ID C0DB58_9FIRM Unreviewed; 569 AA.
AC C0DB58;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=CLOSTASPAR_06513 {ECO:0000313|EMBL:EEG51473.1};
OS [Clostridium] asparagiforme DSM 15981.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Enterocloster.
OX NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG51473.1, ECO:0000313|Proteomes:UP000004756};
RN [1] {ECO:0000313|EMBL:EEG51473.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG51473.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG51473.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG51473.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium asparagiforme (DSM 15981).";
RL Submitted (FEB-2009) 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:EEG51473.1}.
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DR EMBL; ACCJ01000545; EEG51473.1; -; Genomic_DNA.
DR AlphaFoldDB; C0DB58; -.
DR HOGENOM; CLU_005965_2_4_9; -.
DR Proteomes; UP000004756; 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 CDD; cd10235; HscC_like_NBD; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR042030; HscC_NBD.
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.
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 569 AA; 62503 MW; 55C7E3F1C1F18BCC CRC64;
MGGVGMAVIG IDLGTTNSLA CVWRDGKPEL VPNSLGEYLT PSAVYADEQQ VLWTGAVARE
HMCIRPERCA ASFKRHMGTD KRIFLGSMGF TPQELSSMVL KQLKEDAEQY LGCEVEEAVI
SVPAYFNDEQ RFATKEAGEM AGLRVERLVN EPSAAALACR SESGEEDSSF LVVDLGGGTL
DVSVVECFEQ VIEIQAVAGD NHLGGDDFDH RIAEHFCREH GLVFELLSPG DQAELLKKAE
QCKRALTASS AGMIEFSGDK GTMGMFLTGA QFTELSAPLL VRLEKVLRQA LKDAGKTMGD
IDQVVLVGGS CKMPLVRQFI AKILEREPYL CGRPDEIVAL GAGIYAGIKS RQAEIRDVIL
TDICPFTLGV GIVDYDNPDD LIMSSVIERN SVLPVSRMRE YVTTADNQRK VAFRVFQGES
IHCSQNQYMG TVELEVPPAP KGREAALVRL TYDINGILEV EAMNRLGQRA GKVIMSRKVR
MSEEELKRRT AELEAIKRSP REEAANQLVI SRAERLYAEV LGNDREVISQ LLRWFSQILG
EGGPAAVAAA QKKAMETLDY IERKLNGDV
//
