ID A0A0D8FY77_9ACTN Unreviewed; 618 AA.
AC A0A0D8FY77;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Chaperone protein DnaK {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000256|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000256|HAMAP-Rule:MF_00332,
GN ECO:0000313|EMBL:KJE77222.1};
GN ORFNames=FEAC_09340 {ECO:0000313|EMBL:KJE77222.1};
OS Ferrimicrobium acidiphilum DSM 19497.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Ferrimicrobium.
OX NCBI_TaxID=1121877 {ECO:0000313|EMBL:KJE77222.1, ECO:0000313|Proteomes:UP000032336};
RN [1] {ECO:0000313|EMBL:KJE77222.1, ECO:0000313|Proteomes:UP000032336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T23 {ECO:0000313|EMBL:KJE77222.1,
RC ECO:0000313|Proteomes:UP000032336};
RA Poehlein A., Eisen S., Schloemann M., Johnson B.D., Daniel R., Muehling M.;
RT "Draft genome of the acidophilic iron oxidizer Ferrimicrobium acidiphilum
RT strain T23.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000256|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000256|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|HAMAP-Rule:MF_00332,
CC ECO:0000256|RuleBase:RU003322}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJE77222.1}.
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DR EMBL; JXUW01000006; KJE77222.1; -; Genomic_DNA.
DR RefSeq; WP_035392517.1; NZ_KN050778.1.
DR AlphaFoldDB; A0A0D8FY77; -.
DR STRING; 1121877.FEAC_09340; -.
DR GeneID; 78372204; -.
DR PATRIC; fig|1121877.4.peg.1002; -.
DR eggNOG; COG0443; Bacteria.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000032336; Unassembled WGS sequence.
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 CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
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 NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 2.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00332}; Chaperone {ECO:0000256|HAMAP-Rule:MF_00332};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00332};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_00332}; Reference proteome {ECO:0000313|Proteomes:UP000032336};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 574..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 618 AA; 66311 MW; 4BDC99A657BE4C4B CRC64;
MAKAVGIDLG TTNSVVSVLE GGDPTVIPNS EGGRTTPSIV AFSKTGEVLV GEVAKRQAIT
NPDRTIRSVK RHMGTDWTID IDGKKYTPQE ISSRILSKLK RDAEAYLGDT VNQAVITVPA
YFDDAQRTAT KEAGQIAGLE VLRIINEPTA AALAYGLDKE TEDQTVLVFD LGGGTFDVSV
LEIGDGVFEV KSTAGNTQLG GDDWDQRVID WMIKSFKDNE GVDLGADKMA MQRLKESAEK
AKIELSASLE TTINIPFISA TSEGPKHLEM KLTRSRFQEL TADLVQACKG PFEQAIKDAG
LTVGKVDHVV LVGGSTRMPA IQDLVQQMTG KEPHRGVNPD EVVAVGAAIQ AGVLKGEVKD
VLLLDVTPLS LGIETKGGVM TKLIERNTTI PTKRTEVFTT ADDNQPSVEI HVLQGERDMA
SYNKTLGRFQ LVGIPPAPRG IPQIEVTFDI DANGIVHVSA KDRATNKEQS ITITGTTSLS
KEEIDQMMRD AEAHVAEDKQ RKEEAEVRNN ADTLVYQTEK LLTEQGDKLE GPERDKVTEA
LNEVKHSLDG TDIAAIKSAT DALMSASQGF TQRLYEEASR QASASGAADG TAGPSASDGD
AGGDDEVVDA EIVDEPKE
//
