DNAK_CLOPA
ID DNAK_CLOPA Reviewed; 20 AA.
AC P81341;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Chaperone protein DnaK;
DE AltName: Full=CP 2;
DE AltName: Full=HSP70;
DE AltName: Full=Heat shock 70 kDa protein;
DE AltName: Full=Heat shock protein 70;
DE Flags: Fragment;
GN Name=dnaK;
OS Clostridium pasteurianum.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1501;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5;
RX PubMed=9629918; DOI=10.1002/elps.1150190533;
RA Flengsrud R., Skjeldal L.;
RT "Two-dimensional gel electrophoresis separation and N-terminal sequence
RT analysis of proteins from Clostridium pasteurianum W5.";
RL Electrophoresis 19:802-806(1998).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
DR PROSITE; PS00297; HSP70_1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Direct protein sequencing; Nucleotide-binding;
KW Stress response.
FT CHAIN 1..>20
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078449"
FT NON_TER 20
SQ SEQUENCE 20 AA; 2002 MW; 2E2E68F21E7AD48F CRC64;
SKVIGIDLGT TNSXVAVMEG