ID D4LF86_RUMC1 Unreviewed; 632 AA.
AC D4LF86;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Chaperone protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE AltName: Full=Heat shock protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE AltName: Full=High temperature protein G {ECO:0000256|HAMAP-Rule:MF_00505};
GN Name=htpG {ECO:0000256|HAMAP-Rule:MF_00505};
GN OrderedLocusNames=RUM_22830 {ECO:0000313|EMBL:CBL18281.1};
OS Ruminococcus champanellensis (strain DSM 18848 / JCM 17042 / KCTC 15320 /
OS 18P13).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=213810 {ECO:0000313|EMBL:CBL18281.1, ECO:0000313|Proteomes:UP000007054};
RN [1] {ECO:0000313|Proteomes:UP000007054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18848 / JCM 17042 / 18P13
RC {ECO:0000313|Proteomes:UP000007054};
RA Pajon A., Turner K., Parkhill J., Bernalier A.;
RT "The genome sequence of Ruminococcus sp. 18P13.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000256|HAMAP-
CC Rule:MF_00505}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239, ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00505}.
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DR EMBL; FP929052; CBL18281.1; -; Genomic_DNA.
DR AlphaFoldDB; D4LF86; -.
DR STRING; 213810.RUM_22830; -.
DR KEGG; rch:RUM_22830; -.
DR PATRIC; fig|213810.4.peg.2172; -.
DR HOGENOM; CLU_006684_3_0_9; -.
DR Proteomes; UP000007054; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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 HAMAP; MF_00505; HSP90; 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; 2.
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, ECO:0000256|HAMAP-
KW Rule:MF_00505};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00505};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00505}; Reference proteome {ECO:0000313|Proteomes:UP000007054};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 24..177
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..347
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 559..632
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT COILED 494..521
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 632 AA; 72867 MW; 31836810D0C59DCE CRC64;
MKTKQFKAES KRLLDMMIHS IYTHKEIFLR ELISNASDAM DKLYFRSLTD EKVGMNREDF
AIDLKIDKDA RTLTITDNGI GMTQEELEKN LGTIANSGSL KFKNENKLED DVDIIGQFGV
GFYSAFMVAK RVTVRSKAYG SDEAYQWQSE GVDGYTIEPC DKETVGTEII LEIKDDAEDE
TYSEFLEQYR IQGLVKKYSD YIRYPIRMDM TKSRRKETEN ADKDAAPEYE EYVENETLNS
MVPLWRKNKS ELTDADYNAF YKEKFFDYNE PLLHIHTKSE GTATFNALLY IPSKAPYDYY
TKEYEKGLQL YSSGVMIMEK CADLLPDYFS FVKGLVDSED LSLNISRELL QHDRQLKIIA
KALEKSIRNE LTKLLKNDRA AYEKFFEAFG LQLKFGVYNG YGMNKDALKD LLLFYSSSEK
KPVTLAEYVS RMKEDQTCIY YATGENIARI DHLPQTELVK DKGFEILYLT ENVDEFAIKM
LMNYEGKEFK SVSAGDLDLE TEEEKKEIEE KSKEHADLFN DMQKALEGKV KSVRLSQRLK
SHPVCLTSEG ALSLEMEKVL NAMPTDQKVQ ADRVLEINPE HPIFAKLVQL QKENPDKLKA
YAKLLYDQAL LIEGMSIEDP VAFSNQICEL MA
//
