DNAK_GUITH
ID DNAK_GUITH Reviewed; 627 AA.
AC P29215; O78509;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Chaperone protein dnaK;
DE AltName: Full=HSP70;
DE AltName: Full=Heat shock 70 kDa protein;
DE AltName: Full=Heat shock protein 70;
GN Name=dnaK; Synonyms=ctp70;
OS Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG Plastid; Chloroplast.
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX NCBI_TaxID=55529;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1961745; DOI=10.1073/pnas.88.23.10783;
RA Wang S., Liu X.-Q.;
RT "The plastid genome of Cryptomonas phi encodes an hsp70-like protein, a
RT histone-like protein, and an acyl carrier protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10783-10787(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9929392; DOI=10.1007/pl00006462;
RA Douglas S.E., Penny S.L.;
RT "The plastid genome of the cryptophyte alga, Guillardia theta: complete
RT sequence and conserved synteny groups confirm its common ancestry with red
RT algae.";
RL J. Mol. Evol. 48:236-244(1999).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AF041468; AAC35702.1; -; Genomic_DNA.
DR PIR; A41609; A41609.
DR RefSeq; NP_050768.1; NC_000926.1.
DR AlphaFoldDB; P29215; -.
DR SMR; P29215; -.
DR GeneID; 857076; -.
DR HOGENOM; CLU_005965_2_4_1; -.
DR OMA; KRQGVVN; -.
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..627
FT /note="Chaperone protein dnaK"
FT /id="PRO_0000078608"
FT REGION 597..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 551
FT /note="K -> L (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="L -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="E -> Q (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 627 AA; 68466 MW; 18121DDCBFF7033C CRC64;
MGKVVGIDLG TTNSVVAVME GGKPAVIQNA EGFRTTPSVV AYTKTGDRLV GQIAKRQAVI
NPDNTFYSVK RFIGRRSEEV SEELKQVSYI VKTDSNGNIK LDCPSLKKEF ASEEISAEVL
RKLVDDASKY LGESVKQAVI TVPAYFNDSQ RQATKDAGRI AGLEVLRIIN EPTAASLAYG
LDKKNNETIL VFDLGGGTFD VSVLEVGDGV FEVLSTSGDT HLGGDDFDDK IVQWLLKEFE
TEHSINLKSD RQALQRLTEA SEKAKIELSN LSQTEINLPF LTATETGPKH LERSITRAKF
EELCSDLINR VKIPVENALK DAKLDSSKID EVVLVGGSTR IPAIQELVKR ILNKTPNQTV
NPDEVVAIGA AVQAGVLAGE VKDILLLDVT PLSLGVETLG GVTTRIIPRN TTIPTKKSEV
FSTAVDNQPN VEIHVLQGER EFAKDNKSLG TFRLDGILPA PRGVPQIEVT FDIDANGILS
VTAKDKGTGK EQSITITGAS TLPSDEVERM VNEAQNSAKE DKEKRDKIDL KNQSDSLCYQ
SEKQLKELEG KIDDTNKNKI SSMISELRNA INNENYDEMR DLNSKLQTAL MDLGKSVYEK
TSKEQTSTSS PTNSNDSVID ADFSETK