ID A0A1Y4V3C3_9FIRM Unreviewed; 588 AA.
AC A0A1Y4V3C3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Chaperone protein DnaK {ECO:0000256|ARBA:ARBA00014415};
DE AltName: Full=Chaperone protein dnaK {ECO:0000256|ARBA:ARBA00017249};
DE AltName: Full=HSP70 {ECO:0000256|ARBA:ARBA00033103};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000256|ARBA:ARBA00030945};
DE AltName: Full=Heat shock protein 70 {ECO:0000256|ARBA:ARBA00030019};
GN ORFNames=B5E53_13960 {ECO:0000313|EMBL:OUQ64542.1};
OS Eubacterium sp. An11.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1965542 {ECO:0000313|EMBL:OUQ64542.1, ECO:0000313|Proteomes:UP000195664};
RN [1] {ECO:0000313|Proteomes:UP000195664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An11 {ECO:0000313|Proteomes:UP000195664};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000256|ARBA:ARBA00002290}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, 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:OUQ64542.1}.
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DR EMBL; NFLV01000022; OUQ64542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4V3C3; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000195664; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
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; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Stress response {ECO:0000256|ARBA:ARBA00023016}.
SQ SEQUENCE 588 AA; 63708 MW; D094B77D1777BBA4 CRC64;
MSKTIGIDLG TTNSCVAVVE NGQPVIVPNS SGARTTPSVV AFTKKGERLV GDVARRQAAT
NPDRTISSVK REMGTDWSIR IDGKDYKPQT ISAMILMQLK KDAEEFLGEP VTSAVITVPA
YFNDVQRQAT KDAGRIAGLD VKRIINEPTS AALSYGLDHG EAQKVMVYDL GGGTFDVSVI
EIGDDVIEVL ATAGDNHLGG DDFDERIVRW LVAECKNQNH VDPSGDFTAM QRIREAAEQA
KKELSTAQSS SIVLPYLMQA KGTPVHLETT LTRTKFQELI QDLVERTAAP VQQALSDAGI
AASELGRVLL VGGSTRIPAV QEKVRLLTGK EPSRNINPDE CVAMGAAVLG NTLEGNSLAV
AGSDLLLLDV TPMSLSIETV GGVATRLVER NTTLPTKYSR VFSTAAPYQR DVEIHVLQGE
RPMAKDNKTI GKFRLKGIRR APAGVPQIEV TFDIDTNGIL KVSARDLDTG KEQSITITAD
DRMSDAEIEQ AIRDAQQYAG MDNLRKEAIA LTGDAQKVLS QAQRALKNGG KQIERPVKKQ
VKSDINALSK LMGRFRLDRM TEEDMTAIRQ AKENLERSAG NIIAQYGN
//
