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Database: UniProt
Entry: A0A073IM85_9RHOB
LinkDB: A0A073IM85_9RHOB
Original site: A0A073IM85_9RHOB 
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}.
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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
//
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