ID I0EG38_HELPX Unreviewed; 620 AA.
AC I0EG38;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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:AFI01907.1};
GN ORFNames=HPPC18_00570 {ECO:0000313|EMBL:AFI01907.1};
OS Helicobacter pylori PeCan18.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1163742 {ECO:0000313|EMBL:AFI01907.1, ECO:0000313|Proteomes:UP000005006};
RN [1] {ECO:0000313|EMBL:AFI01907.1, ECO:0000313|Proteomes:UP000005006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PeCan18 {ECO:0000313|EMBL:AFI01907.1,
RC ECO:0000313|Proteomes:UP000005006};
RA Kersulyte D., Ramirez Ramos A., Recarvarren S., Barua R.L., Watanabe J.,
RA Gilman R.H., Berg D.E.;
RL Submitted (APR-2012) 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}.
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DR EMBL; CP003475; AFI01907.1; -; Genomic_DNA.
DR RefSeq; WP_000521047.1; NC_017742.1.
DR AlphaFoldDB; I0EG38; -.
DR KEGG; hca:HPPC18_00570; -.
DR PATRIC; fig|1163742.3.peg.118; -.
DR HOGENOM; CLU_005965_2_1_7; -.
DR Proteomes; UP000005006; 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 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.
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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 592..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 246..277
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 603..620
FT /note="Basic and acidic 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; 67035 MW; 552AA4769C181756 CRC64;
MGKVIGIDLG TTNSAMAVYE GNEAKIIANK EGKNTTPSIV AFTDKGEILV GESAKRQAVT
NPEKTIYSIK RIMGLMFNED KAKEAEKRLP YKIVDRNGAC AVEISGKIYT PQEISAKILM
KLKEDAESYL GESVTEAVIT VPAYFNDSQR KATKEAGTIA GLNVLRIINE PTSAALAYGL
DKKESEKIMV YDLGGGTFDV TVLETGDNVV EVLATGGDAF LGGDDFDNRV IDFLAAEFKS
ETGIEIKNDV MALQRLKEAA ENAKKELSSA METEINLPFI TADATGPKHL VKKLTRAKFE
SLTEDLVEET ISKIESVIKD AGLTKNEISE VVMVGGSTRI PKVQERVKAF INKDLNKSVN
PDEVVAVGAS IQGGVLKGDV KDVLLLDVTP LSLGIETLGG VMTKVIDRGT TIPAKKSQVF
STAEDNQPAV SIMVLQGERE LARDNKSLGK FDLQGIAPAP RGVPQIEVTF DIDANGILTV
SAQDKNTGKS QEIKISGSSG LSDSEIEKMV KDAELHKEED ARKKEVIEAR NHADSLAHQT
QKSLDEHKAN LNENDANEIQ NAINTLKDCI KNDNTTKAEL EDKTKALAQA AQKLGEAMAN
KNNAEQPKKK DDDVIDAEVE
//
