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Database: UniProt
Entry: R7H7Y0_9FIRM
LinkDB: R7H7Y0_9FIRM
Original site: R7H7Y0_9FIRM 
ID   R7H7Y0_9FIRM            Unreviewed;       584 AA.
AC   R7H7Y0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Chaperone protein DnaK {ECO:0000256|ARBA:ARBA00014415, ECO:0000256|HAMAP-Rule:MF_00332};
DE   AltName: Full=HSP70 {ECO:0000256|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein {ECO:0000256|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 {ECO:0000256|HAMAP-Rule:MF_00332};
GN   Name=dnaK {ECO:0000256|HAMAP-Rule:MF_00332};
GN   ORFNames=BN634_02353 {ECO:0000313|EMBL:CDE35500.1};
OS   Eubacterium sp. CAG:38.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1262889 {ECO:0000313|EMBL:CDE35500.1, ECO:0000313|Proteomes:UP000017954};
RN   [1] {ECO:0000313|EMBL:CDE35500.1, ECO:0000313|Proteomes:UP000017954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:38 {ECO:0000313|Proteomes:UP000017954};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000256|ARBA:ARBA00002290,
CC       ECO:0000256|HAMAP-Rule:MF_00332}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000256|HAMAP-
CC       Rule:MF_00332}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|HAMAP-Rule:MF_00332,
CC       ECO:0000256|RuleBase:RU003322}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDE35500.1}.
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DR   EMBL; CBIU010000022; CDE35500.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7H7Y0; -.
DR   STRING; 1262889.BN634_02353; -.
DR   Proteomes; UP000017954; Unassembled WGS sequence.
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   CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 2.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00332};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00332};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00332};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW   Rule:MF_00332}; Reference proteome {ECO:0000313|Proteomes:UP000017954};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   COILED          225..252
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         176
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   584 AA;  63803 MW;  C281804E90D06D9C CRC64;
     MVMSRVIGID LGTTNSCVAV LEGDVPTVIA NKEGYRTTPS VVAFAKDKTM LVGDPARRQA
     AVNAERTIFS IKRHMGSDYR KKIDGKAYSP QEISAFILMK LKKDAEDFLG DTVTDAVITV
     PAYFNDAQRQ ATKDAGRIAG LNVLRIINEP TSAALAYGLD NGQAQKILVY DLGGGTFDVS
     IIEIGDHVIE VLATSGDNHL GGDDFDERIV QYLVEQFKKT EGINLSKDTA ALQRLKEEAE
     KAKKELSSCM TTNINLPFLA MAKDGPHHMD IQLSRSKFEE LTKDLIERTV IPVENAIHDA
     GLTKSQIDMV LLVGGSTRIP AVQDKVRTLM GKEPSRNVNP DECVAIGAAV QAGKLGGQLM
     AGSAASEMIL MDVTPLSLSI ETVGGVSSRL IERNTTIPTR HSQIFTTAGN FQTSVDIKVF
     QGERKFTRDN KLLGNFRLSG IKRAMAGTPQ IEVTFDIDAN GIVNVSAKDL GTGHEQSITI
     TSSSNLSEEE IERAKWEAQM YGRQDEAKTQ LLAVRQEAVQ FAGQAQAELD SHKKEWERSK
     KKAVKEILGK LKRTLYKVPP EKITADSAAV IRDLQEELQR ALNS
//
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