CBPA_ECOLC
ID CBPA_ECOLC Reviewed; 306 AA.
AC B1IV97;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Curved DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_01154};
GN Name=cbpA {ECO:0000255|HAMAP-Rule:MF_01154}; OrderedLocusNames=EcolC_2595;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS WDCM 00012 / Crooks).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
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; CP000946; ACA78226.1; -; Genomic_DNA.
DR RefSeq; WP_000420621.1; NZ_CP022959.1.
DR AlphaFoldDB; B1IV97; -.
DR SMR; B1IV97; -.
DR KEGG; ecl:EcolC_2595; -.
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..306
FT /note="Curved DNA-binding protein"
FT /id="PRO_1000085339"
FT DOMAIN 5..69
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01154"
SQ SEQUENCE 306 AA; 34455 MW; A3893D2BFDE75803 CRC64;
MELKDYYAIM GVKPTDDLKT IKTAYRRLAR KYHPDVSKEP DAEARFKEVA EAWEVLSDEQ
RRAEYDQMWQ HRNDPQFNRQ FHHGDGQSFN AEDFDDIFSS IFGQHARQSR QRPATRGHDI
EIEVAVFLEE TLTEHKRTIS YNLPVYNAFG MIEQEIPKTL NVKIPAGVGN GQRIRLKGQG
TPGENGGPNG DLWLVIHIAP HPLFDIVGQD LEIVVPVSPW EAALGAKVTV PTLKESILLT
IPPGSQAGQR LRVKGKGLVS KKQTGDLYAV LKIVMPPKPD ENTAALWQQL ADAQSSFDPR
KDWGKA