ID   G5CBS1_9BACL            Unreviewed;       263 AA.
AC   G5CBS1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   03-MAY-2023, entry version 29.
DE   RecName: Full=Chaperone protein DnaK {ECO:0000256|ARBA:ARBA00014415};
DE   AltName: Full=Chaperone protein dnaK {ECO:0000256|ARBA:ARBA00017249};
DE   AltName: Full=HSP70 {ECO:0000256|ARBA:ARBA00033103};
DE   AltName: Full=Heat shock 70 kDa protein {ECO:0000256|ARBA:ARBA00030945};
DE   AltName: Full=Heat shock protein 70 {ECO:0000256|ARBA:ARBA00030019};
DE   Flags: Fragment;
GN   Name=dnaK {ECO:0000313|EMBL:AEP19962.1};
OS   Exiguobacterium sp. EF3.
OC   Bacteria; Bacillota; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=1088858 {ECO:0000313|EMBL:AEP19962.1};
RN   [1] {ECO:0000313|EMBL:AEP19962.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EF3 {ECO:0000313|EMBL:AEP19962.1};
RA   Moreno-Letelier A., Olmedo G., Souza V.;
RT   "Divergence of Firmicutes form the Cuatro Cienegas Basin, Mexico: a window
RT   to the Precambrian.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000256|ARBA:ARBA00002290}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381}.
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DR   EMBL; JN001858; AEP19962.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5CBS1; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT   COILED          12..39
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEP19962.1"
FT   NON_TER         263
FT                   /evidence="ECO:0000313|EMBL:AEP19962.1"
SQ   SEQUENCE   263 AA;  28058 MW;  0FE3F8400122A3F8 CRC64;
     VSEFKKENGI DLGQDKMALQ RLKDAAEKAK KDLSGVTSAH ISLPFITAGA AGPLHLETTL
     TRAKFDELTA DLVERTMEPT RRALKDSGLT PSDLDKIILV GGSTRIPAVQ KAIHDFTKKE
     PFKGVNPDEV VALGAAIQGG VLAGDVKDVV LLDVTPLSLG IETMGGVMTK LIDRNTTIPT
     SKSQVFSTAA DNQPAVDIHV LQGERPMAPD NKTLGRFQLT DIPPAPRGVP QIEVKFDIDA
     NGIVHVSAKD LGTNKEQSIT IQS
//