ID A0A173LPM3_9ACTN Unreviewed; 603 AA.
AC A0A173LPM3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Chaperone protein HscA {ECO:0000313|EMBL:ANI93883.1};
GN ORFNames=BJL86_3124 {ECO:0000313|EMBL:ANI93883.1};
OS Dietzia timorensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC Dietzia.
OX NCBI_TaxID=499555 {ECO:0000313|EMBL:ANI93883.1, ECO:0000313|Proteomes:UP000186104};
RN [1] {ECO:0000313|EMBL:ANI93883.1, ECO:0000313|Proteomes:UP000186104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ID05-A0528 {ECO:0000313|EMBL:ANI93883.1,
RC ECO:0000313|Proteomes:UP000186104};
RA Wu X.;
RT "Complete genome sequence of a saline-alkali tolerant type strain Dietzia
RT timorensis ID05-A0528T.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR EMBL; CP015961; ANI93883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A173LPM3; -.
DR STRING; 499555.BJL86_3124; -.
DR KEGG; dtm:BJL86_3124; -.
DR Proteomes; UP000186104; Chromosome.
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:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322}.
FT REGION 377..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 62009 MW; 48BE76DD7E394914 CRC64;
MAGGWKLAID FGTSNTAAAH TSPRSGEVEP VALTHGGNLL PSAVYAEPSG AIAAGAAAAN
RAEGDASGFM PFPKRAIGSN TVRLRDREVA VVDLFAAVLH VAYRSACRKH GDIPPEKVVL
THPEAWDDSA LLALKEASRR AGIDPDSLLF VSEPRAAATY YTTTSNLQPG ERIGVFDFGG
GTLDIAILEA VPGGDFRILA ARGDNGIGGR NFDALIREWV FSQLDDSNPP LAEHLRSGAS
TSSLRALDIS VRAAKEVLSE EASASISVST SVGAETLLLT RAEFDGLIGA EIQRAVELTW
QAMSDGGVAQ NGLRALYLTG GSSQVPLIHS RLSEFAPVAT LDDPKTVVAQ GALLGALRVE
QMQPPAQSED YNFAQHGFAP APALDGSGPA QGPQQNVAGP HQAASPQAGS GSKKKSGGLS
GGKLAAVIGA AVVAVAVAVG GTYFLTSGGF GGAESFVTDP VGEGPDGITA ALPEAMRNVT
TCEAKEQTAP SGKTVPGAQC MADNEAGALG EKSSYSFPAY VDEVAAISLV DEQRADAANP
ESRIKVTEMT SDSGNVLGFI QEGQGFLSLL VVNTANHLIL DSFFPGDVAA AETLWESSGF
AAM
//