ID A0A0D0JLT3_9NOCA Unreviewed; 487 AA.
AC A0A0D0JLT3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Chaperone protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=RU01_18490 {ECO:0000313|EMBL:KIQ11787.1};
OS Rhodococcus sp. MEB064.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1587522 {ECO:0000313|EMBL:KIQ11787.1, ECO:0000313|Proteomes:UP000032087};
RN [1] {ECO:0000313|EMBL:KIQ11787.1, ECO:0000313|Proteomes:UP000032087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEB064 {ECO:0000313|EMBL:KIQ11787.1,
RC ECO:0000313|Proteomes:UP000032087};
RA Perisin M.A., Vetter M., Gilbert J.A., Bergelson J.;
RT "16Stimator: statistical estimation of ribosomal gene copy numbers from
RT draft genome assemblies.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KIQ11787.1}.
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DR EMBL; JXQS01000053; KIQ11787.1; -; Genomic_DNA.
DR RefSeq; WP_042576047.1; NZ_JXQS01000053.1.
DR AlphaFoldDB; A0A0D0JLT3; -.
DR Proteomes; UP000032087; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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; PTHR42749; CELL SHAPE-DETERMINING PROTEIN MREB; 1.
DR PANTHER; PTHR42749:SF1; CELL SHAPE-DETERMINING PROTEIN MREB; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT REGION 325..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 49858 MW; 95137351E9F8740D CRC64;
MTSVLGVSVG TSAVRLARPV HGLRAGVQAA FRHRAIDTTF DQAEQLAAES IGVILADPAD
PESVSATGVA YRDDAQAGAV ARAMARQHIV NYRLVPEVHA AVEFLRSTGD LDGLHTVALY
DLGSSGLSVT VVDLDDGRVL ASQRSFDVSG NMFDATIRDS QISRQQSGLD DVDGREFELR
CRVAKEQLSS SGAVCLPGIG GLILLSREAF ESMVAVPVEQ SARLTREVIA RAGRPVDALV
MIGGGSRIPL VRATLAGWVG LPTITPAEPE LVAAKGAALS ATPVDGSDVP FRAAPVQGPP
EPAVEEPLPE RPLTAPSAAT MAYSDVQERP ASASALPTSD VADPRAAETP SWLSGSGSVA
PERTKRPRLP LVAALGLAVV AAIGLALGYG ATPASTADES PAEPAAVTTS SSSTTVPPTT
STRARSTTAT PTTTIAPPPP VVEAPAPVEE APEAPAPAPY VPPTIPGLPG VQLPPGIQIP
PGLIPGF
//
