ID K9ST38_9SYNE Unreviewed; 634 AA.
AC K9ST38;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Molecular chaperone of HSP90 family {ECO:0000313|EMBL:AFY73300.1};
GN ORFNames=Syn7502_01197 {ECO:0000313|EMBL:AFY73300.1};
OS Synechococcus sp. PCC 7502.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1173263 {ECO:0000313|EMBL:AFY73300.1, ECO:0000313|Proteomes:UP000010385};
RN [1] {ECO:0000313|EMBL:AFY73300.1, ECO:0000313|Proteomes:UP000010385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7502 {ECO:0000313|EMBL:AFY73300.1,
RC ECO:0000313|Proteomes:UP000010385};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Synechococcus sp. PCC 7502.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; CP003594; AFY73300.1; -; Genomic_DNA.
DR RefSeq; WP_015167959.1; NC_019702.1.
DR AlphaFoldDB; K9ST38; -.
DR STRING; 1173263.Syn7502_01197; -.
DR KEGG; synp:Syn7502_01197; -.
DR PATRIC; fig|1173263.3.peg.1235; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_2_3; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000010385; Chromosome.
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; SSF110942; HSP90 C-terminal domain; 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:UP000010385}.
FT DOMAIN 25..181
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 634 AA; 72325 MW; F353A3C37A1EE91A CRC64;
MLEQGTISIH TENIFPIIKK ALYSERDIFL RELISNGVDA TSKLKMVAYA GETTAEVPAP
EISITVDKEK KIITVTDNGI GMTADEVKKY INQVAFSSAE EFIQKYTNTS NDSQQQIIGH
FGLGFYSAFM VAAQVEIDTL SYKDGAEAVH WFCDGSTAFT LSRSDRTTVG TTITLKLQED
AEEFLEVFEL RRIIRNYCDF IPVPIKLNDE VVNKQTALWN QSPSSLTKED YLEFYRYLYP
FQEDPLFWIH LNTDYPFIIK GILYFPKLKA DIDPNKGQIK LFCNQVFISD NCEEVIPKFL
LPLRGVIDSS DIPLNVSRSF LQGDRKVRKI QDYIAKKVGD HLSNLYADQR EEFLKCWQDI
SLFMKFGAMN SDKFYSQVKE ILVYPTTFID SEAKSEYGNY TTLQNYLERN KEQHQNQVFY
TSDPVAQATY IDLHKAQGLE VITLDSFIDS HFIHFLEREF SDVKFSRVDS ELSDRLINQD
AKTELVDPKT NKTKSDQLQE IFRAALHNPK LVIRTEALKY EDLASAPPAM ILLPESARRM
QEMAALMQQT NAPFPEDHIL LVNTSHPLME NLLSLDHSVI LSAAGKPSES KELANLICNH
VYDLALIAQK GFDANGMKAF LDRSNKLLLH LAKA
//
