CBPA_COXBN
ID CBPA_COXBN Reviewed; 313 AA.
AC A9KE65;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Curved DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_01154};
GN Name=cbpA {ECO:0000255|HAMAP-Rule:MF_01154}; OrderedLocusNames=CBUD_1223;
OS Coxiella burnetii (strain Dugway 5J108-111).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=434922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dugway 5J108-111;
RX PubMed=19047403; DOI=10.1128/iai.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the genus
RT Coxiella.";
RL Infect. Immun. 77:642-656(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABS77033.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000733; ABS77033.2; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_012220518.1; NC_009727.1.
DR AlphaFoldDB; A9KE65; -.
DR SMR; A9KE65; -.
DR PRIDE; A9KE65; -.
DR EnsemblBacteria; ABS77033; ABS77033; CBUD_1223.
DR KEGG; cbd:CBUD_1223; -.
DR HOGENOM; CLU_017633_0_0_6; -.
DR OMA; WDAGFEF; -.
DR Proteomes; UP000008555; 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..313
FT /note="Curved DNA-binding protein"
FT /id="PRO_1000085337"
FT DOMAIN 5..69
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01154"
FT REGION 71..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 313 AA; 34935 MW; 185AD1B5F9B80A86 CRC64;
MEYQDYYKIL GVSRDATADE IKKSYRKLAR KYHPDVSSEP NAEEKFKQVK EAYEVLKDVE
KRKAYDAIGS GWKQGQGFTP PPGWESRPGG EGVRPEFREG FSDFFESLFG GLGQEARWTR
QEFKQRGQDQ HSRVTVSLEE AFNGSTRLLT LQEPIVDYQT GQVTSKTRQL RIKIPAGVTE
GQQIRLQGQG LPGIGGAPNG DLYLEIHLAP HSLFTVEGKD VYLNLPVTPW EAALGAKVSI
PTLGGSVDLT LPPGSQTGQK LRLKGRGLPG GTPGDQYVLI KIYIPEPKND QQKELYQQMA
EQMPFDPRKE LLG
