HTPG_CLOBJ
ID HTPG_CLOBJ Reviewed; 626 AA.
AC C1FPN9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=CLM_2202;
OS Clostridium botulinum (strain Kyoto / Type A2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyoto / Type A2;
RA Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL Submitted (OCT-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001581; ACO86628.1; -; Genomic_DNA.
DR RefSeq; WP_012705422.1; NC_012563.1.
DR AlphaFoldDB; C1FPN9; -.
DR SMR; C1FPN9; -.
DR STRING; 536232.CLM_2202; -.
DR EnsemblBacteria; ACO86628; ACO86628; CLM_2202.
DR KEGG; cby:CLM_2202; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_9; -.
DR OMA; MRRMKEM; -.
DR Proteomes; UP000001374; 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_1000146005"
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; 72867 MW; 84015799B3ECB7E9 CRC64;
METKQFKAES KRLLDLMINS IYTHKEIFLR ELISNSSDAI DKIYYKTLTD DSLKFERDDY
YIRVVSDKEN RILKIADTGI GMTKEELENN LGVIAKSGSL QFKKENEVKE GYDIIGQFGV
GFYSAFLVSD DVTVISKAFG SNEAYKWNSK GAEGYTIEPC EKEAYGTEII LKIKDNTEEE
NYDEFLEEYT LKSIIKKYSD FIRYPIKMDL TKTKPKEDNK EEFEEYKEEE TINSMVPIWR
KNKNELKSED 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 TSNSDDKENK ELFESMKDIL SGKVKDVRAS KRLKNHPVCL
ANEGELSIEM EKVLNAMPNN QNIKADKVLE INMNHDVFKS LKEAYEGDKE KLKLYTDLLY
NQALLIEGLA INDPVEFTNN ICKIMK