DNAK_RUMCH
ID DNAK_RUMCH Reviewed; 616 AA.
AC B8I305;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Ccel_1798;
OS Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS H10) (Clostridium cellulolyticum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminiclostridium.
OX NCBI_TaxID=394503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
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., Saunders E., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Zhou J., Richardson P.;
RT "Complete sequence of Clostridium cellulolyticum H10.";
RL Submitted (JAN-2009) 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; CP001348; ACL76148.1; -; Genomic_DNA.
DR RefSeq; WP_015925263.1; NC_011898.1.
DR AlphaFoldDB; B8I305; -.
DR SMR; B8I305; -.
DR STRING; 394503.Ccel_1798; -.
DR PRIDE; B8I305; -.
DR EnsemblBacteria; ACL76148; ACL76148; Ccel_1798.
DR KEGG; cce:Ccel_1798; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001349; 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; 2.
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..616
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133139"
FT REGION 575..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 616 AA; 66088 MW; 11DBDA9B6E63BCCC CRC64;
MAKVIGIDLG TTNSCVAVME GGEPIVIANP EGNRTTPSVV AFSKTGERMT GQVAKRQAIT
NPERTIISIK RDMGTDHKVD IDGKKFSPQE ISSMILQKLK SDAEAYLGET VTQAVITVPA
YFSDAQRQAT KDSGKIAGLE VLRIINEPTA AALAYGLDKE HDQKIMVYDL GGGTFDVSIL
EIGDGVFEVL ATNGNNKLGG DDFDQRIIDF LVDTFKKESG IDLKNDKMAM QRLKEAAEKA
KVELSGVTSS NINLPFITAD ASGPKHLDVT LTRAKFDEIT ADLVENTMVP TRQAMQDAGL
TPDKIDKILL VGGSTRIPAV QEAVKKYLGK DPFKGINPDE CVAVGAAIQA GVLTGDVTGL
LLLDVTPLSL GLETLGGVFT KLIERNTTIP TKKSQVFSTA ADGQTSVEIH VLQGEREMAQ
YNKSLGRFQL TGIPSAPRGV PQIEVTFDID ANGIVHVSAK DLGTGNEQKI TITASTNLSD
SDIDKAVKEA EKFAAEDKQR KEEIDVRNNA DSLIYQSEKS LKDLGDKVSA DDKSKIESGV
NKVKDALKGT DIEVIKKATE ELQQSFYDIS SKIYQQTQGA QSDPGAAGFG GQQEAPGAGQ
DENVVDADYK VVDDDK