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IBPB_SHIFL
ID   IBPB_SHIFL              Reviewed;         142 AA.
AC   P0C060; P29210; P76733;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Small heat shock protein IbpB {ECO:0000255|HAMAP-Rule:MF_02001};
DE   AltName: Full=16 kDa heat shock protein B {ECO:0000255|HAMAP-Rule:MF_02001};
GN   Name=ibpB {ECO:0000255|HAMAP-Rule:MF_02001};
GN   OrderedLocusNames=SF3777, S3993;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_02001}.
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       {ECO:0000255|HAMAP-Rule:MF_02001}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02001}.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_02001}.
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC       {ECO:0000255|HAMAP-Rule:MF_02001, ECO:0000255|PROSITE-
CC       ProRule:PRU00285}.
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DR   EMBL; AE005674; AAN45219.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18978.1; -; Genomic_DNA.
DR   RefSeq; NP_709512.2; NC_004337.2.
DR   RefSeq; WP_001243431.1; NZ_WPGW01000019.1.
DR   AlphaFoldDB; P0C060; -.
DR   SMR; P0C060; -.
DR   STRING; 198214.SF3777; -.
DR   PRIDE; P0C060; -.
DR   EnsemblBacteria; AAN45219; AAN45219; SF3777.
DR   EnsemblBacteria; AAP18978; AAP18978; S3993.
DR   GeneID; 1026113; -.
DR   GeneID; 67417681; -.
DR   KEGG; sfl:SF3777; -.
DR   KEGG; sfx:S3993; -.
DR   PATRIC; fig|198214.7.peg.4458; -.
DR   HOGENOM; CLU_046737_4_2_6; -.
DR   OMA; SGNEGYP; -.
DR   OrthoDB; 1523369at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050821; P:protein stabilization; IEA:UniProtKB-UniRule.
DR   CDD; cd06470; ACD_IbpA-B_like; 1.
DR   Gene3D; 2.60.40.790; -; 1.
DR   HAMAP; MF_02001; HSP20_IbpB; 1.
DR   InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR   InterPro; IPR037913; ACD_IbpA/B.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR022848; HSP20_IbpB.
DR   Pfam; PF00011; HSP20; 1.
DR   SUPFAM; SSF49764; SSF49764; 1.
DR   PROSITE; PS01031; SHSP; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Reference proteome; Stress response.
FT   CHAIN           1..142
FT                   /note="Small heat shock protein IbpB"
FT                   /id="PRO_0000126036"
FT   DOMAIN          26..137
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
SQ   SEQUENCE   142 AA;  16093 MW;  7666BB1BDB8A673A CRC64;
     MRNFDLSPLM RQWIGFDKLA NALQNAGESQ SFPPYNIEKS DDNHYRITLA LAGFRQEDLE
     IQLEGTRLSV KGTPEQPKEE KKWLHQGLMN QPFSLSFTLA ENMEVSGATF VNGLLHIDLI
     RNEPEPIAAQ RIAISERPAL NS
 
 
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