DNAK_SHEB9
ID DNAK_SHEB9 Reviewed; 639 AA.
AC A9L0R8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Sbal195_3537;
OS Shewanella baltica (strain OS195).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=399599;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS195;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS195.";
RL Submitted (NOV-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; CP000891; ABX50699.1; -; Genomic_DNA.
DR RefSeq; WP_006082794.1; NC_009997.1.
DR AlphaFoldDB; A9L0R8; -.
DR SMR; A9L0R8; -.
DR EnsemblBacteria; ABX50699; ABX50699; Sbal195_3537.
DR GeneID; 11773577; -.
DR KEGG; sbn:Sbal195_3537; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000000770; 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_1000079244"
FT REGION 602..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; 68974 MW; 9BD078A5B19DED7F 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 LIIRTLEPLK 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 EAIEKATQEL IEASAKLMEI
AQAKSQAQGG DNADAGKQAN ATADDVVDAE FEEVKDDKK