CBPA_PSEPG
ID CBPA_PSEPG Reviewed; 318 AA.
AC B0KK26;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Curved DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_01154};
GN Name=cbpA {ECO:0000255|HAMAP-Rule:MF_01154};
GN OrderedLocusNames=PputGB1_4905;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-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; CP000926; ABZ00790.1; -; Genomic_DNA.
DR RefSeq; WP_012274421.1; NC_010322.1.
DR AlphaFoldDB; B0KK26; -.
DR SMR; B0KK26; -.
DR STRING; 76869.PputGB1_4905; -.
DR EnsemblBacteria; ABZ00790; ABZ00790; PputGB1_4905.
DR KEGG; ppg:PputGB1_4905; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_017633_0_0_6; -.
DR OMA; WDAGFEF; -.
DR Proteomes; UP000002157; 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 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..318
FT /note="Curved DNA-binding protein"
FT /id="PRO_1000085340"
FT DOMAIN 5..69
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01154"
FT REGION 111..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 318 AA; 34696 MW; 152942690C7A94B1 CRC64;
MDFKDYYKIL GVEPTADDKA IKAAYRKLAR KYHPDVSKER DAEDKFKEAN EAYEVLGDAQ
KRAEFDEIRK YGGQHGRPFQ APPGWENRGG GGGFEGGDFS DFFSSIFGGR GGGNPFGGAR
QQQRSAGRRG QDVELELAVF LEETLSKESK QISFQVPQTN AMGQRTGFTT KTLNVKIPAG
VTDGERIRLK GQGAPGSGGG ANGDLFLTLR MAPHPLFDVE GHDLIITVPL APWEAALGAK
VAVPTLEGKI NLTIRPDSQS GQRLRVPGKG LANKQGERGN LYAQLKVVMP TTSDESTREL
WAKLSEKAAF NPRAQWSK