ID A0A0M1JDM6_9GAMM Unreviewed; 544 AA.
AC A0A0M1JDM6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Molecular chaperone DnaK {ECO:0008006|Google:ProtNLM};
GN ORFNames=TI05_13360 {ECO:0000313|EMBL:KOR30835.1};
OS Achromatium sp. WMS3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Achromatium.
OX NCBI_TaxID=1604836 {ECO:0000313|EMBL:KOR30835.1, ECO:0000313|Proteomes:UP000036918};
RN [1] {ECO:0000313|EMBL:KOR30835.1, ECO:0000313|Proteomes:UP000036918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMS3 {ECO:0000313|EMBL:KOR30835.1};
RX PubMed=26322031; DOI=10.3389/fmicb.2015.00822;
RA Mansor M., Hamilton T.L., Fantle M.S., Macalady J.L.;
RT "Metabolic diversity and ecological niches of Achromatium populations
RT revealed with single-cell genomic sequencing.";
RL Front. Microbiol. 6:822-822(2015).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOR30835.1}.
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DR EMBL; JXSO01000377; KOR30835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M1JDM6; -.
DR PATRIC; fig|1604836.3.peg.2607; -.
DR Proteomes; UP000036918; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10170; HSP70_NBD; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF513; SLR0086 PROTEIN; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS00329; HSP70_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000036918}.
SQ SEQUENCE 544 AA; 60340 MW; D62FC90F2DBBCCBD CRC64;
MPLAMDFGTC NTVLARWQPS SRQVKTLQIG GPTRIYNYLI PGTQKRQLSA VIPSLIHYGS
RVDIAHAGKT IGAQVENVGL ATDRGTFRWM KLDLLKGNNR ARRINGQLIT PRQAAESFIE
QVLFAAAGNE DEDLVITLPI ESFDHYANWL QNTTSRVFPG RIRMLDEATA CILGYGTRVR
EGQVYIVFDF GGGTLDISVV KILELDADQT RPCIVLGRSG EEIGGALVDQ WLLKELAQAQ
GLNSDTIGAI GSDLLHAIEN AKVKLSDGIE QVKVEHFDGA KRISHTFSVT DLRHVLEADR
VSLGNRNFYR LISLTLERAL TQAQERYATK RSDIRAVFMV GGSSLLLGVA DLVKNLLPDC
PVHCENPFEA IARGACRYAG GNINLTLVHD YCLRAWDSER SEYSLIPIIP KGTHYPTERP
ISIKYINGAC EGSEYLSLVV IERSEMVRPE GLWEIIGGRL QRRTTDWHTD NALKELNPAD
REFIHANPSC IAGARRFIAS FGVDANKRLT ISLKDLNPEG NSTIQFSDGK HLPLPIQDLP
FVKL
//