ID A0A078KR83_9FIRM Unreviewed; 612 AA.
AC A0A078KR83;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Molecular chaperone of HSP90 family {ECO:0000313|EMBL:CDZ23675.1};
GN ORFNames=CCDG5_0544 {ECO:0000313|EMBL:CDZ23675.1};
OS [Clostridium] cellulosi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=29343 {ECO:0000313|EMBL:CDZ23675.1, ECO:0000313|Proteomes:UP000032431};
RN [1] {ECO:0000313|Proteomes:UP000032431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5 {ECO:0000313|Proteomes:UP000032431};
RA Wibberg D.;
RL Submitted (JUL-2014) 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; LM995447; CDZ23675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078KR83; -.
DR STRING; 29343.CCDG5_0544; -.
DR KEGG; ccel:CCDG5_0544; -.
DR PATRIC; fig|29343.3.peg.562; -.
DR HOGENOM; CLU_006684_3_2_9; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000032431; 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; PF02518; HATPase_c; 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.
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:UP000032431}.
FT DOMAIN 27..176
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF02518"
SQ SEQUENCE 612 AA; 71406 MW; 7A3529204E1D45F8 CRC64;
MKTGKISVKA ENMLPIIKKW LYSDKDIFLR EAVSNASDAI FKFERLVVFG EAQKAENEKM
HIDVSVNKEK GTLKISDTGI GMTEDEVVKY IAQVAFSGAV DFIEKYKDIA DKNNIIGHFG
LGFYSVFMVS DYVELDTLSY KKDAKPVKWI CDGGSDYQIG EGERTERGTT LTLHISKDSE
EFLDTARIRE ILRKYCSFIS YEITLTDECQ EKKEDEKPEI INNISPLWLK NPKDCTDDEY
KKFYKDVFHD YMDPLFWIHL NVDYPFQLKG IIYFPRLREN LDLMEMGQIK LYYNQVFVAD
NIKEILPEFL VVLKGVIDCP DIPINVSRSF LQNDGSVAKI SNLISKKVSD KLHSIFKENR
EEYQKYWDDI NLLIKFGCIK DSKFFDRMKD TILFKTTDGK YLTLSEYLEG QKDKDKKTVY
YTDNKAQQSV NIDMFKRNGI EVVEFRGPID QRFAQELEMR EEGLKFSSVV SELPDDLVSG
KAANEDDVKV LSEIFRKALG KDKLEVKAEY FKNENTPAIL TLSEQSKRFA DMVRLYGQDF
AYKPDDEYVI TLNPDHPLIK KVMDMRFDES KKECMNMLCQ QIYDIALMSH RDFSKEEKEK
FIERNYKLLE MI
//