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Database: UniProt
Entry: A0A1E4IUV9_9BURK
LinkDB: A0A1E4IUV9_9BURK
Original site: A0A1E4IUV9_9BURK 
ID   A0A1E4IUV9_9BURK        Unreviewed;       424 AA.
AC   A0A1E4IUV9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Heat-shock protein {ECO:0000313|EMBL:ODU13876.1};
GN   ORFNames=ABS94_25160 {ECO:0000313|EMBL:ODU13876.1};
OS   Variovorax sp. SCN 67-85.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1660152 {ECO:0000313|EMBL:ODU13876.1, ECO:0000313|Proteomes:UP000094461};
RN   [1] {ECO:0000313|EMBL:ODU13876.1, ECO:0000313|Proteomes:UP000094461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA   Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA   Banfield J.F.;
RT   "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT   unravelled with genome-resolved metagenomics.";
RL   Environ. Microbiol. 17:4929-4941(2015).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381}.
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:ODU13876.1}.
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DR   EMBL; MEFM01000031; ODU13876.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4IUV9; -.
DR   Proteomes; UP000094461; 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; cd10231; YegD_like; 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   InterPro; IPR042054; YegD-like.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
SQ   SEQUENCE   424 AA;  45918 MW;  7618EE2D9197A428 CRC64;
     MSSPSSLPTI GIDFGTSNSA VACRVDGAAR LLPIEGAATT LPTAIFFNSE DRTTHFGRDA
     IAQYLSGTEG RLMRSLKSLL GSALMQEKTA IYDGLVSFED IIARFLRELA VRAGRELGQL
     PERVVIGRPV HFVDDDPKRD ERAEESLRVA ARAAGFREIA FQLEPIAAAF DYEQRIAKES
     IVLIVDIGGG TSDFTVVRVG PDRAAREDRS DDVLATSGVH IGGTDFDQRL NLERVMPHFG
     FRHHGPQGRE VPSKVFFELS SWHLINWLYA AKAVRQAKEL RTSYSDTRLH DRLMNVLEER
     HGHRIASAVE AAKIDASVTD AETAIDLDCA ERGLVASLSP ADMAQQLAGP LENVIACAHA
     CVKRAGLRSG DLDAIYLTGG SSALRPFQHA LRKSFAGVNL VEGDLFGGVA TGLACVARTA
     RAAR
//
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