ID A0A0J6E9Y3_9SYNE Unreviewed; 639 AA.
AC A0A0J6E9Y3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 08-NOV-2023, entry version 30.
DE SubName: Full=Molecular chaperone Hsp90 {ECO:0000313|EMBL:KMM17125.1};
GN ORFNames=SYNGFB01_06420 {ECO:0000313|EMBL:KMM17125.1};
OS Synechococcus sp. GFB01.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1662190 {ECO:0000313|EMBL:KMM17125.1, ECO:0000313|Proteomes:UP000035901};
RN [1] {ECO:0000313|EMBL:KMM17125.1, ECO:0000313|Proteomes:UP000035901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GFB01 {ECO:0000313|EMBL:KMM17125.1,
RC ECO:0000313|Proteomes:UP000035901};
RA Guimaraes P.I., Leao T.F., de Melo A.G., Ramos R.T., Silva A., Fiore M.F.,
RA Schneider M.P.;
RT "Draft genome of the picocyanobacterium Synechococcus sp. strain GFB01
RT isolated from a freshwater lagoon of the Brazilian Amazon.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KMM17125.1}.
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DR EMBL; LFEK01000038; KMM17125.1; -; Genomic_DNA.
DR RefSeq; WP_048017405.1; NZ_LFEK01000038.1.
DR STRING; 1662190.SYNGFB01_06420; -.
DR PATRIC; fig|1662190.3.peg.1880; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000035901; 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 CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
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:UP000035901}.
FT DOMAIN 28..179
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 639 AA; 71539 MW; 1B566DB88F3A5A8C CRC64;
MVLQAEQGQI QIHTENIFPI IKKAVYSGHE VFLRELVSNG VDAISKRRMA AMAGDCSEGP
EGRIQIRIDR EAKTLTISDN GIGMTADEVK RYINQVAFSS AEDFLEKYKS ETDAIIGHFG
LGFYSSFMVA KQVELITLSA REGSEAVRWS CDGSPSFRLE GSERSESGTD VILHLMEEEL
EYIEPARIRT LITTYCDFLP VEVQLEGETV NKRQAPXRAN PRELSDNDYI ELYRYLYPFQ
GDPLLWVHLN TDYPYNLQGI LYFPKLSGRA DWEKGEIRLY CNQVFVSDSI KEVVPRYLLP
LRGVIDSPDI PLNVSRSALQ TDRRVRSIGG FVAKKVADRL KQLHRDEPKR YAEIWESLAP
FIKIGAMEDE KFADQVADLV LFGTTAQAQE QPAEGHSLDP IPADHGRAFT TLAGYRSRLS
GDNDKRILYC TDEAGQAGXL ALWKGQGAEV LLADTFIDTQ FIPWLEYRHN ELKFQRVDSE
LDDSLQEKES ELADADGKDA GEKLRELFRG ALGNDKVTIQ VQALKGDSAP AALILLPEQM
RRLNDMGALM EQRLPGLPDH HVLLVNRRHP LVDGLLKLSA GSVITGSGTS SPSQQLASDL
SRHLYEMARL AVGGLEPNEL AGFQQRSAEL MGRLMERGL
//
