ID A0A060JHJ5_9MICO Unreviewed; 613 AA.
AC A0A060JHJ5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Chaperone protein DnaK {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=Rhola_00013610 {ECO:0000313|EMBL:AIC48150.1};
OS Rhodoluna lacicola.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Luna cluster; Luna-1 subcluster; Rhodoluna.
OX NCBI_TaxID=529884 {ECO:0000313|EMBL:AIC48150.1, ECO:0000313|Proteomes:UP000067708};
RN [1] {ECO:0000313|EMBL:AIC48150.1, ECO:0000313|Proteomes:UP000067708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-Ta8 {ECO:0000313|EMBL:AIC48150.1,
RC ECO:0000313|Proteomes:UP000067708};
RX PubMed=24984700; DOI=10.1099/ijs.0.065292-0;
RA Hahn M., Schmidt J., Taipale S.J., Doolittle W.F., Koll U.;
RT "Rhodoluna lacicola gen. nov., sp. nov., a planktonic freshwater bacterium
RT with stream-lined genome.";
RL Int. J. Syst. Evol. Microbiol. 64:3254-3263(2014).
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 ---------------------------------------------------------------------------
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; CP007490; AIC48150.1; -; Genomic_DNA.
DR RefSeq; WP_038503384.1; NZ_CP007490.1.
DR AlphaFoldDB; A0A060JHJ5; -.
DR STRING; 529884.Rhola_00013610; -.
DR KEGG; rla:Rhola_00013610; -.
DR PATRIC; fig|529884.3.peg.1318; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_11; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000067708; Chromosome.
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; 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:UP000067708};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 493..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 228..255
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 613 AA; 66030 MW; BD5514F981FD4D2E CRC64;
MARAVGIDLG TTNSAVSVLE GGEPTVIANA EGFRTTPSIV AFTKDGEVLV GETAKRQAVT
NVDRTIASVK RHMGTDWTFN VDDKKYTPQE ISARILAKLK RDAETYLGEA VTDAVITVPA
YFNDAERQAT KDAGEIAGLN VLRIINEPTA AALAYGLDKG KEDELILVFD LGGGTFDVSL
LEVGKDEGFS TIQVRATSGD NRLGGDDWDQ RIVDHLVKKF KETSGVDVSK DKIALQRLKE
AAEQAKKELS QSMSANIQLP YLSLTENGPA NLDETLTRAQ FEQMTNDLLE RTRKPFNDVI
KEAGVKVGDI AHVVLVGGST RMPAVTELVK SLTGGKEPNK GVNPDEVVAV GASLQAGVLK
GERKDVLLID VTPLSLGIET KGGIMTKLIE RNTAIPTKRS ETFTTADDNQ PSVSIQVYQG
EREFVRDNKS LGNFDLSGIA PAPRGVPQIE VTFDIDANGI VHVSAKDKGT GKEASVTITG
GSSLSKEDIE RMVREGEEHA AEDKKRREEA DTRNQAESLV YQIEKLIKEN DEKLPEDVKT
TVQADVDALK TALAGEDIDA VKAAVEKLNE SQQKLGEAIY AAQPAEGEAA TEANAEDVVD
AEVVDDETEE AKK
//