ID   DNAK_FINM2              Reviewed;         608 AA.
AC   B0S1F8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=FMG_0780;
OS   Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS   (Peptostreptococcus magnus).
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Finegoldia.
OX   NCBI_TaxID=334413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29328 / DSM 20472 / WAL 2508;
RX   PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA   Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA   Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT   "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT   pathogen.";
RL   DNA Res. 15:39-47(2008).
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; AP008971; BAG08198.1; -; Genomic_DNA.
DR   RefSeq; WP_012290623.1; NC_010376.1.
DR   AlphaFoldDB; B0S1F8; -.
DR   SMR; B0S1F8; -.
DR   STRING; 334413.FMG_0780; -.
DR   PRIDE; B0S1F8; -.
DR   EnsemblBacteria; BAG08198; BAG08198; FMG_0780.
DR   KEGG; fma:FMG_0780; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001319; 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..608
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119706"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   608 AA;  66002 MW;  65DA72DBB3BF262E CRC64;
     MSKVIGIDLG TTNSAVAVME GGESVIVPNS EGNRTTPSIV AFTKDGERLV GETAKRQAIT
     NPDRTITSIK REMGTEYKVN IDGKDYTPEE ISAMILQKLK ADTESYLGEE VTEAVITVPA
     YFTDSQRQAT KNAGKIAGLN VKRIINEPTA AALAYGIDKE TDQHKVMVYD LGGGTFDVSI
     LEVGDGVFEV LATRGNNRLG GDDFDEKLLN YLADEFMKQN GVDLRKDPTS KQRLKDAAEN
     AKKELSTRVS TNVNLPFISA VNGTPVHLNM DITRSKFDEL TSDLVEESLK PVRQALEDAG
     LSHNDIEKVL LVGGSTRIPA VQEAVKKLIG KNPQKDINPD ECVAIGAALQ GGVLTGEVKD
     LLLLDVTPLS LGIETLGGVC TKLIERNTTI PTKKSQVFTT AADGQTSVEI KVLQGEREMA
     ADNTLLGQFN LTEIPAAPRG VPQIEVTFDI DANGIVNVSA KDLGSGKQQA MTITSSTKMS
     DDEIKRKVDE ASKYAEEDKN KKETIETKNS AESVIYQVEK TIKDLGDKVS ETEKSDINSK
     IEALKSILDS GDNKDIKAKT DELTQEMYKL SSKLYENNAQ QPGASQEAKK DDDVVDADYE
     VVDDDENK