ID   HTPG_CLOBK              Reviewed;         626 AA.
AC   B1IN79;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=CLD_2640;
OS   Clostridium botulinum (strain Okra / Type B1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okra / Type B1;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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; CP000939; ACA45545.1; -; Genomic_DNA.
DR   RefSeq; WP_003405400.1; NC_010516.1.
DR   AlphaFoldDB; B1IN79; -.
DR   SMR; B1IN79; -.
DR   EnsemblBacteria; ACA45545; ACA45545; CLD_2640.
DR   KEGG; cbb:CLD_2640; -.
DR   HOGENOM; CLU_006684_3_0_9; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000008541; 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..626
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000127025"
FT   REGION          1..341
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          342..552
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          490..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..626
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   626 AA;  72764 MW;  37B6413356626D03 CRC64;
     METKQFKAES KRLLDLMINS IYTHKEIFLR ELISNSSDAI DKIYYKTLTD DSLKFERDDY
     YIKVVSDKEN RVLKIADTGI GMTKEELENN LGVIAKSGSL QFKKENEVKE GYDIIGQFGV
     GFYSAFLVSD DVTVISKAFG SNEAYKWNSK GAEGYTIEPC EKEAYGTEII LKIKDNTEEE
     NYDEFLEEYT LKSIIKKYSD FIRYPIKMDL TKTKPKEDNK EEFEEYKEEE TINSMVPIWR
     KNKNELKAED YENFYAEKHY GFDKPIKYIH TSVDGVVSYN AILFIPETTP YDFYTKEYEK
     GLELYSSGVL IMNKCGDLLP DYFGFVKGIV DSEDLSLNIS REILQHDRQL KLIAKNIKTK
     IKNELESLLK KERDKYEKFY ESFGRQLKYG VYSDFGSNKD ILQDLLMFYS SKEKKMVTLA
     EYVSRMPEDQ KYIYYAVGES NERIEKLPQI EGVLDKGYEV LYFTDDIDEF AIKMLMNYKE
     KEFKSVSSGD LGIEGEEKEN TSSSDDKENK ELFESMKDIL SGKVKDVRAS KRLKNHPVCL
     ANEGELSIEM EKVLNAMPNN QNIKADKVLE ININHDVFKS LKEAYEGDKE KLKLYTDLLY
     NQALLIEGLA INDPVEFTNN ICKIMK