ID W0F6C9_9BACT Unreviewed; 627 AA.
AC W0F6C9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Heat shock protein Hsp90 {ECO:0000313|EMBL:AHF16911.1};
GN ORFNames=NIASO_20400 {ECO:0000313|EMBL:AHF16911.1};
OS Niabella soli DSM 19437.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niabella.
OX NCBI_TaxID=929713 {ECO:0000313|EMBL:AHF16911.1, ECO:0000313|Proteomes:UP000003586};
RN [1] {ECO:0000313|EMBL:AHF16911.1, ECO:0000313|Proteomes:UP000003586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19437 {ECO:0000313|Proteomes:UP000003586};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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; CP007035; AHF16911.1; -; Genomic_DNA.
DR RefSeq; WP_025299150.1; NZ_CP007035.1.
DR AlphaFoldDB; W0F6C9; -.
DR STRING; 929713.NIASO_20400; -.
DR KEGG; nso:NIASO_20400; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_2_10; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000003586; 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; IPR019805; Heat_shock_protein_90_CS.
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.
DR PROSITE; PS00298; HSP90; 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:UP000003586};
KW Stress response {ECO:0000313|EMBL:AHF16911.1}.
FT DOMAIN 25..165
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 627 AA; 71169 MW; 66B97E8CE17816C5 CRC64;
MQEKGSISIH TENIFPIIKK FLYSDHEIFL RELVSNAVDA IQKAKRLASL GQFNGEIGAP
LVQVKVDKEA KTITVSDNGI GMTADEIKKY INQIAFSGAE EFMEKFKEAK DASEIIGRFG
LGFYSAFMVA DRVEIQTLSY QPGAEPAQWT CDGSTEFEIS AGSRTTRGTD VILYVNEENK
EFLEEGRIES ILKKYAKFLP VPVQFGTKTE SEPDGEDAEG KPKYKEVEVP NIINTGVPIW
TIAPSELKKE DYLNFYRELY PFSEDPLFWI HLNVDYPFHL TGVLYFPKIK NDIELQRNKI
QLYSRQVFIT DEVKDIVPEF LMLLHGVIDS PDIPLNVSRS FLQSDSNVKK INTYITRKVA
DKLAELFKSD RKSYEEKWGD IGIFVKYGSI SDPKFWERAK DFVLLENTKK EYFTLSEYSE
KVAPTQTDKD GNVVYLYTPN PERQDGYIQA ANKKGYDVLL MNSPLDNHFI SHLERDLEKT
QIKRVDADVL EKLIDKGEEV ASNLSEEQTK EIKDIYEKAI TQPGMEVSVE NLSPEAMPVT
VTMDEFMRRM KDMAALGGGM SFYGSMPDRY KVAVNANHPL ATKILSETND DTRKALAQQA
FDLALLAQGM LTGAALTSFV ERSMKMI
//