ID A0A073IM85_9RHOB Unreviewed; 639 AA.
AC A0A073IM85;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
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:KEJ90700.1};
GN ORFNames=DSW25_01925 {ECO:0000313|EMBL:KEJ90700.1};
OS Sulfitobacter donghicola DSW-25 = KCTC 12864 = JCM 14565.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1300350 {ECO:0000313|EMBL:KEJ90700.1, ECO:0000313|Proteomes:UP000027734};
RN [1] {ECO:0000313|EMBL:KEJ90700.1, ECO:0000313|Proteomes:UP000027734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14565 {ECO:0000313|EMBL:KEJ90700.1,
RC ECO:0000313|Proteomes:UP000027734};
RA Lai Q., Hong Z.;
RT "Sulfitobacter donghicola JCM 14565 Genome Sequencing.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {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:KEJ90700.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAMC01000001; KEJ90700.1; -; Genomic_DNA.
DR RefSeq; WP_025059079.1; NZ_JASF01000005.1.
DR AlphaFoldDB; A0A073IM85; -.
DR STRING; 1300350.Z948_1675; -.
DR eggNOG; COG0443; Bacteria.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000027734; 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 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}; Chaperone {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:UP000027734};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 604..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 246..273
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 511..577
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 639 AA; 68639 MW; B4D6DE21AB895A9B CRC64;
MAKVIGIDLG TTNSCIAIMD GSQPRVIENA EGARTTPSIV AFTEDERLVG QPAKRQAVTN
PDNTIFGVKR LIGRRNDDAD LAKDKKNLPF NVINGGNGDA WVEARGEKYS PSQISAFILG
KMKETAESYL GEEVSQAVIT VPAYFNDAQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
DKEETQTIAV YDLGGGTFDV TILEIDDGLF EVKSTNGDTF LGGEDFDMRI VNYLADEFKK
ENQVDLTQDK MALQRLKEAA EKAKIELSSA TQTEINQPFI SMGSTGQPLH MVMKLTRAKL
ESLVGDLIKA SMKPCAAALK DAGLAASDID EVVLVGGMTR MPRVIEEVTK FFGKEPHKGV
NPDEVVALGA AIQAGVLQGD VKDVVLLDVT PLSLGIETLG GVFTRLIDRN TTIPTKKSQI
FSTAEDNQNA VTIRCFQGER EMAADNKILG AFNLEEIPPA PRGMPQIEVT FDIDANGIVS
VGALDKGTGK EQKITIQASG GLSDADIEKM VQDAEDNAEA DKERRELIEA KNQAESLIHS
TEKSVEEHSD KVDPTTVEAI ELAIAALKDE METENAEKIK SGIQNVTEAA MKLGEAIYKS
AQEAGEDDMA AAADEGPAGG PDDDIVDADF EDLDGDKRS
//