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Conserved domains on  [gi|1747555994|gb|KAA5942336|]
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heat shock chaperone IbpB [Klebsiella pneumoniae]

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
 1-142 2.21e-107

heat shock chaperone IbpB; Provisional


:

Pssm-ID: 183223  Cd Length: 142  Bit Score: 301.28  E-value: 2.21e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747555994   1 MRNYDLSPLLRQWIGFDKLASALQTAGESQSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLVVKGTPQQPEKE 80
Cdd:PRK11597    1 MRNYDLSPLLRQWIGFDKLANALQNAGESQSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLTVKGTPEQPEKE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1747555994  81 TTWLHQGLVSQAFSLSFTLADNMEVSGATFTNGLLHIDLTRNEPEQIAPQRIAISERPALNS 142
Cdd:PRK11597   81 VKWLHQGLVNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEAIAPQRIAISERPALNS 142
 
Name Accession Description Interval E-value
PRK11597 PRK11597
heat shock chaperone IbpB; Provisional
 1-142 2.21e-107

heat shock chaperone IbpB; Provisional


Pssm-ID: 183223  Cd Length: 142  Bit Score: 301.28  E-value: 2.21e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747555994   1 MRNYDLSPLLRQWIGFDKLASALQTAGESQSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLVVKGTPQQPEKE 80
Cdd:PRK11597    1 MRNYDLSPLLRQWIGFDKLANALQNAGESQSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLTVKGTPEQPEKE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1747555994  81 TTWLHQGLVSQAFSLSFTLADNMEVSGATFTNGLLHIDLTRNEPEQIAPQRIAISERPALNS 142
Cdd:PRK11597   81 VKWLHQGLVNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEAIAPQRIAISERPALNS 142
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 33-121 3.19e-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: 142.29  E-value: 3.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747555994  33 PPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLVVKGTPQQPE-KETTWLHQGLVSQAFSLSFTLADNMEVSGATFT 111
Cdd:cd06470     1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEEnEEREYLHRGIAKRAFERSFNLADHVKVKGAELE 80

                          90
                  ....*....|
gi 1747555994 112 NGLLHIDLTR 121
Cdd:cd06470    81 NGLLTIDLER 90
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 35-135 4.59e-30

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 104.46  E-value: 4.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747555994  35 YNIEKSDDnHYRITLALAGFRQEDLDIQLEGTRLVVKG--TPQQPEKETTWLHQGLVSQAFSLSFTLADNMEVSG--ATF 110
Cdd:COG0071     2 VDIEETDD-AYVITADLPGVDKEDIDVTVEGNVLTISGerKEEEEEEGENYLRRERRYGSFERSFTLPDDVDVDKieASY 80

                          90       100
                  ....*....|....*....|....*
gi 1747555994 111 TNGLLHIDLTRNEPEQiaPQRIAIS 135
Cdd:COG0071    81 ENGVLTITLPKAEEAK--PRKIEIK 103
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 38-135 1.27e-27

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: 98.07  E-value: 1.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747555994  38 EKSDDNHYRITLALAGFRQEDLDIQLEGTRLVVKGTPQQPEKETTWLHQGLVSQAFSLSFTL---ADNMEVSgATFTNGL 114
Cdd:pfam00011   2 IKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEEEKEDDHGLRSERSYGSFSRKFTLpenADPDKVK-ASLKDGV 80

                          90       100
                  ....*....|....*....|.
gi 1747555994 115 LHIDLTRNEPEQiAPQRIAIS 135
Cdd:pfam00011  81 LTVTVPKLEPEP-KERRIQIQ 100
 
Name Accession Description Interval E-value
PRK11597 PRK11597
heat shock chaperone IbpB; Provisional
 1-142 2.21e-107

heat shock chaperone IbpB; Provisional


Pssm-ID: 183223  Cd Length: 142  Bit Score: 301.28  E-value: 2.21e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747555994   1 MRNYDLSPLLRQWIGFDKLASALQTAGESQSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLVVKGTPQQPEKE 80
Cdd:PRK11597    1 MRNYDLSPLLRQWIGFDKLANALQNAGESQSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLTVKGTPEQPEKE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1747555994  81 TTWLHQGLVSQAFSLSFTLADNMEVSGATFTNGLLHIDLTRNEPEQIAPQRIAISERPALNS 142
Cdd:PRK11597   81 VKWLHQGLVNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEAIAPQRIAISERPALNS 142
PRK10743 PRK10743
heat shock chaperone IbpA;
1-134 1.65e-45

heat shock chaperone IbpA;


Pssm-ID: 182691  Cd Length: 137  Bit Score: 144.95  E-value: 1.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747555994   1 MRNYDLSPLLRQWIGFDKLASALQTaGESQS---FPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLVVKGTPQQP 77
Cdd:PRK10743    1 MRNFDLSPLYRSAIGFDRLFNLLEN-NQSQSnggYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1747555994  78 EKETTWLHQGLVSQAFSLSFTLADNMEVSGATFTNGLLHIDLTRNEPEQIAPQRIAI 134
Cdd:PRK10743   80 QKERTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEI 136
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 33-121 3.19e-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: 142.29  E-value: 3.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747555994  33 PPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLVVKGTPQQPE-KETTWLHQGLVSQAFSLSFTLADNMEVSGATFT 111
Cdd:cd06470     1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEEnEEREYLHRGIAKRAFERSFNLADHVKVKGAELE 80

