ID   CBPA_CITK8              Reviewed;         306 AA.
AC   A8AI78;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Curved DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_01154};
GN   Name=cbpA {ECO:0000255|HAMAP-Rule:MF_01154}; OrderedLocusNames=CKO_02066;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000822; ABV13191.1; -; Genomic_DNA.
DR   RefSeq; WP_012132923.1; NC_009792.1.
DR   AlphaFoldDB; A8AI78; -.
DR   BMRB; A8AI78; -.
DR   SMR; A8AI78; -.
DR   STRING; 290338.CKO_02066; -.
DR   EnsemblBacteria; ABV13191; ABV13191; CKO_02066.
DR   GeneID; 45136023; -.
DR   KEGG; cko:CKO_02066; -.
DR   HOGENOM; CLU_017633_0_0_6; -.
DR   OMA; WDAGFEF; -.
DR   OrthoDB; 1738789at2; -.
DR   Proteomes; UP000008148; 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; Reference proteome.
FT   CHAIN           1..306
FT                   /note="Curved DNA-binding protein"
FT                   /id="PRO_1000065525"
FT   DOMAIN          5..69
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01154"
SQ   SEQUENCE   306 AA;  34453 MW;  8B02E6CC5F400B5C CRC64;
     MELKDYYAIM GVKPTDDLKT IKTAYRRLAR KYHPDVSKEP DAEARFKEVA EAWEVLSDEQ
     RRAEYDQLWQ HRNDPQFNRQ FQQGEGQSYN AEDFDDIFSS IFGQHGQQSR QRQATRGHDI
     EIEVAVFLEE TLAEHSRTIS YNLPVYNAFG LVEREIPKTL NVKIPAGVGN GQRIRLKGQG
     TPGENGGPNG DLWLVIHIAP HPLFDIVNQD LEIVVPLAPW EAALGAKVAV PTLKEKILLT
     IPPGSQAGQR LRIRGKGLVS KKHTGDLYAV IKIVMPPKPD DSATALWQQL ADAQSSFDPR
     KEWGKA