(data stored in SCRATCH zone)

HOGENOM: ESCOL1_1_PE3635

ID   ESCOL1_1_PE3635                      STANDARD;      PRT;   142 AA.
AC   ESCOL1_1_PE3635; P0C058; P29210; P76733; Q2M7Z8;
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; (ESCOL1_1.PE3635).
GN   Name=ibpB; Synonyms=hslS, htpE; OrderedLocusNames=b3686, JW3663;
OS   ESCHERICHIA COLI STR. K-12 SUBSTR. MG1655.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=511145;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ESCOL1_1.PE3635.
CC       Escherichia coli str. K-12 substr. MG1655 chromosome, complete genome.
CC       pEp5, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:IBPB_ECOLI
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.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable up to 50 degrees Celsius;
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.
CC   -!- INTERACTION:
CC       P0C054:ibpA; NbExp=3; IntAct=EBI-552784, EBI-550729;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By heat shock.
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.
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20)
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA62038.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -!- GENE_FAMILY: HOG000251750 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P0C058; P29210; P76733; Q2M7Z8; -.
DR   EMBL; M94104; AAA24425.1; -; Genomic_DNA.
DR   EMBL; L10328; AAA62038.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC76709.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77608.1; -; Genomic_DNA.
DR   RefSeq; AP_004107.1; AC_000091.1.
DR   RefSeq; NP_418141.2; NC_000913.2.
DR   ProteinModelPortal; P0C058; -.
DR   SMR; P0C058; 30-123.
DR   DIP; DIP-48244N; -.
DR   IntAct; P0C058; 11.
DR   MINT; MINT-1223453; -.
DR   ECO2DBASE; C014.7; 6TH EDITION.
DR   EnsemblBacteria; EBESCT00000001892; EBESCP00000001892; EBESCG00000001553.
DR   EnsemblBacteria; EBESCT00000001893; EBESCP00000001893; EBESCG00000001553.
DR   EnsemblBacteria; EBESCT00000017776; EBESCP00000017067; EBESCG00000016832.
DR   GeneID; 948192; -.
DR   GenomeReviews; AP009048_GR; JW3663.
DR   GenomeReviews; U00096_GR; b3686.
DR   KEGG; ecj:JW3663; -.
DR   KEGG; eco:b3686; -.
DR   EchoBASE; EB1497; -.
DR   EcoGene; EG11535; ibpB.
DR   eggNOG; COG0071; -.
DR   GeneTree; EBGT00050000010332; -.
DR   OMA; HQGLVFK; -.
DR   ProtClustDB; PRK11597; -.
DR   BioCyc; EcoCyc:EG11535-MON; -.
DR   Genevestigator; P0C058; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0009408; P:response to heat; IEP:EcoliWiki.
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; ESCOL1_1.PE3635; -.
KW   Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Reference proteome; 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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