DNAK1_PROMM
ID DNAK1_PROMM Reviewed; 664 AA.
AC Q7V7N7;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Chaperone protein dnaK1;
DE AltName: Full=HSP70-1;
DE AltName: Full=Heat shock 70 kDa protein 1;
DE AltName: Full=Heat shock protein 70-1;
GN Name=dnaK1; OrderedLocusNames=PMT_0703;
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; BX548175; CAE20878.1; -; Genomic_DNA.
DR RefSeq; WP_011130081.1; NC_005071.1.
DR AlphaFoldDB; Q7V7N7; -.
DR SMR; Q7V7N7; -.
DR STRING; 74547.PMT_0703; -.
DR EnsemblBacteria; CAE20878; CAE20878; PMT_0703.
DR KEGG; pmt:PMT_0703; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_3; -.
DR OMA; PCQSVNP; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001423; Chromosome.
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; 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; 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 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; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..664
FT /note="Chaperone protein dnaK1"
FT /id="PRO_0000078514"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 664 AA; 72549 MW; 44AA513800D91603 CRC64;
MGRIVGIDLG TTNSVVAVLE AGRPQVIANA EGSRTTPSVV GYSKEAELLV GQLARRQLVL
NPRNTFANLK RFVGRGWDEM DDSSLSVPYT VRANEQGNVR VSCQVTEREY APEELVASII
RKLVDDAATY LGEPVEAAVV TVPAYFNDAQ RQATRDAGRL AGITVERILN EPTAAALAYG
FDRSAARRVL VFDLGGGTFD VSLMRVANGV FDVKATCGDT QLGGNDFDQR IVDWLAEAFK
TKHGLDLRRD RQALQRLIEA AEKAKQELSG VLSTPISLPF IATGPDGPLH IETSLDRPTF
EGLCPDLLDR LLNPVQTALR DSGWSADDVD DVVLVGGGTR MPMVQQLLRT LVASEPCQSV
NPDEVVAVGG AVQAGILTGE LRDLMLNDVT PLSLGLETVG GLMKVLIPRN TPIPVRQSDV
FSTSEANQSS VEIHVWQGER QLAADNKSLG RFRLSGIPPA PRGVPQVQVA FDIDANGLLQ
VSATDRTTGR KQSVNIQGGS TLNEEELQAL LAEAEAKAGE DRRRRASIDR RNSALTLVGQ
AERRLRDAAL ELGPYGAERQ QRAVETAMRD VQDLLEQNDL QELELAVASL QEALFGLNRR
ISSERRTDAN PLQGIRNTLG SLKDELFSDD DWDEDPWNSP ARSSDGRRIY RGRELNPWDD
DFYR