ID   DNAK_PORUM              Reviewed;         620 AA.
AC   P69377; P30723;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 61.
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;
OS   Porphyra umbilicalis (Purple laver) (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX   NCBI_TaxID=2786;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Avonport;
RX   PubMed=1720741; DOI=10.1016/0014-5793(91)81355-c;
RA   Reith M., Munholland J.;
RT   "An hsp70 homolog is encoded on the plastid genome of the red alga,
RT   Porphyra umbilicalis.";
RL   FEBS Lett. 294:116-120(1991).
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; X62240; CAA44160.1; -; Genomic_DNA.
DR   PIR; S19660; S19660.
DR   AlphaFoldDB; P69377; -.
DR   SMR; P69377; -.
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; 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;
KW   Stress response.
FT   CHAIN           1..620
FT                   /note="Chaperone protein dnaK"
FT                   /id="PRO_0000078612"
FT   REGION          592..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..612
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   620 AA;  67619 MW;  C9FB4713C142FECF CRC64;
     MGKVVGIDLG TTNSVIAVME GGKPTVIPNA EGFRTTASVV AYTKSGDKLV GQIARQAVIN
     PENTFYSVKR FIGRKQNEIS QEIRQTSYNV KTSGSSIKIE CPALNKDFAP EEISAQVLRK
     LVEDASTYLG ETVTQAVITV PAYFNDSQRQ ATKDAGKIAG LDVLRIINEP TAASLSYGLD
     KQNNETILVF DLGGGTFDVS ILEVGDGVFE VLSTSGDTHL GGDDFDQQIV EWLIKDFKQS
     EGIDLGKDRQ ALQRLTEASE KAKIELSNLT QTEINLPFIT ATQDGPKHLE KTVTRAKFEE
     LCSRLIDKCS IPVNNALKDA KLEASSIDEV VLVGGSTRIP AIQQMVKRLI GKDPNQSVNP
     DEVVAIGAAV QAGVLAGEVK DILLLDVTPL SLGVETLGGV MTKIIPRNTT IPTKKSEVFS
     TAVDNQPNVE IQVLQGEREL TKDNKSLGTF RLDGIMPAPR GVPQIEVTFD IDANGILSVK
     AKEKATGKEQ SITISGASTL PKDDVERMVK EAEENFDVDQ KRRKNIDIRN QAESLCYQSE
     KQVKEFEDKI DEELKNRITN LISELRSNLE KEELDSIEAN SEKLQNALME IGKNATSAEK
     DTQNASNDDT VIDTDFSEAK