ID   CBPA_SALCH              Reviewed;         306 AA.
AC   Q57QP2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-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=SCH_1063;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(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; AE017220; AAX64969.1; -; Genomic_DNA.
DR   RefSeq; WP_001539671.1; NC_006905.1.
DR   AlphaFoldDB; Q57QP2; -.
DR   SMR; Q57QP2; -.
DR   EnsemblBacteria; AAX64969; AAX64969; SCH_1063.
DR   KEGG; sec:SCH_1063; -.
DR   HOGENOM; CLU_017633_0_0_6; -.
DR   OMA; WDAGFEF; -.
DR   Proteomes; UP000000538; 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_0000286883"
FT   DOMAIN          5..69
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01154"
SQ   SEQUENCE   306 AA;  34692 MW;  CE864B23AD34ADAE CRC64;
     MELKDYYAIM GVKPTDDLKT IKTAYRRLAR KYHPDVSKEP NAEARFKEVA EAWEVLSDEQ
     RRAEYDQLWQ HRNDPQFNRQ FQQHEGQPYN AEDFDDIFSS IFGQHGRHSH HRHAARGHDI
     EIEVAVFLEE TLEEHQRTIS YSVPVYNAFG LVEREIPKTL NVKIPAGVSN GQRIRLKGQG
     TPGENGGPNG DLWLVIHIAP HPLFDIVNQD LEVVLPLAPW EAALGAKVSV PTLKERILLT
     IPPGSQAGQR LRIKGKGLAS KKHTGDLYAI IKIVMPPKPD EKTAALWQQL ADAQSSFDPR
     QQWGKA