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Database: UniProt
Entry: A0A3D8JBR7_9HELI
LinkDB: A0A3D8JBR7_9HELI
Original site: A0A3D8JBR7_9HELI 
ID   A0A3D8JBR7_9HELI        Unreviewed;       620 AA.
AC   A0A3D8JBR7;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
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   ORFNames=CQA57_02350 {ECO:0000313|EMBL:RDU74341.1};
OS   Helicobacter anseris.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=375926 {ECO:0000313|EMBL:RDU74341.1, ECO:0000313|Proteomes:UP000256695};
RN   [1] {ECO:0000313|EMBL:RDU74341.1, ECO:0000313|Proteomes:UP000256695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 04-9362 {ECO:0000313|EMBL:RDU74341.1,
RC   ECO:0000313|Proteomes:UP000256695};
RA   Mannion A.J., Shen Z., Fox J.G.;
RT   "Novel Campyloabacter and Helicobacter Species and Strains.";
RL   Submitted (APR-2018) 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}.
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:RDU74341.1}.
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DR   EMBL; NXLX01000003; RDU74341.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8JBR7; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000256695; 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: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.
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:UP000256695};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   REGION          590..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          246..273
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        590..608
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   620 AA;  67157 MW;  F64E40089172D818 CRC64;
     MGKVIGIDLG TTNSAMAVYE GNEAKIITNK EGKNTTPSIV AFTDKGEILV GEPAKRQAIT
     NPQKTIYSIK RIMGLMFNED KAKEAEKRLP YKIVDRNGAC AIEIADKTYT PQEISAKILM
     KLKEDAESYL GESVTEAVIT VPAYFNDAQR KATKEAGTIA GLNVLRIINE PTSAALAYGL
     DKKESEKIMV YDLGGGTFDV TVLETGDNVV EVLATGGDAF LGGDDFDNRI IDWAAGEFKD
     ETGIDIKADV MALQRLKDAA ENAKKELSSA QETEINLPFI TADASGPKHL VKKLTRAKFE
     NLIDDLIEQT ISKIDFVIKD AGLSKSDISE IVMVGGSTRI PKAQERVKEF IGKELNKSVN
     PDEVVAIGAA IQGGVLKGDV KDVLLLDVTP LSLGIETLGG VMTKVIDRGT TIPAKKTQTF
     STAEDNQPAV SISVLQGERE MAKDNKSLGR FDLQGIPPAP RGVPQIEVTF DIDANGILTV
     SAKDKTSGKS QEIKISGSSG LSDSEIEKMV KDAELHKEED AKRKATIESR NLADNLVYQT
     QKMLDESKDK ISNDEAQKIQ GAIDALKDTL KDDNASKEQI EEKMKQLSEA AQNLAQSAQQ
     NANTQQNTKK DDDVIDAEVE
//
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