DNAK_SOLM1
ID DNAK_SOLM1 Reviewed; 637 AA.
AC C4XQ63;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=DMR_17370;
OS Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1)
OS (Desulfovibrio magneticus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Solidesulfovibrio.
OX NCBI_TaxID=573370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700980 / DSM 13731 / RS-1;
RX PubMed=19675025; DOI=10.1101/gr.088906.108;
RA Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N.,
RA Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H.,
RA Matsunaga T.;
RT "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed
RT common gene clusters in magnetotactic bacteria.";
RL Genome Res. 19:1801-1808(2009).
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; AP010904; BAH75228.1; -; Genomic_DNA.
DR RefSeq; WP_015860427.1; NC_012796.1.
DR AlphaFoldDB; C4XQ63; -.
DR SMR; C4XQ63; -.
DR STRING; 573370.DMR_17370; -.
DR PRIDE; C4XQ63; -.
DR EnsemblBacteria; BAH75228; BAH75228; DMR_17370.
DR KEGG; dma:DMR_17370; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_7; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000009071; 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..637
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000205185"
FT REGION 593..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 196
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 637 AA; 68550 MW; CCC2A65DD37B9CA6 CRC64;
MGKIIGIDLG TTNSCVYVME GKDPKCVTNP EGGRTTPSIV AFTKERLVGE IAKRQAVTNP
ERTIFAIKRL MGRRYDAPEV KHWLEHCPYK IVEGQGGDAY VEVEGKKYSP AEISAIILGK
LKKDAEAYLG EPVTEAVITV PAYFNDAQRQ ATKDAGRIAG LEVKRIINEP TAASLAYGFD
KKANEKIAVF DLGGGTFDIS ILEVGDNVVE VRATNGDTFL GGEDFDHRVI SYLVDEFKKE
NGIDLSQDRM ALQRLKEAGE KAKKELSTAM ETEVNLPFIT ADASGPKHMM VKITRGKLES
LVDDLVKRTV EPCRKALADA GLKASDIDEV VLVGGMTRMP LVSKTVQEFF GKEPNRSVNP
DEVVAMGAAI QGGILAGDVK DVLLLDVTPL SLGIETLGGV FTKLIERNTT IPTRKSQVFT
TAADNQPSVS IHVLQGERPM ANDNMTLGRF ELTGLPPAAR GIPQIEVTFD IDANGIVNVS
AKDTGTGKEQ SIRITASSGL SEADIQKLIK DAESHAEDDK KKQALIEIRN QADTLVYTTE
KSLAELGEKI DGVTRGEIEA KLNNVKETLK GEDADAIKRA TDDLSQASHK LAEKLYQQKA
EEGGQPGGPQ AGAAGGQPGA KAGGDDDVVD ADYTEVK