ID A0A0S3QS52_THET7 Unreviewed; 639 AA.
AC A0A0S3QS52;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:BAT71171.1};
GN ORFNames=TST_0363 {ECO:0000313|EMBL:BAT71171.1};
OS Thermosulfidibacter takaii (strain DSM 17441 / JCM 13301 / NBRC 103674 /
OS ABI70S6).
OC Bacteria; Aquificota; Aquificae; Aquificales.
OX NCBI_TaxID=1298851 {ECO:0000313|EMBL:BAT71171.1, ECO:0000313|Proteomes:UP000063234};
RN [1] {ECO:0000313|Proteomes:UP000063234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17441 / JCM 13301 / NBRC 103674 / ABI70S6
RC {ECO:0000313|Proteomes:UP000063234};
RX PubMed=29420286; DOI=10.1126/science.aao3407;
RA Nunoura T., Chikaraishi Y., Izaki R., Suwa T., Sato T., Harada T., Mori K.,
RA Kato Y., Miyazaki M., Shimamura S., Yanagawa K., Shuto A., Ohkouchi N.,
RA Fujita N., Takaki Y., Atomi H., Takai K.;
RT "A primordial and reversible TCA cycle in a facultatively
RT chemolithoautotrophic thermophile.";
RL Science 359:559-563(2018).
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}.
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DR EMBL; AP013035; BAT71171.1; -; Genomic_DNA.
DR RefSeq; WP_068549093.1; NZ_AP013035.1.
DR AlphaFoldDB; A0A0S3QS52; -.
DR STRING; 1298851.TST_0363; -.
DR KEGG; ttk:TST_0363; -.
DR PATRIC; fig|1298851.3.peg.375; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000063234; 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 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; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000063234};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 603..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 502..529
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 196
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 639 AA; 69232 MW; AAEEA46240AB0C73 CRC64;
MSKVIGIDLG TTNSVVAVME GGQPRVIVNQ EGSRTTPSMV AFTKDGEILV GGPAKRQAVT
NPENTIFSIK RFMGRRYEEV QEEIKMVPYK VVKGPHGDAR VEVMGKVYSP PEISAMILRK
LKEAAEAYLG EKVEKAVITV PAYFNDDQRR ATKDAGRIAG LEVLRLVNEP TAAALAYGLD
KKKGGKIAVY DLGGGTFDIS ILEVGEGVFE VKAVNGDTHL GGDNFDQRII DWLVEEFKKE
TGIDLRNDPM AMQRLKEAAE KAKIELSSVM ETEINLPFIT ADASGPKHLI KKLTRAKFES
LIRDLVEKTI EPCELAMKDA GVTPADIDEV ILVGGSTRIP LVQQIVKEIF GKEPRKDINP
DEAVALGAAV QAGVLTGEVK DILLLDVTPL SLGIETLGGV MTVLIPRNTT IPTRKSEIFT
TAADNQTSVE IHVLQGERPL AKDNRTLARF ILDGIPPAPR GVPKIEVTFD IDANGILHVS
AKDLATGKEQ KVTVTASSGL TEEEIERMVR EAEAHAEEDR RKKEEIELRN QLDGLVYSVE
KTLNENREKI PVSDIKEIEE AIADAKKVLE EKRGIDEIKR AIERVTQASH KIATFMYQQA
QASAGGAGAA GGASGSAGSP GSSTGAEGDV IDADFEEKK
//
