DNAK_SHELP
ID DNAK_SHELP Reviewed; 637 AA.
AC A3QGW2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=Shew_2844;
OS Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=323850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1088 / PV-4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA Fredrickson J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella loihica PV-4.";
RL Submitted (MAR-2007) 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; CP000606; ABO24710.1; -; Genomic_DNA.
DR RefSeq; WP_011866641.1; NC_009092.1.
DR AlphaFoldDB; A3QGW2; -.
DR SMR; A3QGW2; -.
DR STRING; 323850.Shew_2844; -.
DR PRIDE; A3QGW2; -.
DR EnsemblBacteria; ABO24710; ABO24710; Shew_2844.
DR KEGG; slo:Shew_2844; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001558; 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; 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_1000059663"
FT REGION 602..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; 68636 MW; 29E58838D1FDC189 CRC64;
MGKIIGIDLG TTNSCVAVLD GDKARVIENA EGDRTTPSII AYTGEEVLVG QPAKRQAVTN
PKNTFFAIKR LIGRRFKDDE VQRDVDIMPF KIIAADNGDA WVEAHDKKMA PPQVSAEILK
KMKKTAEDYL GEPVTEAVIT VPAYFNDSQR QATKDAGRIA GLEVKRIINE PTAAALAYGI
DKKQGDNIVA VYDLGGGTFD ISIIEIDSVD GEQTFEVLAT NGDTHLGGED FDNRLINYLA
DEFKKEQSLD LRNDPLAMQR LKEAAEKAKI ELSSTTQTEV NLPYITADAT GPKHLVVKIT
RAKLESLVED LIQRSLEPLK VALADADLSV SDINEVILVG GQTRMPKVRA EVSAFFGKEL
RQDVNPDEAV AIGAAVQAGV LAGDVKDVLL LDVTPLSLGI ETMGSVMTKL IEKNTTIPTK
ASQTFSTADD NQSAVTIHVL QGERKQSSAN KSLGQFNLEG IEPAPRGMPQ IEVAFDIDAD
GILHVSATDK KTGKAQNITI KASSGLSDEE VEAMVRDAEA HADEDAKFEE LVSARNQADG
MVHATKKQIE EAGDALPSED KEKIEAAMAD VDTATKGNDK EAIEKATQAL MEASAKLMEI
AQAKAQAGQG EQAQQSNEAP ADDVVDAEFE EVKDDKK