HTPG_CLOBL
ID HTPG_CLOBL Reviewed; 626 AA.
AC A7GEU9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=CLI_2051;
OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Langeland / NCTC 10281 / Type F;
RA Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL Submitted (JUN-2007) 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; CP000728; ABS40160.1; -; Genomic_DNA.
DR RefSeq; WP_003405400.1; NC_009699.1.
DR AlphaFoldDB; A7GEU9; -.
DR SMR; A7GEU9; -.
DR EnsemblBacteria; ABS40160; ABS40160; CLI_2051.
DR KEGG; cbf:CLI_2051; -.
DR HOGENOM; CLU_006684_3_0_9; -.
DR OMA; MRRMKEM; -.
DR Proteomes; UP000002410; 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_1000014913"
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
