ID A0A1R1EU49_9BACL Unreviewed; 617 AA.
AC A0A1R1EU49;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=BK138_11865 {ECO:0000313|EMBL:OMF55383.1};
OS Paenibacillus rhizosphaerae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=297318 {ECO:0000313|EMBL:OMF55383.1, ECO:0000313|Proteomes:UP000187172};
RN [1] {ECO:0000313|EMBL:OMF55383.1, ECO:0000313|Proteomes:UP000187172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-0378 {ECO:0000313|EMBL:OMF55383.1,
RC ECO:0000313|Proteomes:UP000187172};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-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}.
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:OMF55383.1}.
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DR EMBL; MRTP01000002; OMF55383.1; -; Genomic_DNA.
DR RefSeq; WP_076169778.1; NZ_MRTP01000002.1.
DR AlphaFoldDB; A0A1R1EU49; -.
DR STRING; 297318.BK138_11865; -.
DR Proteomes; UP000187172; 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:UP000187172};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 580..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 223..250
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 601..617
FT /note="Basic and acidic 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 617 AA; 65928 MW; 3CD2E51E6061B50E CRC64;
MSKVIGIDLG TTNSCVAVME GGEAVVIPNP EGARTTPSVV GFKKDGERIV GETAKRQSIT
NPDRTIISIK RHMGTNHKET IDGKEFTPQE ISAMILQKLK SDAEAYLGQP VTQAVITVPA
YFNDSQRQAT KDAGKIAGLE VLRIVNEPTA AALAYGLEKA EDQTILVYDL GGGTFDVSIL
ELGDGFFEVK ATSGDNHLGG DDFDQVIIDY LVSEFKKDQG IDLSKDKAAV QRLKDAAEKA
KKELSGVLTT TISLPFITVA DGVPQHLEVN LTRAKFEELS ADLVERTLGP TRQALSDAGM
SSSDIDKIVL VGGSTRIPAV QEAIKRLTGK EPHKGVNPDE VVALGAAVQA GVLTGDVKDV
VLLDVTPLSL GIETAGGVFT KMIERNTTIP TSKSQIFSTY ADNQPSVEIH VLQGERQMAA
GNKTLGRFIL GDIPPAPRGV PQIEVTFDID ANGIVNVSAT DKGTNKTQKI TITSSSGLSD
DEVERMMKDA EAHAEEDRQR KELIEAKNNA DQLVYSTEKT IKDLGDKVDA SEVEKANAAK
DKVKAAIDSD DLEQIKSATE ELTEIVQQLS VKLYEQAAQA QQAQGGEGNA DGAAGSAKKD
NVVDADYEVV DEDKNQG
//
