DNAK_SHESA
ID DNAK_SHESA Reviewed; 639 AA.
AC A0KTS5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Shewana3_0959;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
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 Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) 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; CP000469; ABK47194.1; -; Genomic_DNA.
DR RefSeq; WP_011716085.1; NC_008577.1.
DR AlphaFoldDB; A0KTS5; -.
DR SMR; A0KTS5; -.
DR STRING; 94122.Shewana3_0959; -.
DR PRIDE; A0KTS5; -.
DR EnsemblBacteria; ABK47194; ABK47194; Shewana3_0959.
DR KEGG; shn:Shewana3_0959; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002589; 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_1000059665"
FT REGION 603..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..619
FT /note="Polar 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 639 AA; 68876 MW; 67209BB6D8041C64 CRC64;
MGKIIGIDLG TTNSCVAVLD GGKARVLENA EGDRTTPSII AYTDDETIVG QPAKRQAVTN
PNNTFFAIKR LIGRRFKDDE VQRDVNIMPF KIIAADNGDA WVESRGNKMA PPQVSAEILK
KMKKTAEDFL GEEVTEAVIT VPAYFNDSQR QATKDAGRIA GLEVKRIINE PTAAALAYGI
DKKQGDNIVA VYDLGGGTFD ISIIEIDSND GDQTFEVLAT NGDTHLGGED FDNRLINYLA
DEFKKEQGLD LRKDPLAMQR LKEAAEKAKI ELSSTNQTEV NLPYITADAT GPKHLVVKIT
RAKLESLVED LIIRTLEPLK VALADADLSV SDINEVILVG GQTRMPKVQE AVSNFFGKEP
RKDVNPDEAV AVGAAIQAGV LSGDVKDVLL LDVTPLSLGI ETMGSVMTKL IEKNTTIPTK
AQQVFSTADD NQSAVTIHVL QGERKQASAN KSLGQFNLDG IEPAPRGMPQ IEVMFDIDAD
GILHVSATDK KTGKKQNITI KASSGLSEEE VAQMVRDAEA HAEEDKKFEE LVQSRNQADG
LVHATKKQVE EAGDALPADD KAKIEAAMSA VEVATKGNDK EAIEKATQEL IEASAKLMEI
AQAKAQTQGG AQEGAAKQSN ATADDVVDAE FEEVKDDKK