DNAK_GLOVI
ID DNAK_GLOVI Reviewed; 638 AA.
AC Q7NDH1;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=glr4264;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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; BA000045; BAC92205.1; -; Genomic_DNA.
DR RefSeq; NP_927210.1; NC_005125.1.
DR RefSeq; WP_011144248.1; NC_005125.1.
DR AlphaFoldDB; Q7NDH1; -.
DR SMR; Q7NDH1; -.
DR STRING; 251221.35214838; -.
DR PRIDE; Q7NDH1; -.
DR EnsemblBacteria; BAC92205; BAC92205; BAC92205.
DR KEGG; gvi:glr4264; -.
DR PATRIC; fig|251221.4.peg.4293; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_3; -.
DR InParanoid; Q7NDH1; -.
DR OMA; AYTKNQD; -.
DR OrthoDB; 161217at2; -.
DR PhylomeDB; Q7NDH1; -.
DR Proteomes; UP000000557; 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 Reference proteome; Stress response.
FT CHAIN 1..638
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078466"
FT REGION 598..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 638 AA; 68270 MW; 4A1B1C1C30A3B6D2 CRC64;
MGKVVGIDLG TTNSVVAVLE GGQPTVIANA EGSRTTPSVV AFTKNHDRLV GQLARRQAVL
NPENTFYSVK RFIGRKYDEI TDEAKQVAYR VVRDGSNVKL HSTNEDKDFA PEEISALVLR
KLVDDASKYL GEKITQAVIT VPAYFNDSQR QATKDAGRIA GIEVLRIINE PTAAALAYGL
DKKANETILV FDLGGGTFDV SILEVGDGVF EVKSTSGDTH LGGDDFDRRI VDYLADEFKK
LEGVDLRTDR QALQRLTEAA EKAKIELSGV TQTQINLPFI TAGADGAKHL DMSLTRAKFE
SLCADLLRRV EKPVEQALRD AKLSKENIDE VVLVGGSTRI PAVQELVKRI IGKDPNQSVN
PDEVVAVGAA IQAGVLSGEV RDVVLLDVTP LSLGVETLGG VATPIIPRNT TIPTRKSETF
STAADGQTSV EIHVIQGERS MAGDNKSLGR FRLDGIPPAP RGVPQVEVTF DIDANGILSV
TAKDKASGKA QTISITGAST LSKDDVAKMV NEAESFAGED KKRREAVDLK NEADSLAYQA
ERQLTEFGDK VDSSDKSKIE GLIKDLREAL SREDMDKVAS LKADLQQAVY DLSSKLYQQS
APSGAAAGPD EGAPSGSGGT SGTRGGDDVI DAEFTETK