(data stored in ACNUC7421 zone)

HOGENOM: ECOKI_1_PE1012

ID   ECOKI_1_PE1012                       STANDARD;      PRT;   306 AA.
AC   ECOKI_1_PE1012; D5CZG2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Curved DNA-binding protein; (ECOKI_1.PE1012).
GN   Name=cbpA; OrderedLocusNames=ECOK1_1053;
OS   ESCHERICHIA COLI IHE3034.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=714962;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECOKI_1.PE1012.
CC       Escherichia coli O18:K1:H7 (strain IHE3034 / ExPEC) chromosome, complet
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D5CZG2_ECOKI
CC   -!- FUNCTION: DNA-binding protein that preferentially recognizes a
CC       curved DNA sequence. It is probably a functional analog of DnaJ;
CC       displays overlapping activities with DnaJ, but functions under
CC       different conditions, probably acting as a molecular chaperone in
CC       an adaptive response to environmental stresses other than heat
CC       shock. Lacks autonomous chaperone activity; binds native
CC       substrates and targets them for recognition by DnaK. Its activity
CC       is inhibited by the binding of CbpM (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid (By similarity).
CC   -!- SIMILARITY: Contains 1 J domain.
CC   -!- GENE_FAMILY: HOG000226716 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D5CZG2; -.
DR   EMBL; CP001969; ADE88511.1; -; Genomic_DNA.
DR   ProteinModelPortal; D5CZG2; -.
DR   SMR; D5CZG2; 2-76, 114-303.
DR   EnsemblBacteria; EBESCT00000232042; EBESCP00000215545; EBESCG00000227186.
DR   GenomeReviews; CP001969_GR; ECOK1_1053.
DR   GeneTree; EBGT00050000009076; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR   GO; GO:0003681; F:bent DNA binding; IEA:HAMAP.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   HAMAP; MF_01154; CbpA; 1; -.
DR   InterPro; IPR023859; DNA-bd_curved-DNA.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR018253; Heat_shock_DnaJ_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR003095; Hsp_DnaJ.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   SUPFAM; SSF49493; HSP40_DnaJ_pep; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   HOGENOMDNA; ECOKI_1.PE1012; -.
KW   ADE88511.1000068575old_1320000031;
KW   Curved DNA-binding protein ;
KW   Chaperone; Complete proteome; Cytoplasm; DNA-binding.
SQ   SEQUENCE   306 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MELKDYYAIM GVKPTDDLKT IKTAYRRLAR KYHPDVSKEP DAEARFKEVA EAWEVLSDEQ
     RRAEYDQMWQ HRNDPQFNRQ FHHGDGQSFN AEDFDDIFSS IFGQHARQSR QRPATRGHDI
     EIEVAVFLEE TLTEHKRTIS YNLPVYNAFG MIEQEIPKTL NVKIPAGVGN GQRIRLKGQG
     TPGENGGPNG DLWLVIHIAP HPLFDIVGQD LEIVVPVSPW EAALGTKVTV PTLKESILLT
     IPPGSQAGQR LRVKGKGLVS KKQTGDLYAV LKIVMPPKPD ENTAALWQQL ADAQSSFDPR
     KDWGKA
//

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