ID A0A0S7YCK0_9BACT Unreviewed; 644 AA.
AC A0A0S7YCK0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 25.
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:KPJ72533.1};
GN ORFNames=AMJ48_03185 {ECO:0000313|EMBL:KPJ72533.1};
OS Parcubacteria bacterium DG_74_1.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1703765 {ECO:0000313|EMBL:KPJ72533.1, ECO:0000313|Proteomes:UP000051540};
RN [1] {ECO:0000313|EMBL:KPJ72533.1, ECO:0000313|Proteomes:UP000051540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_74_1 {ECO:0000313|EMBL:KPJ72533.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ72533.1}.
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DR EMBL; LJNE01000013; KPJ72533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7YCK0; -.
DR STRING; 1703765.AMJ48_03185; -.
DR PATRIC; fig|1703765.3.peg.404; -.
DR Proteomes; UP000051540; 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 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.
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 603..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 511..586
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 624..644
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 644 AA; 70439 MW; D6B039595D49B77D CRC64;
MSKILGIDLG TSISKMATIL HGEPKCLESR EGSILVPSVV ASGKSGERMV GILAERQSVT
NPKNTIHSVK RFIGRRYSDP EVQKELKLLS YETRERQDGG VEVKMGDKWY TAIEISAMIL
QKLKLDAEEK LGEKIEPVVI TCPANFDDSQ RKATKAAGEI AGFKVYQIIN EPTAAALAYG
FGRREAEKVV VYDFGGGTFD VTCLNIAPDT VEVLATGGEA HLGGRDFDQK IINWVLEEFK
KEQGIDLSKD PLALQRLKET CEKAKIELSS VMETEINLPF ITSDASGPKH LLYKLSRAQF
ENMSRDLIET SIERIKKTLA EAKLNKSELN EVILVGGTTL IPAVRQAVKD FFDKEPNKSI
NPEEVVAMGA AINAEIWRAK EEGRAPEGDI KSVLLLDVLP LSLGIETLGG ISTQMIAKNT
TIPTAKTQIF STAADNQPSV EVNVLQGERP MAADNRSIGK FILDGIPPAP RGLPQIEVTF
DVDVNGILTV TAKDKATGKS QSIKIEGSIG ISKEEIEKMK KEAELHAQED KKKQELIEAR
NLADNLVYTT EKTLREAGGK ISSETKKEIE EKISELKKVK DSDNVEEIKQ KTQEASQVIQ
KIGAEMYKAA GGQNPPTGGP PGKEKGPKEG EGPKADEGEY KEKK
//
