ID J9YZQ8_9PROT Unreviewed; 643 AA.
AC J9YZQ8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=HIMB59_00003970 {ECO:0000313|EMBL:AFS48597.1};
OS alpha proteobacterium HIMB59.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=744985 {ECO:0000313|EMBL:AFS48597.1, ECO:0000313|Proteomes:UP000006097};
RN [1] {ECO:0000313|EMBL:AFS48597.1, ECO:0000313|Proteomes:UP000006097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB59 {ECO:0000313|EMBL:AFS48597.1,
RC ECO:0000313|Proteomes:UP000006097};
RA Grote J., Thrash C., Huggett M.J., Landry Z., Carini P., Giovannoni S.J.,
RA Rappe M.S., Brinkac L., Kim M., Beeson K., Ferriera S., Sutton G.,
RA Friedman R., Venter J.C.;
RL Submitted (AUG-2012) 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}.
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DR EMBL; CP003801; AFS48597.1; -; Genomic_DNA.
DR AlphaFoldDB; J9YZQ8; -.
DR STRING; 744985.HIMB59_00003970; -.
DR KEGG; apc:HIMB59_00003970; -.
DR PATRIC; fig|744985.3.peg.397; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000006097; 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; cd11733; HSPA9-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}; 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:UP000006097};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 574..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 246..273
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 580..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 643 AA; 69566 MW; 5EE3F329DC7F6B03 CRC64;
MAKVIGIDLG TTNSCVAIMD GKNPKVIENS EGARTTPSVV AFTESEKLIG QSAKRQAVTN
PENTLYAVKR FIGRSFDDQT VQKDVSLSPF KIIKGNNGDA WVEAQGEKYS PSQISAFILQ
KMKETAESYT GETITQAVIT VPAYFNDAQR QATKDAGKIA GLEVLRIINE PTAASLAYGL
DKKQSGTVVV YDLGGGTFDV SILEVGDGVF EVKATNGDTH LGGEDFDLRI IDFLANEFKK
EQGIDLKNDK LALQRLKEAA EKAKIELSSS TQTDVNLPFI TADQSGPKHL NVKLTRAKLE
ELVDDLLQNT IEPCKKALSD AGLSASDIND VILVGGMTRM PKVTEIVKNF FGKDPSKGVN
PDEVVAMGAA IQAGVLQGDV KDVLLLDVTP LSLGIETLGG VFTKLIERNT TVPTKKSQVF
STAEDNQNAV TIRVFQGERE MAQDNKLLGQ FDLVGIPPAP RGTPQIEVTF DIDANGIVNV
SAKDKSTGKE QQIKIQASGG LSDEEIDKMV KDAEANAEAD KKKREEVDVK NQADSLVFQV
EKNLKEHGDK IAAEDKSKIE SDLKDLKDAI EKNDLEAMKQ KTQDLTQSSM KMGEAMYKDQ
QAAGGAAGAE QPQSDNQQEA PKDDDVIDAD YEEVDEDKKA SGQ
//
