ID G0IVQ9_CYCMS Unreviewed; 627 AA.
AC G0IVQ9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Heat shock protein Hsp90 {ECO:0000313|EMBL:AEL24826.1};
GN OrderedLocusNames=Cycma_1054 {ECO:0000313|EMBL:AEL24826.1};
OS Cyclobacterium marinum (strain ATCC 25205 / DSM 745 / LMG 13164 / NCIMB
OS 1802) (Flectobacillus marinus).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=880070 {ECO:0000313|EMBL:AEL24826.1, ECO:0000313|Proteomes:UP000001635};
RN [1] {ECO:0000313|Proteomes:UP000001635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25205 / DSM 745 / LMG 13164 / NCIMB 1802
RC {ECO:0000313|Proteomes:UP000001635};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Cyclobacterium marinum DSM 745.";
RL Submitted (JUL-2011) 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; CP002955; AEL24826.1; -; Genomic_DNA.
DR RefSeq; WP_014019123.1; NC_015914.1.
DR AlphaFoldDB; G0IVQ9; -.
DR STRING; 880070.Cycma_1054; -.
DR KEGG; cmr:Cycma_1054; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_2_10; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000001635; 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; 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 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:UP000001635};
KW Stress response {ECO:0000313|EMBL:AEL24826.1}.
SQ SEQUENCE 627 AA; 71650 MW; F58C997EC4E4BAA2 CRC64;
MQEKGTISIH TENIFPIIKK FLYSDNEIFL RELVSNSVDA TQKIKRLATL GQYKGELGDL
TIDVNFDKDK KWIKITDRGL GMTAEEIKKY INQIAFSGAS EFVEKFKDAK DANEIIGKFG
LGFYSAFMVA DTVEIDSLSY QEGAEPAKWT CDGSTEFEIS KGTRTERGTE ITLNINSESE
EFLDKFKLQG ILDKYAKFLP VPIRFGTKTE SVEDGVDDKG EKKWKSVEVD NIINTTNPIW
AQSPSELTDE DYLKFYKELY PMSEDPLFWI HLNVDYPFNL TGVLYFPKVK NDFELQRNKI
KLFSRQVFIT DEVKDIVPEF LMLLHGVIDS PDIPLNVSRS FLQADSNVKK INNYITKKVA
DKLGELYKKD RKVYEEKWKD IGLFVKYGMI SEDKFYEKAK NFVLLNNTNG EYFTLDEYQE
KVKPLQTGKD DKLVYLYATD ADKQDTFIQS ANKKDYDVLL MDSPIDSHFI QNIESKLENT
SLKRVDADVV DKLIEKEGGY ENLLSEDQSK KVKEIFEKSI ANQSYSVEVE GASPEEMPVT
ITMDEFMRRM KDMAQNGGGM GFYGAMPDNY KVGINGNHPV IDKILKTEDE EAQLKLAKQA
FDLALVSQGL LTGKALTAFV KRSVDLI
//
