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