ID   CBPA_PSEPW              Reviewed;         317 AA.
AC   B1J5W7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Curved DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_01154};
GN   Name=cbpA {ECO:0000255|HAMAP-Rule:MF_01154};
GN   OrderedLocusNames=PputW619_4640;
OS   Pseudomonas putida (strain W619).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W619;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas putida W619.";
RL   Submitted (FEB-2008) 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; CP000949; ACA75120.1; -; Genomic_DNA.
DR   RefSeq; WP_012316439.1; NC_010501.1.
DR   AlphaFoldDB; B1J5W7; -.
DR   SMR; B1J5W7; -.
DR   STRING; 390235.PputW619_4640; -.
DR   EnsemblBacteria; ACA75120; ACA75120; PputW619_4640.
DR   KEGG; ppw:PputW619_4640; -.
DR   eggNOG; COG0484; Bacteria.
DR   HOGENOM; CLU_017633_0_0_6; -.
DR   OMA; WDAGFEF; -.
DR   OrthoDB; 1738789at2; -.
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..317
FT                   /note="Curved DNA-binding protein"
FT                   /id="PRO_1000137754"
FT   DOMAIN          5..69
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01154"
SQ   SEQUENCE   317 AA;  34552 MW;  4414BEA6EEEC03D2 CRC64;
     MDFKDYYKIL GVEPTADEKA IKAAYRKLAR KYHPDVSKER DAEEKFKEAN EAYEVLGDAQ
     KRAEFDEIRK YGGQHGRPFQ APPGWENRGG AGGGFEGGDF SDFFSSIFGA RGGNPFGGAR
     QQRSAGRRGQ DVELELAIFL EETLSKESKQ ISFQVPQTNA AGQRTGFTTK TLNVKIPAGV
     SDGERIRLKG QGAPGSAGGA NGDLFLTIRM APHPLFDVEG QDLIITVPLA PWEAALGTKV
     AVPTLDGKIN LTIRPDSQSG QRLRVPGKGL ANKQGERGNL YAQLKVVMPP ASDASTRQLW
     TQLSEKAAFN PRTQWSK