(data stored in SCRATCH zone)

HOGENOM: ECOL6_1_PE4514

ID   ECOL6_1_PE4514                       STANDARD;      PRT;   142 AA.
AC   ECOL6_1_PE4514; P0C059; P29210; P76733;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Small heat shock protein ibpB;AltName: Full=16 kDa heat
DE   shock protein B; (ECOL6_1.PE4514).
GN   Name=ibpB; OrderedLocusNames=c4606;
OS   ESCHERICHIA COLI O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECOL6_1.PE4514.
CC       Escherichia coli O6 (strain UPEC / O6:H1 / ATCC 700928 / CFT073)
CC       chromosome, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:IBPB_ECOL6
CC   -!- FUNCTION: Associates with aggregated proteins, together with IbpA,
CC       to stabilize and protect them from irreversible denaturation and
CC       extensive proteolysis during heat shock and oxidative stress.
CC       Aggregated proteins bound to the IbpAB complex are more
CC       efficiently refolded and reactivated by the ATP-dependent
CC       chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-
CC       independent (By similarity).
CC   -!- SUBUNIT: Homodimer. Forms homomultimers of about 100-150 subunits
CC       at optimal growth temperatures. Conformation changes to oligomers
CC       at high temperatures or high ionic concentrations. The decrease in
CC       size of the multimers is accompanied by an increase in chaperone
CC       activity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: The N- and C-terminal flexible termini are involved in
CC       oligomerization and in the binding of non-native substrate
CC       proteins, and are essential for chaperone activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20)
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN83041.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000251750 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P0C059; P29210; P76733; -.
DR   EMBL; AE014075; AAN83041.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_756467.2; NC_004431.1.
DR   ProteinModelPortal; P0C059; -.
DR   SMR; P0C059; 30-123.
DR   MINT; MINT-1223443; -.
DR   EnsemblBacteria; EBESCT00000041391; EBESCP00000039740; EBESCG00000040441.
DR   GeneID; 1039882; -.
DR   GenomeReviews; AE014075_GR; c4606.
DR   KEGG; ecc:c4606; -.
DR   GeneTree; EBGT00050000010332; -.
DR   OMA; HQGLVFK; -.
DR   ProtClustDB; PRK11597; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   HAMAP; MF_02001; HSP20_IbpB; 1; -.
DR   InterPro; IPR002068; Hsp20.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR022848; HSP20_IbpB.
DR   Pfam; PF00011; HSP20; 1.
DR   SUPFAM; SSF49764; HSP20_chap; 1.
DR   PROSITE; PS01031; HSP20; 1.
DR   HOGENOMDNA; ECOL6_1.PE4514; -.
KW   AAN83041.1000068575old_1320000031;
KW   Small heat shock protein ibpB ;
KW   Chaperone; Complete proteome; Cytoplasm; Stress response.
SQ   SEQUENCE   142 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRNFDLSPLM RQWIGFDKLA NALQNAGESQ SFPPYNIEKS DDNHYRITLA LAGFRQEDLE
     IQLEGTRLSV KGTPEQPKEE KKWLHQGLMN QPFSLSFTLA ENMEVSGATF VNGLLHIDLI
     RNEPEPIAAQ RIAISERPAL NS
//

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