ID A0A1I0FVZ7_9BACI Unreviewed; 610 AA.
AC A0A1I0FVZ7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-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=SAMN05216389_11742 {ECO:0000313|EMBL:SET61648.1};
OS Oceanobacillus limi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=930131 {ECO:0000313|EMBL:SET61648.1, ECO:0000313|Proteomes:UP000198618};
RN [1] {ECO:0000313|EMBL:SET61648.1, ECO:0000313|Proteomes:UP000198618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M 10780 {ECO:0000313|EMBL:SET61648.1,
RC ECO:0000313|Proteomes:UP000198618};
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 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; FOHE01000017; SET61648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0FVZ7; -.
DR STRING; 930131.SAMN05216389_11742; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000198618; 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:UP000198618};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 525..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 222..249
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 576..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 610 AA; 66499 MW; 9E4DDFAE377A1CF6 CRC64;
MSKIIGIDLG TTNSCVAVME GGEAVVIPNP EGNRTTPSVV AFKNGERQVG EVAKRQAITN
PDTIQSIKRH MGTDYKVKID DKEYTPQEVS AIILQHIKSY AEDYIGEKVE KAVITVPAYF
NDAERQATKD AGKIAGLEVE RIINEPTAAA LAYGIDKEDQ DQTILVYDLG GGTFDVSILD
IGDGTFEVVS TAGDNRLGGD DFDEVIINHM VAEFKKENGI DLSQDKMAMQ RLKDAAEKAK
KDLSGVTQTQ ISLPFITAGD AGPLHLEMNM TRAKFEELSS DLVERTMVPT RKALSDAGLS
ASDIHKVILV GGSTRIPAVQ EAIKRETGKE PSKGVNPDEV VALGAAIQGG VLQGDVKDVL
LLDVTPLSLG IETMGGVFTK LIERNTTIPT SHSQVFSTAA DNQTAVDIHV LQGEREMAQD
NKTLGRFQLT DIPPAPRGVP QIEVSFDIDA NGIVNVRALD KGTNKEQSIT IKSSSGLSDE
EVDKMVKEAE ENAEADKKRR EEVDLRNEAD QLVFTTDKTI KDLGDKVSDE EKQNAENAKD
ELKKALESDN LDDIKAKKEA LEEQVQQLSV KLYEQMAQEQ QAQQGQEGQS QDDDVVDADY
QEVDDEENKK
//
