ID A6EHN4_9SPHI Unreviewed; 619 AA.
AC A6EHN4;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 13-SEP-2023, entry version 72.
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 ECO:0000313|EMBL:EDM35060.1};
GN ORFNames=PBAL39_08275 {ECO:0000313|EMBL:EDM35060.1};
OS Pedobacter sp. BAL39.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=391596 {ECO:0000313|EMBL:EDM35060.1, ECO:0000313|Proteomes:UP000003664};
RN [1] {ECO:0000313|EMBL:EDM35060.1, ECO:0000313|Proteomes:UP000003664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL39 {ECO:0000313|EMBL:EDM35060.1,
RC ECO:0000313|Proteomes:UP000003664};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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:EDM35060.1}.
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; ABCM01000017; EDM35060.1; -; Genomic_DNA.
DR AlphaFoldDB; A6EHN4; -.
DR STRING; 391596.PBAL39_08275; -.
DR eggNOG; COG0443; Bacteria.
DR Proteomes; UP000003664; 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; 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 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:UP000003664};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 574..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 179
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 619 AA; 66503 MW; 9927E73BDE1D66BF CRC64;
MEGNEPVVIA NSEGKRTTPS IVAFAENGER KVGEPAKRQA ITNPTKTISS IKRFMGSSFA
EVTKESGRVP YTVVKGDNNT PRVEIDDRKY TPQEISAMIL QKMKKTAEDF LGHEVSEAVI
TVPAYFNDAQ RQATKEAGEI AGLTVKRIIN EPTAAALAYG LDKAHKDMKI VVFDCGGGTH
DVSVLELGDG VFEVKSTDGD THLGGDDFDH IIIEWLASEF KSENGMDLHQ DPMALQRLKE
AAEKAKIELS STTSTEINLP YITADATGPK HLVRNLSRAK FEQLAADLIK RTIDPCKSAL
KNAGLKTTDI DEIILVGGST RIPAIQDAVK AFFGKEPSKG VNPDEVVAIG AAIQGGVLTG
EVKDVLLLDV TPLSLGIETM GGVMTKLIEA NTTIPSKKAE TFSTAADNQP SVEIHILQGE
RPMAAQNRTI GRFILDGIPP APRGVPQVEV AFDIDANGIL HVSAKDKATG KEQKIRIEAS
SGLTDEEIKR MKEEAEQNAD ADKAAKDEAD KINSADALIF STEKQLKEFG DKLGADKKAP
IEEGLKKLKD AHAARNFADI DAAQTELQNA WNAASEDMYK AGQDGAQPEG ASDAQADAQS
AGGDDVTDVD FEEVKDDNK
//
