ID A0A1G8PQC1_9FIRM Unreviewed; 603 AA.
AC A0A1G8PQC1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN04487760_101293 {ECO:0000313|EMBL:SDI94425.1};
OS Lachnospiraceae bacterium G41.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1200749 {ECO:0000313|EMBL:SDI94425.1, ECO:0000313|Proteomes:UP000199016};
RN [1] {ECO:0000313|EMBL:SDI94425.1, ECO:0000313|Proteomes:UP000199016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G41 {ECO:0000313|EMBL:SDI94425.1,
RC ECO:0000313|Proteomes:UP000199016};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNEU01000001; SDI94425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8PQC1; -.
DR STRING; 1200749.SAMN04487760_101293; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000199016; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000199016};
KW Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT REGION 581..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 232..259
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 585..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 68052 MW; 9A950CCFF84B6E74 CRC64;
MSKIIGIDLG TTNSLVTVWE DGKAVCIPNA YGDFLTPSVV SFDGEEVIVG KAAKERLITA
PDDTIASFKR NMGRKTLLKN KFTAAELSSF ILKNLKADAE RYLKEEVTEA VISVPAYFDD
KARKATKLAG ELAGLTVNRI INEPSAAALG YLKNTEKGRE LSGDFDNHKL LVFDFGGGTL
DVSLLETFEN VVEIISVSGD NMQGGIDFDK AIAINYIKSL DKDPAQIKPQ DYNIILEDAE
ALKRKLSEKK EASVKVNAKG YKGIMSLTMK EFAALSAPIF KKIYVPIQNV LRDSGNKPED
INEVIVVGGS GKMPIVQQYL KHILKKDKLY VYEPDKIVAL GMGVYAGIKE RDEDVKDVIL
TDVAPFSLGI STVNYTNPEK PLSSFIIPRN TALPASRTHP YTVLYDGQGI IKVDIFQGEE
MYAEENRQIG SFEVNLHGLG KEGMLTYITF TYDLNGFLIV NVDIPDLEMT QEELFVDNEL
GLDEETVKKK VEQLKGLKLV SYEDEENLRI IEWGKKLFVQ CPDNIKREIS KKILFFESKL
AEDRYEAIKL RKYLKMYFLN IEMTILKNLL ENYEYDDSWL DEETRESDES FKRWEEDHKN
DKE
//
