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Database: UniProt
Entry: A0A0T1SL93_9ACTN
LinkDB: A0A0T1SL93_9ACTN
Original site: A0A0T1SL93_9ACTN 
ID   A0A0T1SL93_9ACTN        Unreviewed;       698 AA.
AC   A0A0T1SL93;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Heat-shock protein {ECO:0000313|EMBL:KQX55378.1};
GN   ORFNames=ASD33_31625 {ECO:0000313|EMBL:KQX55378.1};
OS   Streptomyces sp. Root1304.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1736450 {ECO:0000313|EMBL:KQX55378.1, ECO:0000313|Proteomes:UP000051136};
RN   [1] {ECO:0000313|Proteomes:UP000051136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1304 {ECO:0000313|Proteomes:UP000051136};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQX55378.1, ECO:0000313|Proteomes:UP000051136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1304 {ECO:0000313|EMBL:KQX55378.1,
RC   ECO:0000313|Proteomes:UP000051136};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
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:KQX55378.1}.
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DR   EMBL; LMEP01000007; KQX55378.1; -; Genomic_DNA.
DR   RefSeq; WP_056557567.1; NZ_LMEP01000007.1.
DR   AlphaFoldDB; A0A0T1SL93; -.
DR   STRING; 1736450.ASD33_31625; -.
DR   Proteomes; UP000051136; 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   Gene3D; 3.40.50.11980; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   InterPro; IPR021869; RNase_Zc3h12_NYN.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   Pfam; PF11977; RNase_Zc3h12a; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051136}.
FT   DOMAIN          518..648
FT                   /note="RNase NYN"
FT                   /evidence="ECO:0000259|Pfam:PF11977"
FT   REGION          678..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   698 AA;  76616 MW;  83247C8765BC1032 CRC64;
     MTATGIDFGT TNSVVAQWLG DDVDVLSLDA HHIDADWRHP GFEYLFPSVV GMSSLRRGAL
     FGWEAKLRSE EAAEACKRLL KSDEYVTIHG RRFAATTVAA GVFQAMRKGA EHNLTAIDQA
     VITVPANATG AARYRTRAAA RFAGIEVLAL LNEPTAAAIS YVHELREART ILVFDWGGGT
     IDVTVLDYQD GFFEELASRG VTELGGLEID RRLRDLVLER APARSAWTPA QERQFGLDVE
     RSKIRLSSEE SVTIRTPDGD TVEVWQGELE DAITDLVDRA LAPVQQCLTD LHMAPLDVDA
     VLMIGGTSQI PSVRAAVAEV MQQQPVEVDL CDPMTAVARG ASIAAAVLSG EADGVIQVAT
     SHALGTVVTD DTGQRAFSQI IPRNSPLPWK ERKSYTPRRD NARSLAVEIW EGDPDRPLDH
     ADNVQLTDLR LIYQNPRVRE DSRFLLEYTY DTNGLLHVKA TLERTGEEVL NEEIKSFSSG
     GPTPAVRKEL DDLLAGNTVT TLLPTQTRRR SAGSASKALV VDGSNLAWIG RSPRRPGVYG
     RDDRPSYAQL LSARDALASR YPDAVLHVVV DATFRHKVAE EERAAVDSAL ATGNLIQPPA
     GTEGKGDALV TAIAQDTDGI VVTNDNYTEL QGRYPWLRDK ERVLGATLTQ GMWVFTPRTC
     VPPRHRIVRA ETFQQSRALI PPSPHPLPEF RYHRPHEE
//
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