DNAK_SHEB2
ID DNAK_SHEB2 Reviewed; 639 AA.
AC B8E4S1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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};
GN OrderedLocusNames=Sbal223_1042;
OS Shewanella baltica (strain OS223).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=407976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS223;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K.,
RA Tiedje J.;
RT "Complete sequence of chromosome of Shewanella baltica OS223.";
RL Submitted (DEC-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; CP001252; ACK45557.1; -; Genomic_DNA.
DR RefSeq; WP_012586981.1; NC_011663.1.
DR AlphaFoldDB; B8E4S1; -.
DR SMR; B8E4S1; -.
DR EnsemblBacteria; ACK45557; ACK45557; Sbal223_1042.
DR KEGG; sbp:Sbal223_1042; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000002507; 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 Stress response.
FT CHAIN 1..639
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133159"
FT REGION 604..639
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 639 AA; 68929 MW; 2A9F77D905F819EF CRC64;
MGKIIGIDLG TTNSCVAVLD GGKARVLENA EGDRTTPSII AYTDDETIVG SPAKRQAVTN
PTNTFFAIKR LIGRRFKDDE VQRDVNIMPF KIIAADNGDA WVESRGNKMA PPQVSAEILK
KMKKTAEDFL GEEVTEAVIT VPAYFNDSQR QATKDAGRIA GLDVKRIINE PTAAALAYGI
DKKQGDNIVA VYDLGGGTFD ISIIEIDSND GDQTFEVLAT NGDTHLGGED FDNRLINYLA
DEFKKEQGLD LRKDPLAMQR LKEAAEKAKI ELSSTNHTEV NLPYITADAT GPKHLVIKIT
RAKLESLVED LILRTLEPLK VALADADLSV TDINEVILVG GQTRMPKVQE AVTNFFGKEP
RKDVNPDEAV AVGAAIQAGV LSGDVKDVLL LDVTPLSLGI ETMGSVMTKL IEKNTTIPTK
AQQVFSTADD NQSAVTIHVL QGERKQASAN KSLGQFNLDG IEPAQRGQPQ IEVMFDIDAD
GILHVSATDK KTGKKQNITI KASSGLSEEE VAQMVRDAEA HADEDKKFEE LVQSRNQADG
LVHATKKQVE EAGDALPSED KEKIQAAMDA VDTAIKGNDK EAIEKATQNL IEASAKLMEI
AQAKSQAQGG DNADAGKQAN AAADDVVDAE FEEVKDDKK