ID K9LE66_9BACL Unreviewed; 219 AA.
AC K9LE66;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 03-MAY-2023, entry version 24.
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=hsp70 {ECO:0000313|EMBL:AFI58517.1};
OS Exiguobacterium sp. 2EPA.
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=1009114 {ECO:0000313|EMBL:AFI58517.1};
RN [1] {ECO:0000313|EMBL:AFI58517.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=2EPA {ECO:0000313|EMBL:AFI58517.1};
RA Rebollar E.A., Avitia M., Eguiarte L.E., Mora L., Bonilla-Rosso G.,
RA Souza V.;
RT "Evolutionary history and niche differentiation of Exiguobacterium, a
RT halophilic bacterial genus living at Cuatro Cienegas Basin, Mexico.";
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; JF952214; AFI58517.1; -; Genomic_DNA.
DR AlphaFoldDB; K9LE66; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR Gene3D; 3.30.420.40; -; 2.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Stress response {ECO:0000256|ARBA:ARBA00023016,
KW ECO:0000313|EMBL:AFI58517.1}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFI58517.1"
FT NON_TER 219
FT /evidence="ECO:0000313|EMBL:AFI58517.1"
SQ SEQUENCE 219 AA; 23128 MW; ED9FB7E72928DF3D CRC64;
SGVTSAHISL PFITAGAAGP LHLETTLTRA KFDELTADLV ERTMEPTRRA LKDSGLTPSD
LDKIILVGGS TRIPAVQKAI HDFTKKEPFK GVNPDEVVAL GAAIQGGVLA GDVKDVVLLD
VTPLSLGIET MGGVMTKLID RNTTIPTSKS QVFSTAADNQ PAVDIHVLQG ERPMAPDNKT
LGRFQLTDIP PAPRGVPQIE VKFDIDANGI VHVSAKDLG
//
