ID A0A223ARS5_9FIRM Unreviewed; 616 AA.
AC A0A223ARS5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Chaperone protein DnaK {ECO:0000256|ARBA:ARBA00014415, ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000256|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000256|HAMAP-Rule:MF_00332};
GN ORFNames=AXF17_03915 {ECO:0000313|EMBL:ASS37681.1};
OS Mogibacterium pumilum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis; Mogibacterium.
OX NCBI_TaxID=86332 {ECO:0000313|EMBL:ASS37681.1, ECO:0000313|Proteomes:UP000214689};
RN [1] {ECO:0000313|Proteomes:UP000214689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700696 {ECO:0000313|Proteomes:UP000214689};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000256|ARBA:ARBA00002290,
CC ECO:0000256|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000256|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|HAMAP-Rule:MF_00332,
CC ECO:0000256|RuleBase:RU003322}.
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DR EMBL; CP016199; ASS37681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A223ARS5; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000214689; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR NCBIfam; TIGR02350; prok_dnaK; 1.
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; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00332};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00332};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00332};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_00332};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 577..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 224..251
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 481..508
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 577..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 616 AA; 65728 MW; 80AA872B917F66A8 CRC64;
MSKVIGIDLG TTNSCVAVLE GGEPVVIANA EGARTTPSVV AFTKNGERLV GETAKRQAIT
NPDRTIASIK RHMGESYTVE IDGKSYTPQD ISAMILGKLK ADAEAYLGEK VTEAVITVPA
YFSDAQKQAT KDAGKIAGLE VKRIINEPTA ASLAYGLDKA DGTQKILVYD LGGGTFDVSV
LELGDGVFEV LATNGDTHLG GDDFDNAVLN FLADSFMAEH GIDLRKDNMA LQRLKEAAEK
AKKELSSAQT TKINLPFITV SEAGPLHMDM DLTRARFDQL TSDLVERSIE PMKKAMSDAG
VSNSDIAKVI LVGGSTRIPA VQAAVQKVTG KEPFKGINPD ECVAVGASIQ AGVLTGEVND
VLLLDVTPLS LSIETLGGVA TKLIERNTTI PTKKSQIFST AADNQTAVDV HVMQGEREMA
ADNITLGRFQ LTGIAPAPRG IPQIEVTFDI DANGIVNVSA KDLGTGKEQQ ITITSSTKLS
EDEINAKIKE AEQYAEEDKK KKEEVEVKNQ AEGILFETEK QMNELGDKVT ADEKAKVDAA
REDLKKAVEA NDVEDTKAKI EALTQAFYPI SSRIYQEAQA QAGATGAAEQ TQDGTQSEGP
NGNTVDADYE VVDEDK
//
