ID   HTPG_CLOPS              Reviewed;         623 AA.
AC   Q0SVV8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=CPR_0413;
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM101 / Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
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; CP000312; ABG86071.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0SVV8; -.
DR   SMR; Q0SVV8; -.
DR   EnsemblBacteria; ABG86071; ABG86071; CPR_0413.
DR   KEGG; cpr:CPR_0413; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000001824; 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; Stress response.
FT   CHAIN           1..623
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258508"
FT   REGION          1..341
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          342..549
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          550..623
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   623 AA;  72480 MW;  B4DD4F2E8EA2854B CRC64;
     MEKREFKAES KRLLDIVINS IYTNREIFLR ELISNASDAI DKVYYKTLGD SSLTFNKDDY
     YIKIKPNKEE RTLTISDKGI GMTEKELDEN LGVIAKSGSL QFKKENEIKD GFDIIGQFGV
     GFYSGFLVAD KITVITKAFG ADKAYKWESD GVDGYTISEA EKDSFGTDII LHLKANDEDE
     NYDEFLEEYK LKSLIKKYSD FIRYPIKLDV TKSRVKEGTE NEHEEYVEEE TVNSMVPLWR
     RNKNELTDDD YNNFYVEKRF GFDKPLRHMH ISVDGMISYN SILYIPENIP YDYYTKEYEK
     GLELYSNGVL IMEKCSELLP DYFGFVKGIV DSQDLSLNIS REMLQHDRQL SRIAKNIKTK
     IKNELESMMK NDRESYEKFY KSFGRQLKYG VYDDFGMNKD ELKDLLMFYS SKEKKMVSLA
     EYVERMAEDQ KYIYYAVGES NERIEKMPQT EMVLDKGYEI LYFTEDVDEF AIKMLMNYKE
     KEFKSVSSGD LGIESEEENK KENEENKGIF EAMKEALGEK ISAVKASSRL KNYPVCLSSE
     GEVSIEMEKI LSAMPNNQGV KAQKVLEVNT NHEVFNSLKD ALENDRDKFN LYTKLLYNQA
     LLVEGLSIED PVDFTNDICK LMK