ID A0A1V2QMA9_9PSEU Unreviewed; 584 AA.
AC A0A1V2QMA9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=HSP90 family protein {ECO:0000313|EMBL:ONI89387.1};
GN ORFNames=ALI22I_15250 {ECO:0000313|EMBL:ONI89387.1};
OS Saccharothrix sp. ALI-22-I.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI89387.1, ECO:0000313|Proteomes:UP000188617};
RN [1] {ECO:0000313|EMBL:ONI89387.1, ECO:0000313|Proteomes:UP000188617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI89387.1,
RC ECO:0000313|Proteomes:UP000188617};
RX PubMed=28087533;
RA Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA Kuske C.R.;
RT "Polysaccharide degradation capability of Actinomycetales soil isolates
RT from a semi-arid grassland of the Colorado Plateau.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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:ONI89387.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MTQP01000056; ONI89387.1; -; Genomic_DNA.
DR RefSeq; WP_077006312.1; NZ_MTQP01000056.1.
DR AlphaFoldDB; A0A1V2QMA9; -.
DR STRING; 1933778.ALI22I_15250; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000188617; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF26; HEAT SHOCK PROTEIN (HSP90 FAMILY)-RELATED; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 2.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000188617}.
SQ SEQUENCE 584 AA; 64551 MW; 74D3B0CD7E765697 CRC64;
MAHTFGVDLR GIIDLLSHHL YSSPRVYARE LLQNAVDAIT ARRALQPDAP GEVVIEPVGS
SGGTFRISDT GIGLTEREVH DLLSTLGRTS KRDDLGFARQ GFLGQFGVGL LSAFLVAERI
RLVSRSATGG PAVRWTADAA GNYEVEVDED ARVDIGTTIE LVPHRDSEHW LEQDVVRALV
TEYGELLPVT VRIGDEVITH GELPWTEDAL AYGEKVLGVR PFDAIPVEVP TVGLKGVAYV
LPRGVHPGAR QSHRVYLKRM LVGDTIEGLL PEWAYFVRCV VDSTSLRPTA SREALYQDET
LLAVREELGR QVRDWLVRLD ATDPDRTRAL LDAHHLGIKS LARVDDEMLR LVERWLPFET
TDGPQSLRQF RRKHGVIAHV PDVDEFRQLA PVAHAQGMGL VNAGYAYDAE IMERLVALDG
PTAARRVAPS EVLAALGDPD PELERAMRER LVQAKDVLER HDCDAVPRDF DPGSLPALLV
TNVEAERKRD AQQVGEQADP LWAELLGSLV ESSSGAAQRL VLNCRNPLVR RLAQLTDPAL
VELTVESLYV HALLQARRPM RPKDTAALNR SFLELLDRAV GDHL
//
