ID   CBPA_SHISS              Reviewed;         306 AA.
AC   Q3Z3C3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Curved DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_01154};
GN   Name=cbpA {ECO:0000255|HAMAP-Rule:MF_01154}; OrderedLocusNames=SSON_1008;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: DNA-binding protein that preferentially recognizes a curved
CC       DNA sequence. It is probably a functional analog of DnaJ; displays
CC       overlapping activities with DnaJ, but functions under different
CC       conditions, probably acting as a molecular chaperone in an adaptive
CC       response to environmental stresses other than heat shock. Lacks
CC       autonomous chaperone activity; binds native substrates and targets them
CC       for recognition by DnaK. Its activity is inhibited by the binding of
CC       CbpM. {ECO:0000255|HAMAP-Rule:MF_01154}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP-
CC       Rule:MF_01154}.
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DR   EMBL; CP000038; AAZ87739.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3Z3C3; -.
DR   SMR; Q3Z3C3; -.
DR   EnsemblBacteria; AAZ87739; AAZ87739; SSON_1008.
DR   KEGG; ssn:SSON_1008; -.
DR   HOGENOM; CLU_017633_0_0_6; -.
DR   OMA; WDAGFEF; -.
DR   Proteomes; UP000002529; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR   GO; GO:0003681; F:bent DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   HAMAP; MF_01154; CbpA; 1.
DR   InterPro; IPR023859; DNA-bd_curved-DNA.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR036869; J_dom_sf.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   SUPFAM; SSF49493; SSF49493; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; DNA-binding.
FT   CHAIN           1..306
FT                   /note="Curved DNA-binding protein"
FT                   /id="PRO_0000286887"
FT   DOMAIN          5..69
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01154"
SQ   SEQUENCE   306 AA;  34406 MW;  8CFD7CA1F44BA317 CRC64;
     MELKDYYAIM GVKPTDDLKT IKTAYRRLAR KYHPDVSKEP DAEARFKEVA EAWEVLSDEQ
     RRAEYDQMWQ HRNDPQFNHQ FHHGDGQSFN AEDFDDIFSS IFGQHARQSR QRPAARGHDI
     EIEVAVFLEE TLTEHKRTIS YNLPVYNAFG MIEQEIPKTL NVKIPAGVGN GQRIRLKGQG
     TPGENGGPNG DLWLVIHIAP HPLFDIVGQD LEIVVPVSPW EAALGAKVTV PTLKESILLT
     IPPGSQAGQR LRVKGKGLVS KKQTGDLYAV LKIVMPPKPD ENTAALWQQL ADAQSSFDPR
     KDWGKA