAGS-TYPPYNVEKHGDDEYRIVIAAAGFQEEDLDLQVERGVLTVSGgKR 79
Cdd:PRK11597   1 MRN-YDLSPLLRQWIGFDKL----ANALQNAGESqSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLTVKG-TP 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598322   80 EKSTDNVTYLHQGIAQRAFKLSFRLADHIEVKAASLANGLLNIDLVRLVPEEAKPKRIAInGQRPALD 147
Cdd:PRK11597  75 EQPEKEVKWLHQGLVNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEAIAPQRIAI-SERPALN 141
PRK10743 PRK10743
heat shock chaperone IbpA;
1-140 1.69e-45

heat shock chaperone IbpA;


Pssm-ID: 182691  Cd Length: 137  Bit Score: 144.95  E-value: 1.69e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598322    1 MSNaFSLAPLFRHSVGFDRFNDLFESAlRNEAGSTYPPYNVEKHGDDEYRIVIAAAGFQEEDLDLQVERGVLTVSGGKRE 80
Cdd:PRK10743   1 MRN-FDLSPLYRSAIGFDRLFNLLENN-QSQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHAD 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598322   81 KSTDNvTYLHQGIAQRAFKLSFRLADHIEVKAASLANGLLNIDLVRLVPEEAKPKRIAIN 140
Cdd:PRK10743  79 EQKER-TYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEIN 137
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 39-142 1.03e-32

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 111.40  E-value: 1.03e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598322  39 YNVEKHgDDEYRIVIAAAGFQEEDLDLQVERGVLTVSGGKR-EKSTDNVTYLHQGIAQRAFKLSFRLADHIEVKA--ASL 115
Cdd:COG0071   2 VDIEET-DDAYVITADLPGVDKEDIDVTVEGNVLTISGERKeEEEEEGENYLRRERRYGSFERSFTLPDDVDVDKieASY 80

                        90       100
                ....*....|....*....|....*..
gi 15598322 116 ANGLLNIDLVRlvPEEAKPKRIAINGQ 142
Cdd:COG0071  81 ENGVLTITLPK--AEEAKPRKIEIKAG 105
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 41-140 7.54e-20

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: 78.42  E-value: 7.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598322    41 VEKHGDDEYRIVIAAAGFQEEDLDLQVERGVLTVSgGKREKSTDNVTYLHQGIAQRAFKLSFRL---ADHIEVKaASLAN 117
Cdd:pfam00011   1 DIKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVK-GEHEEEKEDDHGLRSERSYGSFSRKFTLpenADPDKVK-ASLKD 78

                          90       100
                  ....*....|....*....|...
gi 15598322   118 GLLNIDLVRLVPeEAKPKRIAIN 140
Cdd:pfam00011  79 GVLTVTVPKLEP-EPKERRIQIQ 100
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 45-124 1.51e-19

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: 77.59  E-value: 1.51e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598322  45 GDDEYRIVIAAAGFQEEDLDLQVERGVLTVSGGKREKSTDNVTYLHQGIAQRAFKLSFRLADHIEVKA--ASLANGLLNI 122
Cdd:cd06464   5 TDDAYVVEADLPGFKKEDIKVEVEDGVLTISGEREEEEEEEENYLRRERSYGSFSRSFRLPEDVDPDKikASLENGVLTI 84


                ..
gi 15598322 123 DL 124
Cdd:cd06464  85 TL 86
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 46-126 1.73e-12

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: 59.14  E-value: 1.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598322  46 DDEYRIVIAAAGFQEEDLDLQVERGVLTVSgGKREKSTDnvtylhQGIAQRAFKLSFRLADHIEVKA--ASLANGLLNID 123
Cdd:cd00298   5 DDEVVVTVDLPGVKKEDIKVEVEDNVLTIS-GKREEEEE------RERSYGEFERSFELPEDVDPEKskASLENGVLEIT 77


                ...
gi 15598322 124 LVR 126
Cdd:cd00298  78 LPK 80
ACD_LpsHSP_like cd06471
Group of bacterial proteins containing an alpha crystallin domain (ACD) similar to ...
 46-124 4.89e-08

Group of bacterial proteins containing an alpha crystallin domain (ACD) similar to Lactobacillus plantarum (Lp) small heat shock proteins (sHsp) HSP 18.5, HSP 18.55 and HSP 19.3. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Transcription of the genes encoding Lp HSP 18.5, 18.55 and 19.3 is regulated by a variety of stresses including heat, cold and ethanol. Early growing L. plantarum cells contain elevated levels of these mRNAs which rapidly fall of as the cells enter stationary phase. Also belonging to this group is Bifidobacterium breve (Bb) HSP20 and Oenococcus oenis (syn. Leuconostoc oenos) (Oo) HSP18. Transcription of the gene encoding BbHSP20 is strongly induced following heat or osmotic shock, and that of the gene encoding OoHSP18 following heat, ethanol or acid shock. OoHSP18 is peripherally associated with the cytoplasmic membrane.


Pssm-ID: 107228  Cd Length: 93  Bit Score: 47.86  E-value: 4.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598322  46 DDEYRIVIAAAGFQEEDLDLQVERGVLTVSgGKREKSTD----NVTYLHQGIAQRAFKLSFRL--ADHIEVKaASLANGL 119
Cdd:cd06471   9 DDEYIVEADLPGFKKEDIKLDYKDGYLTIS-AKRDESKDekdkKGNYIRRERYYGSFSRSFYLpnVDEEEIK-AKYENGV 86


                ....*
gi 15598322 120 LNIDL 124
Cdd:cd06471  87 LKITL 91
 
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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