ID CBPA_SALSV Reviewed; 306 AA.
AC B4TSM3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Curved DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_01154};
GN Name=cbpA {ECO:0000255|HAMAP-Rule:MF_01154}; OrderedLocusNames=SeSA_A1176;
OS Salmonella schwarzengrund (strain CVM19633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=439843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CVM19633;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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; CP001127; ACF90419.1; -; Genomic_DNA.
DR RefSeq; WP_000420603.1; NC_011094.1.
DR AlphaFoldDB; B4TSM3; -.
DR SMR; B4TSM3; -.
DR KEGG; sew:SeSA_A1176; -.
DR HOGENOM; CLU_017633_0_0_6; -.
DR Proteomes; UP000001865; 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_1000137762"
FT DOMAIN 5..69
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01154"
SQ SEQUENCE 306 AA; 34693 MW; CE844989AD3162CE CRC64;
MELKDYYAIM GVKPTDDLKT IKTAYRRLAR KYHPDVSKEP DAEARFKEVA 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
//
