DNAK_MAGSA
ID DNAK_MAGSA Reviewed; 642 AA.
AC Q2VYT1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=amb4440;
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
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; AP007255; BAE53244.1; -; Genomic_DNA.
DR RefSeq; WP_011386784.1; NC_007626.1.
DR AlphaFoldDB; Q2VYT1; -.
DR SMR; Q2VYT1; -.
DR STRING; 342108.amb4440; -.
DR PRIDE; Q2VYT1; -.
DR EnsemblBacteria; BAE53244; BAE53244; amb4440.
DR KEGG; mag:amb4440; -.
DR HOGENOM; CLU_005965_2_3_5; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000007058; 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 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 Reference proteome; Stress response.
FT CHAIN 1..642
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059595"
FT REGION 602..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 642 AA; 68713 MW; 007CE5C7B93B1566 CRC64;
MSKVIGIDLG TTNSCVAVME GKNAKVIENA EGMRTTPSMT AFTESGERLV GQPAKRQAVT
NPTSTLFAIK RLIGRRFEDP ITKKDMNLVP YHIVAGDNGD AWVEARDAKY SPSQVSAFIL
QKMKETAEGY LGEKVTQAVI TVPAYFNDAQ RQATKDAGRI AGLEVLRIIN EPTAAALAYG
LEKKGAGTIA VYDLGGGTFD VSVLEIGDGV FEVKSTNGDT FLGGEDFDAR IMDYLADEFK
KEQGIDLRKD RLALQRLKEA AEKAKIELSS SMQTEVNLPF ITADASGPKH LNIKLTRSKL
EALVEDLVAR TVEPCKAALK DAGVKASEID EVILVGGMTR MPKIQEVVKE FFGREPHKGV
NPDEVVAIGA AIQGGVLKGE VKDVLLLDVT PLSLGIETLG GVFTRLIDRN TTIPTRKSQV
FSTAEDNQTA VTIRVFQGER EMAADNKVLG QFDLVGIPPA PRGVPQVEVT FDIDANGLVN
VSAKDKATGK EQQIRIQASG GLSDADIEKM VKEAEAHAAE DKKRKELIEA RNHADGLIHT
TEKSLKEFGD KAGAELTGAI EKEITALKAV MDGDDVEAIK AKTESLMQAS MKLGEAMYKA
QEAAGGAEAE AAAGGHGGAS GSHDDKVVDA DFEEVDGDKK GK