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Database: UniProt
Entry: G7WQC8_METH6
LinkDB: G7WQC8_METH6
Original site: G7WQC8_METH6 
ID   G7WQC8_METH6            Unreviewed;       619 AA.
AC   G7WQC8;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Chaperone protein DnaK {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   OrderedLocusNames=Mhar_2126 {ECO:0000313|EMBL:AET65481.1};
OS   Methanothrix harundinacea (strain 6Ac) (Methanosaeta harundinacea).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=1110509 {ECO:0000313|EMBL:AET65481.1, ECO:0000313|Proteomes:UP000005877};
RN   [1] {ECO:0000313|EMBL:AET65481.1, ECO:0000313|Proteomes:UP000005877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6Ac {ECO:0000313|EMBL:AET65481.1,
RC   ECO:0000313|Proteomes:UP000005877};
RX   PubMed=22590603; DOI=10.1371/journal.pone.0036756;
RA   Zhu J., Zheng H., Ai G., Zhang G., Liu D., Liu X., Dong X.;
RT   "The genome characteristics and predicted function of methyl-group
RT   oxidation pathway in the obligate aceticlastic methanogens, Methanosaeta
RT   spp.";
RL   PLoS ONE 7:E36756-E36756(2012).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000256|HAMAP-Rule:MF_00332}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00332, ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; CP003117; AET65481.1; -; Genomic_DNA.
DR   RefSeq; WP_014587657.1; NC_017527.1.
DR   AlphaFoldDB; G7WQC8; -.
DR   STRING; 1110509.Mhar_2126; -.
DR   GeneID; 12511300; -.
DR   KEGG; mhi:Mhar_2126; -.
DR   PATRIC; fig|1110509.7.peg.2359; -.
DR   HOGENOM; CLU_005965_2_4_2; -.
DR   OrthoDB; 9944at2157; -.
DR   Proteomes; UP000005877; 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; 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; 2.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00332}; Chaperone {ECO:0000256|HAMAP-Rule:MF_00332};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00332}; Reference proteome {ECO:0000313|Proteomes:UP000005877}.
FT   REGION          582..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   619 AA;  67065 MW;  DB23A3D105F8CD02 CRC64;
     MSKIIGIDLG TSNSAAAVLI GGKPTMIPSA EGTSIVAGGK AFPSYVAFTK DGQRLVGEPA
     RRQAATNPEG TITGIKRKMG QDYRVEVYGK SYTPQDISSF ILRKIKDDSE AFLGEKVEKA
     VITVPAYFND NQRQATKDAG TIAGLDVVRI INEPTAAALA YGMDKEGEAT LMVFDLGGGT
     LDVTIMEAGE GVFEVKSTSG DTQLGGRDMD EILTNYVVER YRQESGIDLK GDRMAMQRLR
     EAVEIAKIEL SSVLQTTINL PYITADQTGP KHLEMTITRA KLEELIKEVL ERCRNPMIQA
     IRDAKLDKSG IDKIVLVGGP TRMPAVRKFV TEFMGKEPEG GVDPMECVAI GAAVQGGVLG
     GEVKDILLLD VTPLSLGIET LGGVATKLIE RNTTIPTRKS QIFTTAADNQ TTVEIHVLQG
     ERPLAKDNTS LGRFTLSGIP PAPRGIPQIE VAFDIDANGI LNVSAKDLAT GKEQAITISA
     PHKLSQNEIE RKIREAEQHA YEDTRRKEEI EAKNQAETLV YTAEKTLKDA GEVVTADQKE
     KIERAIGEAK EALAGGDIAK IKEKTEALQN AIYELSTAMY QRAAEQQQRE QEKQQQSQGG
     PTASGETIDA DFEVVNDKR
//
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