ID A0A0A3IF74_9BACI Unreviewed; 610 AA.
AC A0A0A3IF74;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
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:KGR81478.1};
GN ORFNames=CD32_19155 {ECO:0000313|EMBL:KGR81478.1};
OS Lysinibacillus odysseyi 34hs-1 = NBRC 100172.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1220589 {ECO:0000313|EMBL:KGR81478.1, ECO:0000313|Proteomes:UP000030437};
RN [1] {ECO:0000313|EMBL:KGR81478.1, ECO:0000313|Proteomes:UP000030437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100172 {ECO:0000313|EMBL:KGR81478.1,
RC ECO:0000313|Proteomes:UP000030437};
RA Zhang F., Wang G., Zhang L.;
RT "Draft genome sequence of Lysinibacillus odysseyi NBRC 100172.";
RL Submitted (FEB-2014) 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:KGR81478.1}.
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DR EMBL; JPVP01000060; KGR81478.1; -; Genomic_DNA.
DR RefSeq; WP_036157761.1; NZ_JPVP01000060.1.
DR AlphaFoldDB; A0A0A3IF74; -.
DR STRING; 1220589.CD32_19155; -.
DR eggNOG; COG0443; Bacteria.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000030437; 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:UP000030437};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 579..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 222..249
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 479..552
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 589..610
FT /note="Basic and acidic 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; 65338 MW; 8DEE0DA44F8D3B81 CRC64;
MSKIIGIDLG TTNSCVAVLE GGEPKVIPNP EGNRTTPSVV AFKNGEKQVG EVAKRQSVTN
PNTIISVKSK MGTAEKVKAE DKEYTPQEVS AMILQYLKGY AEDYLGEKVT KAVITVPAYF
NDAQRQATKD AGKIAGLEVE RIINEPTAAA LAYGLDKQDQ DQKILVFDLG GGTFDVSILE
LGDGVFEVLA TAGDNKLGGD DFDQKIIDFL VAEFKKENGI DLSKDKMAMQ RLKDAAEKAK
KDLSGVTSTQ ISLPFITAGA EGPLHLEVTL TRAKFDDLTR DLVERTIVPT RQALSDAGLA
ASELDKVILV GGSTRIPAVV EAIKKETGHE PHKGVNPDEV VAMGAAVQGG VLTGDVQDIV
LLDVTPLSLG IETMGGVFTK LIDRNTTIPT SKSQVFSTAA DNQPAVDIHV LQGERPMAAD
NKTLGRFQLS DIPPAPRGVP QIEVTFDIDK NGIVSVKAKD LGTNKEQTIV IQSDSGLSEE
EIERMVKDAE ANAEADAKRK EEAEVRNEAD QLVFQVDKTI TDLGEQITED EKKSVEDARD
ELKKALEAGE IEGIKSAKEK LEGVLQPLVM KVYEQAAAAA QAAQGDAGAD AGKKDDGIVD
ADFEEVKDDK
//
