ID CBPA_SHIF8 Reviewed; 306 AA.
AC Q0T634;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Curved DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_01154};
GN Name=cbpA {ECO:0000255|HAMAP-Rule:MF_01154}; OrderedLocusNames=SFV_1012;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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; CP000266; ABF03231.1; -; Genomic_DNA.
DR RefSeq; WP_000420619.1; NC_008258.1.
DR AlphaFoldDB; Q0T634; -.
DR SMR; Q0T634; -.
DR KEGG; sfv:SFV_1012; -.
DR HOGENOM; CLU_017633_0_0_6; -.
DR Proteomes; UP000000659; 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 CDD; cd10747; DnaJ_C; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 1.20.5.460; Single helix bin; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
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 PANTHER; PTHR43096:SF69; CURVED DNA-BINDING PROTEIN; 1.
DR PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 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_0000286886"
FT DOMAIN 5..69
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01154"
SQ SEQUENCE 306 AA; 34455 MW; E5EFED8D8A26F47A CRC64;
MELKDYYAIM GVKPTDDLKT IKTAYRRLAR KYHPDVSKEP DAEARFKEVA EAWEVLSDEQ
RRAEYDQMWQ HRNDPQFNRQ FHHGDGQSFN AEDFDDIFSS IFGQHARQSR QRPAARGHDI
EIEVAVFLEE TLTEHKRTIS YNLPVYNAFG MIEQEIPKTL NVKIPAGVGN GQRIRLKGQG
TPGENGGPNG DLWLVIHIAP HPLFDIVGQD LEIVVPVSPW EAALGTKVTV PTLKESILLT
IPPGSQAGQR LRVKGKGLVS KKQTGDLYAV LKIVMPPKPD ENTAALWQQL ADAQSSFDPR
KDWGKA
//
