AC   MF_02001;
DC   Protein; auto
TR   HAMAP; MF_02001; -; 1; level=0
XX
Names: HSP20_IbpB
XX
ID   IBPB
DE   RecName: Full=Small heat shock protein IbpB;
DE   AltName: Full=16 kDa heat shock protein B;
GN   Name=ibpB;
XX
CC   -!- FUNCTION: Associates with aggregated proteins, together with IbpA, to
CC       stabilize and protect them from irreversible denaturation and extensive
CC       proteolysis during heat shock and oxidative stress. Aggregated proteins
CC       bound to the IbpAB complex are more efficiently refolded and
CC       reactivated by the ATP-dependent chaperone systems ClpB and
CC       DnaK/DnaJ/GrpE. Its activity is ATP-independent.
CC   -!- SUBUNIT: Homodimer. Forms homomultimers of about 100-150 subunits at
CC       optimal growth temperatures. Conformation changes to oligomers at high
CC       temperatures or high ionic concentrations. The decrease in size of the
CC       multimers is accompanied by an increase in chaperone activity.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: The N- and C-terminal flexible termini are involved in
CC       oligomerization and in the binding of non-native substrate proteins,
CC       and are essential for chaperone activity.
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
XX
DR   Pfam; PF00011; HSP20; 1; trigger=no
DR   PROSITE; PS01031; SHSP; 1; trigger=yes
XX
KW   Cytoplasm
KW   Chaperone
KW   Stress response
XX
GO   GO:0050821; P:protein stabilization
GO   GO:0005737; C:cytoplasm
XX
FT   None
XX
Size: 140-170;
Related: None;
Template: P0C058;
Scope:
 Bacteria; Enterobacterales
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.15 2019/11/20
//