ID W6SKN0_9CLOT Unreviewed; 564 AA.
AC W6SKN0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=CM240_3348 {ECO:0000313|EMBL:CDM70465.1};
OS Clostridium bornimense.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1216932 {ECO:0000313|EMBL:CDM70465.1, ECO:0000313|Proteomes:UP000019426};
RN [1] {ECO:0000313|EMBL:CDM70465.1, ECO:0000313|Proteomes:UP000019426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M2/40 {ECO:0000313|Proteomes:UP000019426};
RA Wibberg D., Puehler A., Schlueter A.;
RT "Complete genome sequence of Clostridum sp. M2/40.";
RL Submitted (NOV-2013) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG917869; CDM70465.1; -; Genomic_DNA.
DR RefSeq; WP_044040639.1; NZ_HG917869.1.
DR AlphaFoldDB; W6SKN0; -.
DR STRING; 1216932.CM240_3348; -.
DR KEGG; clt:CM240_3348; -.
DR PATRIC; fig|1216932.3.peg.3322; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000019426; Chromosome 2.
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; -; 3.
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; 1.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000019426};
KW Stress response {ECO:0000256|ARBA:ARBA00023016,
KW ECO:0000313|EMBL:CDM70465.1}.
SQ SEQUENCE 564 AA; 63254 MW; E4216C56FCCFD574 CRC64;
MTTIGIDLGT TNSLVAYWKE KEAIIIPNVL NKNMTPSVVS IDENDEILVG EIAKERLITH
PECTVSNFKR FMGTNKIFNM GKYNLTPEEL ASFVLKSLKS DAENFLGEEI TEAVISVPAY
FNDAQRKATK RAGELAGLKV ERLISEPTAA AIAYGLNQKD GETQFLIFDL GGGTFDVSIL
ELFDEVMEVK SIAGDNYLGG EDFNNLLVHY FIKENNLNVS QLERKDISAL YKQGEMCKIS
LTEKQSAEME LIISGKSISM NISREEFEKI SEELVLKLRN PIERALNDAD IDSDELDSII
LVGGSTRMPL VRSIVTKMFN KIPYSTINPD EVVAKGAAIQ AALKEKNEDL REMVLTDVCP
YTLGVDVVSE LGNGRYEEGY FLPIIERNSP IPISKVRTLY TVADNQRHML VNIYQGERRR
VADNIKLGEI EIDIPKGAAG EHPVDVRYTY DINGLLEVEV TIVSTGEVKS LVIENTPGLL
SEEEIEERLK ILSSLKIHPR EKTENRLLVA RGERLYEESL GSKRLYISQL LQGFESILET
QDSKLIEEAS KNLTEEFNKL EENH
//
