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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
 
 
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