(data stored in SCRATCH zone)

SWISSPROT: DNAJ_CHLAB

ID   DNAJ_CHLAB              Reviewed;         391 AA.
AC   Q5L6F7;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   11-DEC-2019, entry version 89.
DE   RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152};
GN   Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; OrderedLocusNames=CAB318;
OS   Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=218497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27085 / S26/3;
RX   PubMed=15837807; DOI=10.1101/gr.3684805;
RA   Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA   Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA   Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA   Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT   "The Chlamydophila abortus genome sequence reveals an array of variable
RT   proteins that contribute to interspecies variation.";
RL   Genome Res. 15:629-640(2005).
CC   -!- FUNCTION: Participates actively in the response to hyperosmotic and
CC       heat shock by preventing the aggregation of stress-denatured proteins
CC       and by disaggregating proteins, also in an autonomous, DnaK-independent
CC       fashion. Unfolded proteins bind initially to DnaJ; upon interaction
CC       with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting
CC       in the formation of a stable complex. GrpE releases ADP from DnaK; ATP
CC       binding to DnaK triggers the release of the substrate protein, thus
CC       completing the reaction cycle. Several rounds of ATP-dependent
CC       interactions between DnaJ, DnaK and GrpE are required for fully
CC       efficient folding. Also involved, together with DnaK and GrpE, in the
CC       DNA replication of plasmids through activation of initiation proteins.
CC       {ECO:0000255|HAMAP-Rule:MF_01152}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01152};
CC       Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000255|HAMAP-
CC       Rule:MF_01152};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01152}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01152}.
CC   -!- DOMAIN: The J domain is necessary and sufficient to stimulate DnaK
CC       ATPase activity. Zinc center 1 plays an important role in the
CC       autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2
CC       is essential for interaction with DnaK and for DnaJ activity.
CC       {ECO:0000255|HAMAP-Rule:MF_01152}.
CC   -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01152}.
DR   EMBL; CR848038; CAH63768.1; -; Genomic_DNA.
DR   RefSeq; WP_011096982.1; NC_004552.2.
DR   SMR; Q5L6F7; -.
DR   STRING; 218497.CAB318; -.
DR   PRIDE; Q5L6F7; -.
DR   EnsemblBacteria; CAH63768; CAH63768; CAB318.
DR   KEGG; cab:CAB318; -.
DR   eggNOG; ENOG4105BZ5; Bacteria.
DR   eggNOG; COG0484; LUCA.
DR   HOGENOM; HOG000226717; -.
DR   KO; K03686; -.
DR   OMA; MNMDDIF; -.
DR   OrthoDB; 1738789at2; -.
DR   BioCyc; CABO218497:G1GI1-342-MONOMER; -.
DR   Proteomes; UP000001012; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10719; DnaJ_zf; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   HAMAP; MF_01152; DnaJ; 1.
DR   InterPro; IPR012724; DnaJ.
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; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR   InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR   InterPro; IPR036869; J_dom_sf.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   SUPFAM; SSF49493; SSF49493; 2.
DR   SUPFAM; SSF57938; SSF57938; 1.
DR   TIGRFAMs; TIGR02349; DnaJ_bact; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51188; ZF_CR; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5L6F7.
DR   SWISS-2DPAGE; Q5L6F7.
KW   Chaperone; Cytoplasm; DNA replication; Metal-binding; Repeat;
KW   Stress response; Zinc; Zinc-finger.
FT   CHAIN           1..391
FT                   /note="Chaperone protein DnaJ"
FT                   /id="PRO_0000070755"
FT   DOMAIN          2..67
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   REPEAT          161..168
FT                   /note="CXXCXGXG motif"
FT   REPEAT          178..185
FT                   /note="CXXCXGXG motif"
FT   REPEAT          200..207
FT                   /note="CXXCXGXG motif"
FT   REPEAT          214..221
FT                   /note="CXXCXGXG motif"
FT   ZN_FING         148..226
FT                   /note="CR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   COMPBIAS        71..131
FT                   /note="Gly-rich"
FT   METAL           161
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   METAL           164
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   METAL           178
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   METAL           181
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   METAL           200
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   METAL           203
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   METAL           214
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   METAL           217
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
SQ   SEQUENCE   391 AA;  42072 MW;  5A90BEE9EE391D99 CRC64;
     MDYYDVLGVS KTASPEEIKK SYRKLAVKYH PDKNPGDAEA EKRFKEVSEA YEVLSDPQKR
     ESYDRYGKDG PFAGAGGFGG AGMSNMEDAL RTFMGAFGGE LGGSGSFFEG LFGGLGEAFG
     MRGDPAGARQ GASKKVHITL TFEEAARGVK KELLVSGYKT CETCSGSGAS SKQGIKCCDR
     CKGSGQVVQS RGFFSMASTC PECGGEGRMI TDPCSSCRGQ GRIKDKRSVH VQIPAGVDSG
     MRLKMEGYGD AGQNGAPAGD LYVFIDVEAH PVFERRGDDL ILELPIGFVD AALGMKKEVP
     TLLKEGACRL TVPEGIQSGT ILKIKNQGFP NVHGRGRGDL LVRVSVETPQ NLSEEQKELL
     RKFAATEKAE NFPKKRSFLD KIKGFFSDLT V
//

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