ID A0A162MBF5_9FIRM Unreviewed; 623 AA.
AC A0A162MBF5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 ECO:0000313|EMBL:KYO65159.1};
GN ORFNames=ATZ99_17480 {ECO:0000313|EMBL:KYO65159.1};
OS Thermovenabulum gondwanense.
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Thermosediminibacteraceae; Thermovenabulum.
OX NCBI_TaxID=520767 {ECO:0000313|EMBL:KYO65159.1, ECO:0000313|Proteomes:UP000075737};
RN [1] {ECO:0000313|EMBL:KYO65159.1, ECO:0000313|Proteomes:UP000075737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R270 {ECO:0000313|EMBL:KYO65159.1,
RC ECO:0000313|Proteomes:UP000075737};
RA Patel B.K.;
RT "Draft genome of Thermovenabulum gondwanense isolated from a red
RT thermophilic microbial mat colonisisng an outflow channel of a bore well.";
RL Submitted (DEC-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO65159.1}.
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DR EMBL; LOHZ01000037; KYO65159.1; -; Genomic_DNA.
DR RefSeq; WP_068748863.1; NZ_LOHZ01000037.1.
DR AlphaFoldDB; A0A162MBF5; -.
DR STRING; 520767.ATZ99_17480; -.
DR PATRIC; fig|520767.4.peg.1863; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000075737; Unassembled WGS sequence.
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; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000075737};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 577..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 223..250
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 487..549
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 577..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 623 AA; 68243 MW; 8604716DC85A2AA4 CRC64;
MGRIIGIDLG TTNSVAAYME GGQPVVIPNA EGSRLTPSAV AFTKDGQRLV GQLAKRQAIL
NPERTILSIK RHMGTDYKVH IDGKAYTPQE ISAMILQKIK QDAESYLGEK ITQAVITVPA
YFTDSQRQAT KDAGRIAGLE VLRIINEPTA AALAYGLDKG EDQIILVFDL GGGTFDVSIL
ELGDGVFEVK ATSGNNRLGG DDFDQRIIDY IANEFYKEHG IDLRKDRMAL QRLKEAAEKA
KIELSSMLET TISLPFITAD ASGPKHIEMT LTRAKFEELT RDLVEATMGP TQQALKDAGL
TPQDIDKVIL VGGSTRIPAV QEAIRRFIGK EPCKGVNPDE VVAMGAAIQA GVLAGEVKDI
VLLDVTPLSL GIETLGGVFT KIIERNTTIP VSKSQIFTTA ADGQTTVDIH VLQGERPMAA
DNVTLGRFQL TGIPPAPRGV PRIEVKFDID VNGIVHVSAK DLGTGKEQKI TITSTTNLKE
EEIQRMIKDA ERFAEEDRKR KEKVEAKNHA DSLIYQSEKM LNDLKDKINN EEREKIQKEI
ENVKKAIESD DIDKIRKATD DLTKAFYDIS SRLYSQADSQ TQTGTGTNAG GSTNFGFSAA
NDNKKDEKVF DADYKFVNDD EKK
//
