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DNAK_CYAPA
ID   DNAK_CYAPA              Reviewed;         618 AA.
AC   Q37106;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 93.
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-A;
GN   and
GN   Name=dnaK-B;
OS   Cyanophora paradoxa.
OG   Plastid; Cyanelle.
OC   Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora.
OX   NCBI_TaxID=2762;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RA   Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J.,
RA   Bryant D.A.;
RT   "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa.";
RL   Plant Mol. Biol. Rep. 13:327-332(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RA   Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M.,
RA   Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M.,
RA   Jakowitsch J., Bohnert H.J., Bryant D.A.;
RT   "The complete sequence of the cyanelle genome of Cyanophora paradoxa: the
RT   genetic complexity of a primitive plastid.";
RL   (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W.
RL   (eds.);
RL   Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, cyanelle.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA81171.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAA81295.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U30821; AAA81171.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U30821; AAA81295.1; ALT_INIT; Genomic_DNA.
DR   PIR; T06828; T06828.
DR   RefSeq; NP_043140.2; NC_001675.1.
DR   RefSeq; NP_043264.2; NC_001675.1.
DR   AlphaFoldDB; Q37106; -.
DR   SMR; Q37106; -.
DR   GeneID; 801616; -.
DR   GeneID; 801637; -.
DR   GO; GO:0009842; C:cyanelle; 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; Cyanelle; Nucleotide-binding; Plastid;
KW   Stress response.
FT   CHAIN           1..618
FT                   /note="Chaperone protein dnaK"
FT                   /id="PRO_0000078604"
FT   REGION          595..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..618
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  67418 MW;  9EA7373E802C2CA6 CRC64;
     MGKIVGIDLG TTNSVVAVME GGKPTVITNA EGFRTTPSVV AYTKTGDRLV GQIAKRQAVL
     NPGNTFYSVK RFIGRKFDEV TEEAKQVPYK VTGTQNVRIE CPALQTSFTP EEISAQVLRK
     LAEDASKYIG EPVTQAVITV PAYFNDSQRQ ATKDAGKIAG LEVLRIINEP TAASLAYGLD
     KKKNETILVF DLGGGTFDVS ILEVGDGVFE VLSTSGDTHL GGDDFDKKLV DFFIEEFQKL
     ENINLREDQQ ALQRLTEAAE KAKIELSSVT QTEITLPFLS LTPSGPKHFD TTLNRAKFEE
     LCSTLIDRCR IPVETALKDA KLTKEDIDEV VLVGGSTRIP AVRELVQKVL DKVPKQSVNP
     DEVVAVGAAV QAGVLAGEVK DIVLLDVTPL SLGVETLGGV MSKIIVRNTT IPTQKSELFS
     TATDGQTNVE IHVLQGERGF AKDNKSLGTF RLDGIAPAPR GVPQIEVTFD IDANGILSVT
     AKDKGTGKEK SITITGASTL SQDEVERMVQ EAEKNAAQDK ENRQKIELRN QAESLINQAE
     RQLKEFKLEP NVQAPIEQTI QQLQTALKED NLEQVQSLCQ ELQNSLLEIG KQVYSKTETT
     TPNKNEEDVI DASFSEEK
 
 
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