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Conserved domains on  [gi|504345588|ref|WP_014532690|]
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MULTISPECIES: Hsp20/alpha crystallin family protein [Staphylococcus]

Protein Classification

Hsp20/alpha crystallin family protein( domain architecture ID 11414641)

Hsp20/alpha crystallin family protein is a small, stress-induced protein, between 12-43 kDa, which functions as an ATP-independent chaperone that prevents aggregation and protects against cell stress, induced by heat, osmotic, or acid shock

Gene Ontology:  GO:0009408|GO:0042802
PubMed:  15335775|2853609|7723051|22177323
SCOP:  4002439

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 41-142 1.45e-28

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


:

Pssm-ID: 439841  Cd Length: 105  Bit Score: 100.61  E-value: 1.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345588  41 NIYETDELYYLEAELAGVNKEDISIDFNNNTLTIQATRSAKH--KSEQLILDERNFESLMRQFDF-EAVDKQHITASFEN 117
Cdd:COG0071    3 DIEETDDAYVITADLPGVDKEDIDVTVEGNVLTISGERKEEEeeEGENYLRRERRYGSFERSFTLpDDVDVDKIEASYEN 82

                         90       100
                 ....*....|....*....|....*
gi 504345588 118 GLLTITLPKikpsNETTSSTSIPIS 142
Cdd:COG0071   83 GVLTITLPK----AEEAKPRKIEIK 103
 
Name Accession Description Interval E-value
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 41-142 1.45e-28

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 100.61  E-value: 1.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345588  41 NIYETDELYYLEAELAGVNKEDISIDFNNNTLTIQATRSAKH--KSEQLILDERNFESLMRQFDF-EAVDKQHITASFEN 117
Cdd:COG0071    3 DIEETDDAYVITADLPGVDKEDIDVTVEGNVLTISGERKEEEeeEGENYLRRERRYGSFERSFTLpDDVDVDKIEASYEN 82

                         90       100
                 ....*....|....*....|....*
gi 504345588 118 GLLTITLPKikpsNETTSSTSIPIS 142
Cdd:COG0071   83 GVLTITLPK----AEEAKPRKIEIK 103
ACD_LpsHSP_like cd06471
Group of bacterial proteins containing an alpha crystallin domain (ACD) similar to ...
 38-126 2.89e-27

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: 97.16  E-value: 2.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345588  38 FVTNIYETDELYYLEAELAGVNKEDISIDFNNNTLTIQATRSA----KHKSEQLILDERNFESLMRQFDFEAVDKQHITA 113
Cdd:cd06471    1 MKTDIKETDDEYIVEADLPGFKKEDIKLDYKDGYLTISAKRDEskdeKDKKGNYIRRERYYGSFSRSFYLPNVDEEEIKA 80

                         90
                 ....*....|...
gi 504345588 114 SFENGLLTITLPK 126
Cdd:cd06471   81 KYENGVLKITLPK 93
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 42-142 1.34e-15

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: 67.25  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345588   42 IYETDELYYLEAELAGVNKEDISIDFNNNTLTIQATRSAKHKSEQLILDERNFESLMRQFDF-EAVDKQHITASFENGLL 120
Cdd:pfam00011   2 IKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEEEKEDDHGLRSERSYGSFSRKFTLpENADPDKVKASLKDGVL 81

                          90       100
                  ....*....|....*....|..
gi 504345588  121 TITLPKIKPSNettSSTSIPIS 142
Cdd:pfam00011  82 TVTVPKLEPEP---KERRIQIQ 100
 
Name Accession Description Interval E-value
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 41-142 1.45e-28

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 100.61  E-value: 1.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345588  41 NIYETDELYYLEAELAGVNKEDISIDFNNNTLTIQATRSAKH--KSEQLILDERNFESLMRQFDF-EAVDKQHITASFEN 117
Cdd:COG0071    3 DIEETDDAYVITADLPGVDKEDIDVTVEGNVLTISGERKEEEeeEGENYLRRERRYGSFERSFTLpDDVDVDKIEASYEN 82

                         90       100
                 ....*....|....*....|....*
gi 504345588 118 GLLTITLPKikpsNETTSSTSIPIS 142
Cdd:COG0071   83 GVLTITLPK----AEEAKPRKIEIK 103
ACD_LpsHSP_like cd06471
Group of bacterial proteins containing an alpha crystallin domain (ACD) similar to ...
 38-126 2.89e-27

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: 97.16  E-value: 2.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345588  38 FVTNIYETDELYYLEAELAGVNKEDISIDFNNNTLTIQATRSA----KHKSEQLILDERNFESLMRQFDFEAVDKQHITA 113
Cdd:cd06471    1 MKTDIKETDDEYIVEADLPGFKKEDIKLDYKDGYLTISAKRDEskdeKDKKGNYIRRERYYGSFSRSFYLPNVDEEEIKA 80

