ID   CBPA_COXBR              Reviewed;         313 AA.
AC   A9NDK6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Curved DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_01154};
GN   Name=cbpA {ECO:0000255|HAMAP-Rule:MF_01154};
GN   OrderedLocusNames=COXBURSA331_A1271;
OS   Coxiella burnetii (strain RSA 331 / Henzerling II).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=360115;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 331 / Henzerling II;
RA   Seshadri R., Samuel J.E.;
RT   "Genome sequencing of phylogenetically and phenotypically diverse Coxiella
RT   burnetii isolates.";
RL   Submitted (NOV-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; CP000890; ABX77619.1; -; Genomic_DNA.
DR   RefSeq; WP_012220518.1; NC_010117.1.
DR   AlphaFoldDB; A9NDK6; -.
DR   SMR; A9NDK6; -.
DR   KEGG; cbs:COXBURSA331_A1271; -.
DR   HOGENOM; CLU_017633_0_0_6; -.
DR   OMA; WDAGFEF; -.
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..313
FT                   /note="Curved DNA-binding protein"
FT                   /id="PRO_1000085338"
FT   DOMAIN          5..69
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01154"
FT   REGION          71..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   313 AA;  34935 MW;  185AD1B5F9B80A86 CRC64;
     MEYQDYYKIL GVSRDATADE IKKSYRKLAR KYHPDVSSEP NAEEKFKQVK EAYEVLKDVE
     KRKAYDAIGS GWKQGQGFTP PPGWESRPGG EGVRPEFREG FSDFFESLFG GLGQEARWTR
     QEFKQRGQDQ HSRVTVSLEE AFNGSTRLLT LQEPIVDYQT GQVTSKTRQL RIKIPAGVTE
     GQQIRLQGQG LPGIGGAPNG DLYLEIHLAP HSLFTVEGKD VYLNLPVTPW EAALGAKVSI
     PTLGGSVDLT LPPGSQTGQK LRLKGRGLPG GTPGDQYVLI KIYIPEPKND QQKELYQQMA
     EQMPFDPRKE LLG