DNAK_ACIF5
ID DNAK_ACIF5 Reviewed; 634 AA.
AC B5ENA3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=Lferr_2291;
OS Acidithiobacillus ferrooxidans (strain ATCC 53993 / BNL-5-31)
OS (Leptospirillum ferrooxidans (ATCC 53993)).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=380394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53993 / BNL-5-31;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA Borole A.P.;
RT "Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR EMBL; CP001132; ACH84492.1; -; Genomic_DNA.
DR RefSeq; WP_009563301.1; NC_011206.1.
DR AlphaFoldDB; B5ENA3; -.
DR SMR; B5ENA3; -.
DR PRIDE; B5ENA3; -.
DR GeneID; 66433623; -.
DR KEGG; afe:Lferr_2291; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
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; 1.20.1270.10; -; 1.
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; IPR029048; HSP70_C_sf.
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; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02350; prok_dnaK; 1.
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 Stress response.
FT CHAIN 1..634
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119657"
FT REGION 601..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 634 AA; 68222 MW; 888BB47971ADD4C9 CRC64;
MAKVIGIDLG TTNSCVAVME GDKVKVIENS EGKRTTPSIV AITEEGEVLV GEAAKRQAVT
NPENTVYEVK RLIGRKFDDA EVQKDLKHVP YKVIKADNGD AWVEVRDKKY SAQQISAFIL
QKMKKTAEDY LGEKVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
EDKKPGDSKI AVYDLGGGTF DISIIEIAEM EGEHQFEVLS TNGDTFLGGG DFDSRVINYL
ADSFKAESGI DLRGDRLAMQ RLKEAAEKAK IELSSAQQTD VNLPFITADQ SGPKHLNMKL
TRAKLESLVE DLIDRSMAPC RVAMKDANLA TSRITDVILV GGQSRMPKVQ EKVKDFFGQD
PRKDVNPDEA VAIGAAIQGA VLSGEKKDVL LMDVTPLSLG IETLGGVMTK LIEKNTTIPT
RKSQIFSTAE DNQSAVTVHV LQGERELARD NKSLARFDLT DIANAPRGMP QIEVTFDIDA
NGILHVSAKD NQTGKEQSIK ITASSGLSEE EIKRMIQEAE AHAADDKKAR ALIEARNEAD
ASVHGARKAV EEHAAAPEHD KTKVTEAISA VENAAKGEDV EAIKGAVATL MAAMSALLQS
AAAGQAQAES GAGAQGNAKP DDVVDAEFEE VDKK