ID J4XQE9_9FIRM Unreviewed; 616 AA.
AC J4XQE9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:EJO22796.1};
GN ORFNames=HMPREF1148_1636 {ECO:0000313|EMBL:EJO22796.1};
OS Selenomonas sp. FOBRC6.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=936572 {ECO:0000313|EMBL:EJO22796.1, ECO:0000313|Proteomes:UP000006984};
RN [1] {ECO:0000313|EMBL:EJO22796.1, ECO:0000313|Proteomes:UP000006984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOBRC6 {ECO:0000313|EMBL:EJO22796.1,
RC ECO:0000313|Proteomes:UP000006984};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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:EJO22796.1}.
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DR EMBL; ALKG01000079; EJO22796.1; -; Genomic_DNA.
DR RefSeq; WP_009656018.1; NZ_ALKG01000079.1.
DR AlphaFoldDB; J4XQE9; -.
DR STRING; 936572.HMPREF1148_1636; -.
DR PATRIC; fig|936572.3.peg.1001; -.
DR eggNOG; COG0443; Bacteria.
DR Proteomes; UP000006984; 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; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 3.
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 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 COMPBIAS 577..598
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; 65718 MW; BFC239CDE878E302 CRC64;
MAKVIGIDLG TTNSVVSVME GGEPVVITNP EGSRITPSVV GFTKDGQRLV GRLAKNQAVS
NPDRTISSIK RHMGDPNYHV AIDGKNYTPP EISAMILQKL KSDAEAYLGE TVTQAVITVP
AYFNDSQRQA TKDAGKIAGL EVLRIINEPT AAALAYGLDK DQDETVLVFD LGGGTFDVSI
LELSEGVFEV KATNGDTVLG GDDFDKKIMD WMVEEFKKEN GIDLSQDKMS AQRLIEAAEK
AKIELSSMSQ TNINLPFITA DASGPKHLDL TLSRAKFDEL TADLVERTMV PTRKAMEDAG
LSSNEIDKII LVGGSTRIPA VQDAIRKILG KEPSKGVNPD ECVSIGAAIQ GGVLVGEVKD
VLLLDVTPLS LGIETLGGVC TKIIDRNTTI PTSKSQVFST AADNQPGVEI HVLQGEREMA
AGNKTLGRFQ LTDIPPAPRG VPQIEVKFDI DANGIVNVSA KDLGTGKEQK ITIQSDSGMS
KEDIERMVKE AESHAAEDKK QKEAVDARNA GDSLVYQAEK AIKDLGENAD QTLVSKTQTA
IDKLKEALKG SDIEAIKAAT EEARQPLYEL SAAAYQQAQQ AAGAAPGTDT NAGAQSGAQD
DNVVDAEFTE VKDDKK
//
