ID J9YYH0_9PROT Unreviewed; 641 AA.
AC J9YYH0;
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=HIMB5_00013490 {ECO:0000313|EMBL:AFS48087.1};
OS alpha proteobacterium HIMB5.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=859653 {ECO:0000313|EMBL:AFS48087.1, ECO:0000313|Proteomes:UP000006098};
RN [1] {ECO:0000313|EMBL:AFS48087.1, ECO:0000313|Proteomes:UP000006098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB5 {ECO:0000313|EMBL:AFS48087.1,
RC ECO:0000313|Proteomes:UP000006098};
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 (SEP-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; CP003809; AFS48087.1; -; Genomic_DNA.
DR AlphaFoldDB; J9YYH0; -.
DR STRING; 859653.HIMB5_00013490; -.
DR KEGG; apm:HIMB5_00013490; -.
DR PATRIC; fig|859653.3.peg.1318; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_5; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000006098; 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 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 515..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 247..274
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 515..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 641 AA; 69367 MW; E658ED319C056F1F CRC64;
MSKIIGIDLG TTNSCVAIME GSQAKVLENA EGARTTPSVV AFTDENEKLI GQPAKRQAVT
NPENTIFAVK RLIGRNFDDP TVKKDIEAAP FKIVNSEKND AWIEAKGEKY SPSQISAFIL
QKMKETAEKY LGQAVTKAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAASLAYG
LDKKQNKKIA VYDLGGGTFD VSILELGDGV FEVKSTNGDT FLGGEDFDNA VVEYLISEFK
KDNGIDLKSD KLALQRLKEA AEKAKIELSS AEQTDINLPF ITADKTGPKH INLKMTRAKL
EALVEDLIAR TVPPCQTALK DAGITASEID EVVMVGGMTR MPKVIDEVKN FFGKDPNKSV
NPDEVVAMGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVSTKLIDKN TTIPTKKSQV
FSTAEDNQPA VSIRVLQGER EMATDNKLLG NFELVGIAPA PRGVPQIEVT FDIDANGIVN
VSAKDKGTGK EQKIQIQASG GLSDEEIEKM VKDAEANKEA DKKKRESVDV RNQADTLIHS
TEKNLKEHGS KISDAEKKAI EDSSAAVKEA LKGDNIEDIK KKTEALVQAS MKLGEAIYKS
QQNTKPESGK DDGKDNKDKK DDNVVDADFE EVKDENKEKS A
//