                         90
                 ....*....|...
gi 504345588 114 SFENGLLTITLPK 126
Cdd:cd06471   81 KYENGVLKITLPK 93
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 41-126 3.88e-26

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: 94.16  E-value: 3.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345588  41 NIYETDELYYLEAELAGVNKEDISIDFNNNTLTIQATRSAKHKSEQ-LILDERNFESLMRQFDF-EAVDKQHITASFENG 118
Cdd:cd06464    1 DVYETDDAYVVEADLPGFKKEDIKVEVEDGVLTISGEREEEEEEEEnYLRRERSYGSFSRSFRLpEDVDPDKIKASLENG 80


                 ....*...
gi 504345588 119 LLTITLPK 126
Cdd:cd06464   81 VLTITLPK 88
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 42-126 1.45e-21

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: 82.25  E-value: 1.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345588  42 IYETDELYYLEAELAGVNKEDISIDFNNNTLTIQATRSAKHKSeqlildERNFESLMRQFDF-EAVDKQHITASFENGLL 120
Cdd:cd00298    1 WYQTDDEVVVTVDLPGVKKEDIKVEVEDNVLTISGKREEEEER------ERSYGEFERSFELpEDVDPEKSKASLENGVL 74


                 ....*.
gi 504345588 121 TITLPK 126
Cdd:cd00298   75 EITLPK 80
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 42-142 1.34e-15

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: 67.25  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345588   42 IYETDELYYLEAELAGVNKEDISIDFNNNTLTIQATRSAKHKSEQLILDERNFESLMRQFDF-EAVDKQHITASFENGLL 120
Cdd:pfam00011   2 IKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEEEKEDDHGLRSERSYGSFSRKFTLpENADPDKVKASLKDGVL 81

                          90       100
                  ....*....|....*....|..
gi 504345588  121 TITLPKIKPSNettSSTSIPIS 142
Cdd:pfam00011  82 TVTVPKLEPEP---KERRIQIQ 100
ACD_ScHsp26_like cd06472
Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein ...
 44-126 4.21e-14

Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein (Hsp)26 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. ScHsp26 is temperature-regulated, it switches from an inactive to a chaperone-active form upon elevation in temperature. It associates into large 24-mers storage forms which upon heat shock disassociate into dimers. These dimers initiate the interaction with non-native substrate proteins and re-assemble into large globular assemblies having one monomer of substrate bound per dimer. This group also contains Arabidopsis thaliana (Ath) Hsp15.7, a peroxisomal matrix protein which can complement the morphological phenotype of S. cerevisiae mutants deficient in Hsps26. AthHsp15.7 is minimally expressed under normal conditions and is strongly induced by heat and oxidative stress. Also belonging to this group is wheat HSP16.9 which differs in quaternary structure from the shell-type particles of ScHsp26, it assembles as a dodecameric double disc, with each disc organized as a trimer of dimers.


Pssm-ID: 107229  Cd Length: 92  Bit Score: 63.48  E-value: 4.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345588  44 ETDELYYLEAELAGVNKEDISIDF-NNNTLTIQATRSA--KHKSEQLILDERNFESLMRQFDF-EAVDKQHITASFENGL 119
Cdd:cd06472    6 ETPEAHVFKADVPGVKKEDVKVEVeDGRVLRISGERKKeeEKKGDDWHRVERSSGRFVRRFRLpENADADEVKAFLENGV 85


                 ....*..
gi 504345588 120 LTITLPK 126
Cdd:cd06472   86 LTVTVPK 92
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 41-124 1.96e-07

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: 45.99  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345588  41 NIYETDELYY-LEAELAGVNKEDISIDFNNNTLTIQATRSAKHKSEQLILD----ERNFEslmRQFDFEavDKQHIT-AS 114
Cdd:cd06470    4 NIEKTGENNYrITLAVAGFSEDDLEIEVENNQLTVTGKKADEENEEREYLHrgiaKRAFE---RSFNLA--DHVKVKgAE 78

                         90
                 ....*....|
gi 504345588 115 FENGLLTITL 124
Cdd:cd06470   79 LENGLLTIDL 88
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 43-131 2.90e-03

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes 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). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107220  Cd Length: 84  Bit Score: 34.57  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345588  43 YETDELYYLEAELAGVNKEDISIDFNNNTLTIqatrSAKHKSEQLILDERNFeslmrqfdFEAVDKQHITASFENGLLTI 122
Cdd:cd06463    2 YQTLDEVTITIPLKDVTKKDVKVEFTPKSLTV----SVKGGGGKEYLLEGEL--------FGPIDPEESKWTVEDRKIEI 69


                 ....*....
gi 504345588 123 TLPKIKPSN 131
Cdd:cd06463   70 TLKKKEPGE 78
 
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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