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Database: UniProt
Entry: A0A0R2HJR3_9FIRM
LinkDB: A0A0R2HJR3_9FIRM
Original site: A0A0R2HJR3_9FIRM 
ID   A0A0R2HJR3_9FIRM        Unreviewed;       605 AA.
AC   A0A0R2HJR3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=IV49_GL001916 {ECO:0000313|EMBL:KRN50597.1};
OS   Kandleria vitulina DSM 20405.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Coprobacillaceae; Kandleria.
OX   NCBI_TaxID=1410657 {ECO:0000313|EMBL:KRN50597.1, ECO:0000313|Proteomes:UP000051841};
RN   [1] {ECO:0000313|EMBL:KRN50597.1, ECO:0000313|Proteomes:UP000051841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20405 {ECO:0000313|EMBL:KRN50597.1,
RC   ECO:0000313|Proteomes:UP000051841};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRN50597.1}.
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DR   EMBL; JQBL01000007; KRN50597.1; -; Genomic_DNA.
DR   RefSeq; WP_029070644.1; NZ_JQBL01000007.1.
DR   AlphaFoldDB; A0A0R2HJR3; -.
DR   PATRIC; fig|1410657.5.peg.1977; -.
DR   Proteomes; UP000051841; 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; 2.
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.
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:UP000051841};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   REGION          575..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          477..571
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        575..596
FT                   /note="Polar 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   605 AA;  65058 MW;  9E228D348FE31CA0 CRC64;
     MSKIIGIDLG TTNSCVSVME NGEAKVIANA EGARTTPSVV AFKNGEIIVG EAAKRQAVTN
     PETVSSIKRH MGTSYKEHVN GKDYTPEEIS AMILQNLKKT AESYLGETVT KAVITVPAYF
     NDAQRQATKD AGKIAGLDVE RIINEPTAAA LAFGIDKIEK EQKVLVYDLG GGTFDVSILD
     LADGTFEVLA TAGNNHLGGD DFDKAVMDWM VSEFKKEQGI DLSSDNMAMQ RVKDAAEKAK
     KDLSGMMQTQ ISLPFISAGA NGPVHLDMTL TRAKFDELTS SLVSATEGPV RQALSDAGMQ
     PSEIDEVLLV GGSTRIIAVQ ESVKRLLGKE PNKSVNPDEV VSMGASIQGG VIAGDVKDVL
     LLDVTPLSLG IETMGGVMTV LIERNTTIPT TKSQIFSTAA DNQPAVDINV LQGERSMAKD
     NKQLGLFKLD GIEPAPRGVP QIEVTFNIDV NGIVNVKAKD MKTNKEQSIT IQNSTGLSDE
     EIDRMVKEAE ANKAEDEKMK KDIETKNKAE QMINEIDKSL ATQGDKISAD QKAQAESLRD
     ELKKALDAND MATLESRMNE LEQMAQQMAA YQYQNAQGGA TQDAGATNAN NNNDDVVDAD
     FTEKN
//
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