DNAK_SYNAS
ID DNAK_SYNAS Reviewed; 637 AA.
AC Q2LUH6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=SYNAS_18590;
GN ORFNames=SYN_01983;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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; CP000252; ABC77738.1; -; Genomic_DNA.
DR RefSeq; WP_011417760.1; NC_007759.1.
DR AlphaFoldDB; Q2LUH6; -.
DR SMR; Q2LUH6; -.
DR STRING; 56780.SYN_01983; -.
DR PRIDE; Q2LUH6; -.
DR EnsemblBacteria; ABC77738; ABC77738; SYN_01983.
DR KEGG; sat:SYN_01983; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_7; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001933; 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..637
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059690"
FT REGION 597..637
FT /note="Disordered"
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 637 AA; 68469 MW; 839E9DBC74587927 CRC64;
MGRIIGIDLG TTNSCVAVME GGDPVVIANQ EGNRTTPSIV AFTESGERLV GQVAKRQAVT
NSENTVYAVK RLIGRKYNSK EVQYDKSISP FKISEAPNGD AQIEVRGRAY SPAEISSMVL
VKMKQTAEDY LGEKITDAVI TVPAYFNDSQ RQATKDAGKI AGLNVLRIIN EPTAAALAYG
LDKKKDEKIA VFDLGGGTFD ISILELGEGV FEVKSTNGDT HLGGEDFDQR IIDYLVSEFK
KDQGIDIRSD KMALQRLKEA AEKAKMELSS SMETDINLPF ITADASGPKH MNIKLTRARM
EALVEELIDR LEGPCRTALK DAGLSPKDID EVILVGGMTR MPRVQQKVKE IFDREPHKGV
NPDEVVAVGA AIQGGVLGGE VKDVLLLDVT PLSLGIETLG GVMTKLIEKN TTIPTRKSQI
FSTAADNQPA VSIHVLQGER SMAGDNRTLG RFDLVGIPPA PRGIPQIEVT FDIDANGIVH
VSAKDLGTGK EQSIKITASS GLSETEIEKL VREAESHGEE DRKKKELVEA RNSADAMAYG
VEKNIKEFGD KVDAAEKARI EDAIAKVRKA VEGDDINAIR SAQDELTTAS HKLAEAMYAK
TSQAGAGPQP GAGPGTGGQG PGKKDEDVVD ADFEEVK