ID C0LLA9_9FIRM Unreviewed; 216 AA.
AC C0LLA9; C0LLB0;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 41.
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};
DE Flags: Fragment;
OS Negativicoccus succinicivorans.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Negativicoccus.
OX NCBI_TaxID=620903 {ECO:0000313|EMBL:ACN60070.1};
RN [1] {ECO:0000313|EMBL:ACN60070.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ADV 03/08/05-B-3158 {ECO:0000313|EMBL:ACN60071.1}, and ADV
RC 12/01/04-B-1195 {ECO:0000313|EMBL:ACN60070.1};
RX PubMed=19667386; DOI=10.1099/ijs.0.013102-0;
RA Marchandin H., Teyssier C., Campos J., Jean-Pierre H., Roger F., Gay B.,
RA Carlier J.P., Jumas-Bilak E.;
RT "Negativicoccus succinicivorans gen. nov., sp. nov., isolated from human
RT clinical samples, emended description of the family Veillonellaceae and
RT description of Negativicutes classis nov., Selenomonadales ord. nov. and
RT Acidaminococcaceae fam. nov. in the bacterial phylum Firmicutes.";
RL Int. J. Syst. Evol. Microbiol. 60:1271-1279(2010).
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}.
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DR EMBL; FJ715932; ACN60070.1; -; Genomic_DNA.
DR EMBL; FJ715933; ACN60071.1; -; Genomic_DNA.
DR AlphaFoldDB; C0LLA9; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 3.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
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 PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Stress response {ECO:0000256|ARBA:ARBA00023016,
KW ECO:0000313|EMBL:ACN60070.1}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACN60070.1"
FT NON_TER 216
FT /evidence="ECO:0000313|EMBL:ACN60070.1"
SQ SEQUENCE 216 AA; 23198 MW; 8C3629386ED3312C CRC64;
VIDLGTTNSV VAVMEGGEPV VITNAEGSRL TPSVVGFSKT GERLVGQLAK RQAVSNPDRT
ISSIKRHMGT NYKVNIDDKA YTPQEISAMV LQKLKQDAEA YLGEKVEKAV ITVPAYFTDS
QRQATKDAGA IAGLEVLRII NEPTAAALAY GLDKDEAHTI LVFDLGGGTF DVSILDLAEG
VFEVKATQGN NHLGGDDFDK KVMNWIISEF KKTNGV
//
