ID A0A369B6J6_9FIRM Unreviewed; 636 AA.
AC A0A369B6J6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:RCX17140.1};
GN ORFNames=DFR58_10833 {ECO:0000313|EMBL:RCX17140.1};
OS Anaerobacterium chartisolvens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerobacterium.
OX NCBI_TaxID=1297424 {ECO:0000313|EMBL:RCX17140.1, ECO:0000313|Proteomes:UP000253034};
RN [1] {ECO:0000313|EMBL:RCX17140.1, ECO:0000313|Proteomes:UP000253034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27016 {ECO:0000313|EMBL:RCX17140.1,
RC ECO:0000313|Proteomes:UP000253034};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCX17140.1}.
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DR EMBL; QPJT01000008; RCX17140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369B6J6; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000253034; Unassembled WGS sequence.
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:UP000253034}.
FT REGION 214..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 73613 MW; 32FB1F63C5211251 CRC64;
MALENGSISI NTENIFPIIK KWLYSEKDIF IRELVSNASD AISKLKKLAS IGEAEIGEDN
RYLIRVVVNK DENTIKIIDN GIGMTEDEVK KYINQIAFSG AKDFIEKYKD KTDEGQIIGH
FGLGFYSAFM VAETVQIDTL SFQKGAKAVK WVSSEGTEYE MDESELDTRG TVITLHMAED
SLEFLDEYKM REILVKYFSF LPYELYLEDS AKKEEPVKDD ADKENAEGEE KKEKEAPKPL
NDISPLWLKA PKDCTDEEYK SFYTKVFHDF NEPLFWIHLN MDYPFNLKGI LYFPKLKHEF
ETNEGQIKLY YNQVFVADNI KEVIPEFLML LKGTIDCPDL PLNVSRSFLQ NDGYVSKISS
HITKKVADKL SALYENEREN YNKYWDDINP FVKYGCLKEE KFFDRVKDIV IYKTTNDDYA
TLKDYLERNK EKHENKVFYI TDEKQQAQYI KLFKDNEMEA IKLTTMIDSH FISFLETKES
GVKFSRIDSD LSDSLKDTEA VSVDAAQKEG LEKLFKEVME DDKLKVQVES LKASAVPGMI
LLSEQSRRMQ EMSKMFGGAD MSYMFPKEET LVLNSNNGLV QFILEAKDDE ARKDDVKMIC
QQVHDLAMMG HKQLEPEAMT RFIERSSQIM LKLAGK
//
