ID G2Z926_LISIP Unreviewed; 613 AA.
AC G2Z926;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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:CBW85911.1};
GN OrderedLocusNames=LIV_1430 {ECO:0000313|EMBL:CBW85911.1};
OS Listeria ivanovii (strain ATCC BAA-678 / PAM 55).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=881621 {ECO:0000313|EMBL:CBW85911.1, ECO:0000313|Proteomes:UP000001286};
RN [1] {ECO:0000313|EMBL:CBW85911.1, ECO:0000313|Proteomes:UP000001286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-678 / PAM 55 {ECO:0000313|Proteomes:UP000001286};
RX PubMed=22072644; DOI=10.1128/JB.06120-11;
RA Buchrieser C., Rusniok C., Garrido P., Hain T., Scortti M., Lampidis R.,
RA Karst U., Chakraborty T., Cossart P., Kreft J., Vazquez-Boland J.A.,
RA Goebel W., Glaser P.;
RT "Complete genome sequence of the animal pathogen Listeria ivanovii, which
RT provides insights into host specificities and evolution of the genus
RT Listeria.";
RL J. Bacteriol. 193:6787-6788(2011).
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}.
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DR EMBL; FR687253; CBW85911.1; -; Genomic_DNA.
DR RefSeq; WP_014092845.1; NZ_CVPH01000005.1.
DR AlphaFoldDB; G2Z926; -.
DR GeneID; 57076412; -.
DR KEGG; liv:LIV_1430; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000001286; 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; 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 577..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 222..249
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 479..552
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 613 AA; 66121 MW; 86E4C9DAEA3F4DBF CRC64;
MSKIIGIDLG TTNSAVAVLE GGEAKIIPNP EGARTTPSVV GFKNGERQVG EVAKRAAITN
PNTISSIKRH MGTNYKETIE GKDYSPQEIS AIILQYLKSY AEDYLGETVD KAVITVPAYF
NDAQRQATKD AGKIAGLEVE RIINEPTAAA LAYGMDKTET DQTILVFDLG GGTFDVSILE
LGDGVFEVHS TAGDNELGGD DFDKKIIDYL VAEFKKDNGI DLSQDKMALQ RLKDAAEKAK
KDLSGVTSTQ ISLPFITAGE AGPLHLEVTL TRAKFDELTH DLVERTIAPT RQALKDANLS
ASDIDQVILV GGSTRIPAVQ ETIKKELGKE PHKGVNPDEV VAMGAAIQGG VITGDVKDVV
LLDVTPLSLG IETMGGVMTT LIERNTTIPT SKSQTFSTAA DNQPAVDIHV LQGERPMAKD
NKTLGRFQLA DIPAAPRGIP QIEVSFDIDK NGIVTVRAKD LGTGKEQNIV IKSSSGLTDE
EIEKMVQDAE ANAEEDKKNK ENAELRNNAD QLVFTVDKTL KELEGKVDED EVKKAEAARD
ELQEALKGED FEAIKEKTDS LNEIVQNLSV KLYEQAAAEQ QAAAGEDGQE APKNDDVVDA
EFEEVNDDDK ESK
//
