ID F2I075_PELSM Unreviewed; 646 AA.
AC F2I075;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 OrderedLocusNames=SAR11G3_00367 {ECO:0000313|EMBL:AEA80842.1};
OS Pelagibacter sp. (strain IMCC9063).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae; Pelagibacter.
OX NCBI_TaxID=1002672 {ECO:0000313|EMBL:AEA80842.1, ECO:0000313|Proteomes:UP000009181};
RN [1] {ECO:0000313|EMBL:AEA80842.1, ECO:0000313|Proteomes:UP000009181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC9063 {ECO:0000313|EMBL:AEA80842.1,
RC ECO:0000313|Proteomes:UP000009181};
RX PubMed=21515764; DOI=10.1128/JB.05033-11;
RA Oh H.M., Kang I., Lee K., Jang Y., Lim S.I., Cho J.C.;
RT "Complete genome sequence of strain IMCC9063, belonging to SAR11 subgroup
RT 3, isolated from the Arctic Ocean.";
RL J. Bacteriol. 193:3379-3380(2011).
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; CP002511; AEA80842.1; -; Genomic_DNA.
DR RefSeq; WP_013695007.1; NC_015380.1.
DR AlphaFoldDB; F2I075; -.
DR STRING; 1002672.SAR11G3_00367; -.
DR KEGG; pel:SAR11G3_00367; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000009181; 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:SF541; CHAPERONE PROTEIN DNAK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 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:UP000009181};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 515..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 244..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 544..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..646
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 646 AA; 69553 MW; 8DDD7E5514B68B8D CRC64;
MSKIIGIDLG TTNSCVAVMD GSTPKVLENL EGARTTPSVV AFTDSEEKLV GTSAKRQGVT
NAENTFFAVK RLIGRKFDGD AVKKDIQGLP YKIIKADNGD AWVESRGKKY SPSQISAFVL
QKMKETAEKY LGSEVKEAVI TVPAYFNDSQ RQATKDAGKI AGLEVKRIIN EPTAAALAYG
LDKKNAKTVA VYDLGGGTFD VSILELGDGV FEVKSTNGDT TLGGEDFDAH IVDYLADEFK
KDNAIDLKQD KLALQRLREA AEKAKIELSS ATQTEINLPF ITADKSGPKH LNLKLTRSKL
ESIVSELIKK TIAPCKTALK DAGLSAGEIG EIILVGGMTR MPKVAETVKN FFGKEPNKSV
NPDEVVAMGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVSTKLIEKN TTIPTKKSQV
FSTAENNQPA VSIRVVQGER EMAADNKSLG NFELTGIAPA PRGIPQIEVT FDIDANGIVN
VSAKDKGTGK EQKIQIQASG GLSDEEIEKM VKDAEVNKEE DKKKREEIDA KNSADSLVAS
TEQSLKEHGD KVSAEDKKTI ETDLQSLKDA IKSENVEDIK TKTQTLMQSS MKMGEAIYKA
QQAKPEGGAE GAKASDGEKK EDVVDAEFEE VKDSKEEEKE DKKDSA
//
