ID   HTPG_CLOTE              Reviewed;         624 AA.
AC   Q894P6;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   03-AUG-2022, entry version 109.
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=CTC_01489;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO36046.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE015927; AAO36046.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_035125161.1; NC_004557.1.
DR   AlphaFoldDB; Q894P6; -.
DR   SMR; Q894P6; -.
DR   STRING; 212717.CTC_01489; -.
DR   PRIDE; Q894P6; -.
DR   EnsemblBacteria; AAO36046; AAO36046; CTC_01489.
DR   GeneID; 64180813; -.
DR   KEGG; ctc:CTC_01489; -.
DR   HOGENOM; CLU_006684_1_3_9; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001412; 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; 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_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 2.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
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..624
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000062983"
FT   REGION          1..341
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          342..550
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          551..624
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   624 AA;  72951 MW;  2F84937258A7BC99 CRC64;
     MAVKQFKAES KRLLDLMINS IYTNKEIFLR ELISNASDAI DKRYYRSLTD ENISFNKKDF
     YIRIIPNKEE RTLTIIDTGI GMSVEELENN LGTIAKSGSL AFKNKMESKE GIDIIGQFGV
     GFYSAFMIAD KIVVKSHSID SDEAYKWESK GVEGYEIEKC EKDELGTEII LKIKENTDDE
     NYDEFLEEYN IKNLIKKYSN FIKYPIKMNM KKTKLKEGTK DEYEDYFEDE TLNSMVPIWK
     KNKNEVKTED YERFYIDKHF GYDKPLKSIR SKVEGVVSYT ALLFIPSTTP YDFYTRNFEK
     GLELYSNGVL IMEKCADLLP DYFSFVQGLV DSEDLSLNIS RELLQHDRQL KLIAKNIKEK
     IKSELLSILK NKREDYIKFY NNFGRQLKYG VYSDFGANKE VLQDLIMFYS STEKKLVTLD
     EYVSRMKDDQ KYIYYAPGEN IDKIEKLPQT EIVRDKGYEI LYFADEVDEF AIKMLMNYKE
     KEFKSVYSKD LGFEAEEKEE QKENDENKEV FEFMKDVLNG KVKEVRASKR LKSHPVCLAN
     ASDISIEMEK VLSMMPNNEN IKADKILEIN TNHNMFNTIK SAFKDDKDKL KMLSSLLYNQ
     ALLIEGLPIE DPVQFANDVC KLIK