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Database: UniProt
Entry: A0A1Q5J4E5_9ACTN
LinkDB: A0A1Q5J4E5_9ACTN
Original site: A0A1Q5J4E5_9ACTN 
ID   A0A1Q5J4E5_9ACTN        Unreviewed;       627 AA.
AC   A0A1Q5J4E5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Heat-shock protein Hsp90 {ECO:0000313|EMBL:OKJ64008.1};
GN   ORFNames=AMK29_18090 {ECO:0000313|EMBL:OKJ64008.1};
OS   Streptomyces sp. CB02261.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703940 {ECO:0000313|EMBL:OKJ64008.1, ECO:0000313|Proteomes:UP000186742};
RN   [1] {ECO:0000313|EMBL:OKJ64008.1, ECO:0000313|Proteomes:UP000186742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB02261 {ECO:0000313|EMBL:OKJ64008.1,
RC   ECO:0000313|Proteomes:UP000186742};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKJ64008.1}.
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DR   EMBL; LIVX01000005; OKJ64008.1; -; Genomic_DNA.
DR   RefSeq; WP_073814160.1; NZ_LIVX01000005.1.
DR   AlphaFoldDB; A0A1Q5J4E5; -.
DR   OrthoDB; 9802640at2; -.
DR   Proteomes; UP000186742; 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; 1.
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}.
SQ   SEQUENCE   627 AA;  68255 MW;  D7897013A033BB02 CRC64;
     MTLPDTAPNP DGADRTFQVD LRGLVDLLSH HLYSSPRVYL RELLQNAVDA LTARHALEPG
     ASADDFGIRL HADGSVVRVE DDGVGLTEAD VHTFLATIGR SSKRAAGGSP DEPVRGWGRI
     EEQRGDFIGQ FGIGLLSCFL VADEIHVLSR SARTPDAPAV EWRGRGDGSY TVRTLPASAR
     PRPGTTVTLT PRADADEWTR PVKVHALARH FGSLLRHPVT FDDGSGGPGV PVNPEPAPWA
     RTFPTPGSRS RALAAYGEKV FGFTPLDTIE LDLPAVGLKG IACVLPEAVP AGRRHGHRVH
     VKGMLLSEQA EEILPEWAFF VRCVIDAESL RPTASRESLY EDATLAAVRD ALAERLRAWI
     SRAAASDPDL LARFLQTHHL AVKSLAVHDD EILRMLLPWL PFETTDGHTT LDEFARTHRT
     VLVTSSVEEF RQVAAIASAA GLGVVNGGYT YDRELVHRLP EVRPEVNVAD LDPATLTAHL
     DPVDRETELA AAAYLARARD ALAVFDCDVA LRTFQPASAP ALLVDSREAR HERTRSQLAR
     EQEGGLWGDI LGALRQEAPR AQLILNQLNP LVRTAVAIDE PELARTSAEA LYGQAALLSR
     RPLRPAESSL INRSFLDLLA HALRKDS
//
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