ID   DNAK_GRATL              Reviewed;         621 AA.
AC   Q6B8V2;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Chaperone protein dnaK;
DE   AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN   Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=Grc000102;
OS   Gracilaria tenuistipitata var. liui (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC   Gracilariaceae; Agarophyton; Agarophyton tenuistipitatum.
OX   NCBI_TaxID=285951;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15638458; DOI=10.1007/s00239-004-2638-3;
RA   Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C.;
RT   "Comparative analysis of the complete plastid genome sequence of the red
RT   alga Gracilaria tenuistipitata var. liui provides insights into the
RT   evolution of rhodoplasts and their relationship to other plastids.";
RL   J. Mol. Evol. 59:464-477(2004).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR   EMBL; AY673996; AAT79683.1; -; Genomic_DNA.
DR   RefSeq; YP_063608.1; NC_006137.1.
DR   AlphaFoldDB; Q6B8V2; -.
DR   SMR; Q6B8V2; -.
DR   GeneID; 2944038; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   HAMAP; MF_00332; DnaK; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR012725; Chaperone_DnaK.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Chloroplast; Nucleotide-binding; Plastid.
FT   CHAIN           1..621
FT                   /note="Chaperone protein dnaK"
FT                   /id="PRO_0000078607"
FT   REGION          597..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..612
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  68081 MW;  CBF26C717EB665A6 CRC64;
     MAKVVGIDLG TTNSVIAVME GGKPTVIPNK EGLRTTPSVV AYTKKQDKLV GQIAKRQAVM
     NPENTFYSVK RFIGRKKDEL GDELKQSSYN VKTDINSNVK LECPALSKDF APEEISAQVL
     RKLVEDASTY LGQQVTQAVI TVPAYFNDSQ RQATKDAGQI AGLDVLRIIN EPTAASLSYG
     LDKKNNETIL VFDLGGGTFD VSILEVGDGV FEVLSTSGDT HLGGDDFDRK IVEWLIHEFS
     HDEGINLGKD RQALQRLTEA AEKAKMELSS LAQTDINLPF ITSTDTGPKH LEKNITRAKF
     EYLCQDLINR CEIPVNNALK DAQLSSGNID EIVLVGGSTR IPAIQQLVKK MIGKDPNQSV
     NPDEVVAIGA AVQAGVLAGE VKDILLLDVT PLSLGVETLG GVMTKIIDRN TTVPTKKSEI
     FSTAVDNQPN VEIHVLQGER EFTKDNKSLG TFRLDGIMPA PRGVPQIEVI FDIDANGILS
     VKAKDKGTGK EQSITITGAS TLPKEEVEKL VKEAEENSEL DKHKREQIDL KNQADALCYQ
     SQNQINELKD KISEDEKQNV QKLIDSLKLS IQEDDYEKIK DIQNQLQQVM MNIGKQVYSS
     TQQDNSKTED GSVIDTNSKE A