ID   HTPG_NATTJ              Reviewed;         627 AA.
AC   B2A875;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Chaperone protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE   AltName: Full=Heat shock protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE   AltName: Full=High temperature protein G {ECO:0000255|HAMAP-Rule:MF_00505};
GN   Name=htpG {ECO:0000255|HAMAP-Rule:MF_00505}; OrderedLocusNames=Nther_0856;
OS   Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS   JW/NM-WN-LF).
OC   Bacteria; Firmicutes; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC   Natranaerobius.
OX   NCBI_TaxID=457570;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT   "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT   LF.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-
CC       Rule:MF_00505}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00505}.
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DR   EMBL; CP001034; ACB84441.1; -; Genomic_DNA.
DR   RefSeq; WP_012447319.1; NC_010718.1.
DR   AlphaFoldDB; B2A875; -.
DR   SMR; B2A875; -.
DR   STRING; 457570.Nther_0856; -.
DR   PRIDE; B2A875; -.
DR   EnsemblBacteria; ACB84441; ACB84441; Nther_0856.
DR   KEGG; nth:Nther_0856; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_9; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001683; 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:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.790; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00505; HSP90; 1.
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_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF00183; HSP90; 2.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..627
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000127033"
FT   REGION          1..343
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          344..553
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          554..627
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   627 AA;  73056 MW;  3DA45118C516F1E0 CRC64;
     MATQEFQAET KRLLDIVINS IYSNKEIFLR ELISNASDAI DKLYYKSLTD NSLDFNKDDY
     YIKITVDKEN RQLKISDTGI GMTRQELEDN IGVIARSGSL DFKKANEQEI KDGHDIIGQF
     GVGFYSAFMV AEEVTIISKA YGSDHAYKWE SEGIEGYSVS PTEKESVGTD VILKIKENTD
     DEDYDQYLDE HRLKSIVKKY SDFIRYPIKM DLTKSKPKDD NEEEYEEYIE EETVNTMVPI
     WERNKNELTD EDYKNFYRER HYGFDEPITH IHINAEGTIS FKAVLFIPER PPFNFYTKEF
     EKGLELYSNG VLIMNKCPDL LPDYFSFVRG VVDSEDLSLN ISREMLQQDK QLKLIAKNIK
     NKVKKELKNV MENDREKYEE FFESFGTLLK YGIYSEFGQN KETLQDLLLF YSSKENKMVS
     LDEYISRMGE DQKYIYYATG ESVERIDKLP QTEFVKDKGY EVLYLTEDVD EFAIKMMGSY
     QDVEFKSVSS KDLGLDSEDE ETSDEKEKEY KGMFDKMAEI LSDKVNTVRA SERLKDHPVC
     LANEGEISIE MEKVLQSMPN NQNVQAEKAL EINVNHDVFD KLTEAYEQDE DKFKLYTDLL
     YNQACLIEGL PIEDPVKYTN NVCKIMS