ID C4Z995_AGARV Unreviewed; 696 AA.
AC C4Z995;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ACR75317.1};
GN OrderedLocusNames=EUBREC_1573 {ECO:0000313|EMBL:ACR75317.1};
OS Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835
OS / VPI 0990) (Eubacterium rectale).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Agathobacter.
OX NCBI_TaxID=515619 {ECO:0000313|EMBL:ACR75317.1, ECO:0000313|Proteomes:UP000001477};
RN [1] {ECO:0000313|EMBL:ACR75317.1, ECO:0000313|Proteomes:UP000001477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / LMG 30912 / VPI
RC 0990 {ECO:0000313|Proteomes:UP000001477};
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; CP001107; ACR75317.1; -; Genomic_DNA.
DR RefSeq; WP_012742416.1; NC_012781.1.
DR AlphaFoldDB; C4Z995; -.
DR STRING; 515619.EUBREC_1573; -.
DR PaxDb; 515619-EUBREC_1573; -.
DR KEGG; ere:EUBREC_1573; -.
DR HOGENOM; CLU_006684_3_2_9; -.
DR Proteomes; UP000001477; 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; 2.
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 Stress response {ECO:0000313|EMBL:ACR75317.1}.
FT REGION 461..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 79751 MW; BA5E5EE1BA6282C5 CRC64;
MTEKHGNLSI DSDNLFPIIK KWLYSDHDIF YRELISNGCD AITKLKKLDM MGEYSLPADY
KGKIQVLVNP DEKTIKIIDN GLGMTADEVE EYISRIAFSG ATDFIEKYKD KSNDDQIIGH
FGLGFYSAFM VADEVTIDTL SYKEGSTPVH WSCDGGTEYN MEDGDMDDVG TEITLYLNDD
CLEFANEYRA REVIEKYCSF MPTEIYLAKE NAPEEYETID KADKRDTDTV IEEIHEDAKY
EEKENDKGEK EQVEVSPAKD QLKIVKRPVP LNDTTPLWIK SPNECTDEEY KEFYRKVFLD
YKEPLFWIHL NMDYPFNLKG ILYFPKINTE YDSIEGTIKL YNNQVFIADN IKEVIPEFLM
LLKGVIDCPD LPLNVSRSAL QNDGFVKKIS EYITKKVADK LIGMCKTDKE AYEKYWDDIS
PFIKFGCLKD EKFCDKINDY ILFKDINDKY QTLPELLAPV AEDEKSDAES ADASDDTKKA
DNTDANASDE NKEPEKNTVY YVTDVVQQGQ YIKLFKEQGM NAVILDHNID TSFITQLEQR
NDHYKFMRID ADLTESLKDE SGADLTEATT TLSEVFKKAL NNDKLTVKVE NLKNADVASV
LTLSEQGRRM QDMMKMYAAG GMGGMDPSMF AADQTLTLNA NNELVKYILD NKDSEHVPMF
AEQLYDLAML SNQPLSVDQM TKFVKRSNDI MLLLTK
//
