DNAK_MANSM
ID DNAK_MANSM Reviewed; 636 AA.
AC Q65U55;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 100.
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}; OrderedLocusNames=MS0898;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU37505.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016827; AAU37505.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041639656.1; NC_006300.1.
DR AlphaFoldDB; Q65U55; -.
DR SMR; Q65U55; -.
DR STRING; 221988.MS0898; -.
DR EnsemblBacteria; AAU37505; AAU37505; MS0898.
DR KEGG; msu:MS0898; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000607; 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..636
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225976"
FT REGION 599..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..620
FT /note="Polar residues"
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 636 AA; 68453 MW; 8C223E995CEC20CF CRC64;
MGKIIGIDLG TTNSCVAVMD GDKPRVIENA EGERTTPSII AYTQDNEVLV GQPAKRQAVT
NPKNTLFAIK RLIGRRFEDQ EVQRDVNIMP FQIIKADNGD AWVDVKGDKL APPQISAEVL
KKMKKTAEDF LGETVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
LDKGKGNQTI AVYDLGGGTF DLSIIEIDEV GGEKTFEVLA TNGDTHLGGE DFDNRVINYL
VDEFKKEQGV DLRNDPLAMQ RLKEAGEKAK IELSSAQQTD VNLPYITADA TGPKHLNIKL
TRAKLEALVE DLVARSMEPV KVALSDAGLS VSQIDDVILV GGQTRMPLVQ QKVAEFFGKE
PRKDVNPDEA VAVGAAVQGG VLAGNVTDVL LLDVTPLSLG IETMGGVMTT LIEKNTTIPT
KKSQVFSTAE DNQSAVTIHV LQGERKQASA NKSLGQFNLE GINPAPRGMP QIEVTFDIDA
DGIIHVSAKD KGTGKEQQIT IKASSGLSDE EIQQMVRDAE ANAEADRKFE ELVQARNQAD
ALVHSTRKQL TEAGDKLSAD DKAPIEKAVN ELEAAAKGED KAEIEAKIQA LIQVSEKLMQ
AAQQQAQADA GAQQAQGNNG GDDVVDAEFE EVKDNK