                          90
                  ....*....|
gi 1747555994 112 NGLLHIDLTR 121
Cdd:cd06470    81 NGLLTIDLER 90
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 35-135 4.59e-30

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 104.46  E-value: 4.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747555994  35 YNIEKSDDnHYRITLALAGFRQEDLDIQLEGTRLVVKG--TPQQPEKETTWLHQGLVSQAFSLSFTLADNMEVSG--ATF 110
Cdd:COG0071     2 VDIEETDD-AYVITADLPGVDKEDIDVTVEGNVLTISGerKEEEEEEGENYLRRERRYGSFERSFTLPDDVDVDKieASY 80

                          90       100
                  ....*....|....*....|....*
gi 1747555994 111 TNGLLHIDLTRNEPEQiaPQRIAIS 135
Cdd:COG0071    81 ENGVLTITLPKAEEAK--PRKIEIK 103
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 38-135 1.27e-27

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: 98.07  E-value: 1.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747555994  38 EKSDDNHYRITLALAGFRQEDLDIQLEGTRLVVKGTPQQPEKETTWLHQGLVSQAFSLSFTL---ADNMEVSgATFTNGL 114
Cdd:pfam00011   2 IKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEEEKEDDHGLRSERSYGSFSRKFTLpenADPDKVK-ASLKDGV 80

                          90       100
                  ....*....|....*....|.
gi 1747555994 115 LHIDLTRNEPEQiAPQRIAIS 135
Cdd:pfam00011  81 LTVTVPKLEPEP-KERRIQIQ 100
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 41-119 8.92e-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: 75.28  E-value: 8.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747555994  41 DDNHYRITLALAGFRQEDLDIQLEGTRLVVKGT-PQQPEKETTWLHQGLVSQAFSLSFTLADNMEVSG--ATFTNGLLHI 117
Cdd:cd06464     5 TDDAYVVEADLPGFKKEDIKVEVEDGVLTISGErEEEEEEEENYLRRERSYGSFSRSFRLPEDVDPDKikASLENGVLTI 84


                  ..
gi 1747555994 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 1.62e-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: 58.75  E-value: 1.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747555994  41 DDNHYRITLALAGFRQEDLDIQLEGTRLVVKGTPQQPEKettwlhQGLVSQAFSLSFTLADNMEVSG--ATFTNGLLHID 118
Cdd:cd00298     4 TDDEVVVTVDLPGVKKEDIKVEVEDNVLTISGKREEEEE------RERSYGEFERSFELPEDVDPEKskASLENGVLEIT 77


                  ...
gi 1747555994 119 LTR 121
Cdd:cd00298    78 LPK 80
ACD_LpsHSP_like cd06471
Group of bacterial proteins containing an alpha crystallin domain (ACD) similar to ...
 39-119 7.59e-06

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: 41.70  E-value: 7.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747555994  39 KSDDNHYRITLALAGFRQEDLDIQLEGTRLVVKGTPQQPE----KETTWLHQGLVSQAFSLSFTLaDNMEVSG--ATFTN 112
Cdd:cd06471     6 KETDDEYIVEADLPGFKKEDIKLDYKDGYLTISAKRDESKdekdKKGNYIRRERYYGSFSRSFYL-PNVDEEEikAKYEN 84


                  ....*..
gi 1747555994 113 GLLHIDL 119
Cdd:cd06471    85 GVLKITL 91
metazoan_ACD cd06526
Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins ...
 37-117 8.75e-06

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: 41.35  E-value: 8.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747555994  37 IEKSDDNHYRITLALAGFRQEDLDIQLEGTRLVVKGtpQQPEKETtwlHQGLVSQAFSLSFTLADNMEVSG--ATFT-NG 113
Cdd:cd06526     1 VVNDDDEKFQVTLDVKGFKPEELKVKVSDNKLVVEG--KHEERED---EHGYVSREFTRRYQLPEGVDPDSvtSSLSsDG 75


                  ....
gi 1747555994 114 LLHI 117
Cdd:cd06526    76 VLTI 79
ArsA_HSP20 pfam17886
HSP20-like domain found in ArsA; This domain is found at the C-terminus of ArsA like proteins. ...
 42-117 1.75e-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: 34.77  E-value: 1.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1747555994  42 DNHYRITLALAGFRQEDLDIQLEGTRLVVKGtpqqpekettwlhqGLVSQAFSLSFTLADnMEVSGATFTNGLLHI 117
Cdd:pfam17886   1 DGGYVLRLRLPFVDKEDVDLSRSGDELIIKI--------------GNFRRNITLPRSLAR-LEVTGAKFEDGVLRI 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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