DNAK_ALTMD
ID DNAK_ALTMD Reviewed; 642 AA.
AC B4S0U1; F2G6L6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332};
GN OrderedLocusNames=MADE_1007055;
OS Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS ecotype).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1774373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype;
RX PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S.,
RA Johnson J., Friedman R., Rodriguez-Valera F.;
RT "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT Alteromonas macleodii suggests alternative lifestyles associated with
RT different kinds of particulate organic matter.";
RL ISME J. 2:1194-1212(2008).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR EMBL; CP001103; AEA97553.1; -; Genomic_DNA.
DR RefSeq; WP_012517895.1; NC_011138.3.
DR AlphaFoldDB; B4S0U1; -.
DR SMR; B4S0U1; -.
DR EnsemblBacteria; AEA97553; AEA97553; MADE_1007055.
DR KEGG; amc:MADE_1007055; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000001870; 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 Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
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 PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Stress response.
FT CHAIN 1..642
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119661"
FT REGION 605..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 642 AA; 69071 MW; 75C7A2502BB24720 CRC64;
MGRIIGIDLG TTNSCVAVLD GDKPRVIENA EGDRTTPSII AYTNDGETLV GQSAKRQAVT
NPENTLFAIK RLIGRRFQDK EVQRDIDIMP FKIVGADNGD AWVEAKGEKM APPQVSAEVL
KKMKKTAEDY LGEEVTGAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
MDKKQGDNVV AVYDLGGGTF DISIIEIDEV DGEHTFEVLA TNGDTHLGGE DFDNRVINYL
VEEFKKDQGI DLRKDPLAMQ RLKEAGEKAK IELSSSQQTE VNLPYITADA TGPKHLAIKL
TRAKLESLVE DLVKNSLNPL KQALADSDLS VGDINDIILV GGQTRMPLVQ KYVTEFFGKE
PRKDVNPDEA VAVGAAIQGG VLSGDVKDVL LLDVTPLSLG IETMGGVMTA LIEKNTTIPT
KKSQTFSTAE DNQSAVTVHV LQGERKQSSG NKSLGQFNLE GIRPAARGVP QIEVTFDLDA
DGILHVSAKD KDTGKEQKIT IKASSGLSDE EVEKMVADAE ANKEADKKFE ELIQARNQAD
GMVHATRKQL EEVGDALSAE DKAPIEEALS ALETAVKGED KAEIEAKTQE LIQASSKLME
AAQAQQAAAG GAEGAEQQAS SGQANDDVVD AEFEEVKDDD KK