ID E4KQB8_9LACT Unreviewed; 613 AA.
AC E4KQB8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
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 ECO:0000313|EMBL:EFR30921.1};
GN ORFNames=HMPREF9257_1719 {ECO:0000313|EMBL:EFR30921.1};
OS Eremococcus coleocola ACS-139-V-Col8.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Eremococcus.
OX NCBI_TaxID=908337 {ECO:0000313|EMBL:EFR30921.1, ECO:0000313|Proteomes:UP000005990};
RN [1] {ECO:0000313|EMBL:EFR30921.1, ECO:0000313|Proteomes:UP000005990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-139-V-Col8 {ECO:0000313|EMBL:EFR30921.1,
RC ECO:0000313|Proteomes:UP000005990};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000256|ARBA:ARBA00002290,
CC 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:EFR30921.1}.
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DR EMBL; AENN01000016; EFR30921.1; -; Genomic_DNA.
DR RefSeq; WP_006418707.1; NZ_AENN01000016.1.
DR AlphaFoldDB; E4KQB8; -.
DR STRING; 908337.HMPREF9257_1719; -.
DR eggNOG; COG0443; Bacteria.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000005990; 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; 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};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, 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:UP000005990};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 576..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 486..571
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 598..613
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 613 AA; 65942 MW; 294633D1360143C1 CRC64;
MAKIIGIDLG TTNSAVAVLE GGEAKIIPNP EGNRTTPSVV AFKNGEIQVG EVAKRQAVTN
MDTVSSIKRY MGEDHKVEAN GKSYTPQEIS AMILQYLKSY AEDYLGDKVT QAVITVPAYF
NDAQRQATKD AGKIAGLEVE RIVNEPTAAA LAYGLDKTEQ EEKILVFDLG GGTFDVSILE
LGDGVFDVLS TAGDNHLGGD DFDNKIIDYL VAEFKKENGI DLSTDKMAMQ RLKDAAEKAK
KDLSGVTQTQ ISLPFITASN AGPLHMETSL SRAKFDELTA DLVDRTKAPV RQALKDAGLG
QNEIDQVILV GGSTRIPAVV EAVRKETGKE PNKSVNPDEV VAMGAAIQGG VISGDVKDIV
LLDVTPLSLG IETMGGIFTK LIDRNTTIPT SKSQIFSTAA DNQPAVDVHV LQGEREMAAD
NKTLGRFQLT DIPAAPRGIP QIEVTFDIDK NGIVNVSAKD LGTQKEQSIT IKSSTGLSDE
EIDRMVKDAE ANAESDKARR EEADLRNEVD QLIFTTTKTL SELEGKVSED EVKKAEEARD
ELKAAVEAND LEQMKEKRDK LSEVVQNLSV KLYEQAAAAQ QAAQADGGNA DASASDSDDT
VVDAEFEEMD DNN
//
