DNAJ2_THET8
ID DNAJ2_THET8 Reviewed; 280 AA.
AC Q56237; P77642; Q5SI85;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Chaperone protein DnaJ 2;
GN Name=dnaJ2; OrderedLocusNames=TTHA1489;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9349721; DOI=10.1016/s0167-4781(97)00071-7;
RA Osipiuk J., Joachimiak A.;
RT "Cloning, sequencing, and expression of dnaK-operon proteins from the
RT thermophilic bacterium Thermus thermophilus.";
RL Biochim. Biophys. Acta 1353:253-265(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Seidel R.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9276481; DOI=10.1016/s0014-5793(97)00847-8;
RA Motohashi K., Yohda M., Odaka M., Yoshida M.;
RT "K+ is an indispensable cofactor for GrpE stimulation of ATPase activity of
RT DnaK/DnaJ complex from Thermus thermophilus.";
RL FEBS Lett. 412:633-636(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=10092456; DOI=10.1006/jmbi.1999.2636;
RA Klostermeier D., Seidel R., Reinstein J.;
RT "The functional cycle and regulation of the Thermus thermophilus DnaK
RT chaperone system.";
RL J. Mol. Biol. 287:511-525(1999).
CC -!- FUNCTION: Does not influence ATP binding or hydrolysis nor ADP release.
CC Exerts influence on the interaction of DnaK with substrates; in the
CC presence of DafA, DnaJ inhibits substrate binding, and substrate
CC already bound to DnaK is displaced by DnaJ and DafA.
CC {ECO:0000269|PubMed:10092456}.
CC -!- SUBUNIT: Forms a heterononamer with DnaJ and DafA in the resting state.
CC Three copies of each protein are present in the complex.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000305}.
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DR EMBL; L57504; AAB04678.1; -; Genomic_DNA.
DR EMBL; Y07826; CAA69161.1; -; Genomic_DNA.
DR EMBL; D84222; BAA12282.1; -; Genomic_DNA.
DR EMBL; AB012390; BAA81743.1; -; Genomic_DNA.
DR EMBL; AB032368; BAA96087.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71312.1; -; Genomic_DNA.
DR RefSeq; WP_011228713.1; NC_006461.1.
DR RefSeq; YP_144755.1; NC_006461.1.
DR PDB; 4J7Z; Other; 1.64 A; A/B/C/D/E/F=2-114.
DR PDB; 4J80; Other; 2.90 A; A/B/C/D=1-280.
DR PDB; 6PPT; NMR; -; A=116-183.
DR PDB; 6PQ2; NMR; -; A=116-183.
DR PDB; 6PQE; NMR; -; A=191-256.
DR PDB; 6PRI; NMR; -; A=192-256.
DR PDB; 6PRJ; NMR; -; A=191-256.
DR PDB; 6PRP; NMR; -; A=190-256.
DR PDB; 6PRQ; NMR; -; A=116-256.
DR PDB; 6PSI; NMR; -; A/C=1-280.
DR PDBsum; 4J7Z; -.
DR PDBsum; 4J80; -.
DR PDBsum; 6PPT; -.
DR PDBsum; 6PQ2; -.
DR PDBsum; 6PQE; -.
DR PDBsum; 6PRI; -.
DR PDBsum; 6PRJ; -.
DR PDBsum; 6PRP; -.
DR PDBsum; 6PRQ; -.
DR PDBsum; 6PSI; -.
DR AlphaFoldDB; Q56237; -.
DR SMR; Q56237; -.
DR STRING; 300852.55772871; -.
DR EnsemblBacteria; BAD71312; BAD71312; BAD71312.
DR GeneID; 3170135; -.
DR KEGG; ttj:TTHA1489; -.
DR PATRIC; fig|300852.9.peg.1464; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_017633_0_0_0; -.
DR OMA; DVNFPET; -.
DR PhylomeDB; Q56237; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; DNA replication; Reference proteome;
KW Stress response.
FT CHAIN 1..280
FT /note="Chaperone protein DnaJ 2"
FT /id="PRO_0000070921"
FT DOMAIN 6..70
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT CONFLICT 129
FT /note="E -> K (in Ref. 1; AAB04678)"
FT /evidence="ECO:0000305"
FT HELIX 7..11
FT /evidence="ECO:0007829|PDB:6PSI"
FT HELIX 19..32
FT /evidence="ECO:0007829|PDB:6PSI"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:6PSI"
FT HELIX 41..58
FT /evidence="ECO:0007829|PDB:6PSI"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:6PSI"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:6PSI"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:6PSI"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:6PSI"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:6PSI"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:6PPT"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:6PPT"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:6PPT"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:6PPT"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:6PPT"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:6PPT"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6PPT"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:6PPT"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:6PRQ"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:6PQE"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:6PQE"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:6PQE"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:6PQE"
FT STRAND 232..242
FT /evidence="ECO:0007829|PDB:6PQE"
FT STRAND 245..256
FT /evidence="ECO:0007829|PDB:6PQE"
FT HELIX 263..277
FT /evidence="ECO:0007829|PDB:6PSI"
SQ SEQUENCE 280 AA; 30978 MW; AE32D959359388D0 CRC64;
MAAKKDYYAI LGVPRNATQE EIKRAYKRLA RQYHPDVNKS PEAEEKFKEI NEAYAVLSDP
EKRRIYDTYG TTEAPPPPPP GGYDFSGFDV EDFSEFFQEL FGPGLFGGFG RRSRKGRDLR
AELPLTLEEA FHGGERVVEV AGRRVSVRIP PGVREGSVIR VPGMGGQGNP PGDLLLVVRL
LPHPVFRLEG QDLYATLDVP APIAVVGGKV RAMTLEGPVE VAVPPRTQAG RKLRLKGKGF
PGPAGRGDLY LEVRITIPER LTPEEEALWK KLAEAYYARA
