HTPG_CLOB6
ID HTPG_CLOB6 Reviewed; 626 AA.
AC C3KXP4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=CLJ_B2190;
OS Clostridium botulinum (strain 657 / Type Ba4).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=515621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=657 / Type Ba4;
RA Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum Ba4 strain 657.";
RL Submitted (MAY-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}.
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DR EMBL; CP001083; ACQ51783.1; -; Genomic_DNA.
DR RefSeq; WP_003362922.1; NC_012658.1.
DR AlphaFoldDB; C3KXP4; -.
DR SMR; C3KXP4; -.
DR EnsemblBacteria; ACQ51783; ACQ51783; CLJ_B2190.
DR KEGG; cbi:CLJ_B2190; -.
DR HOGENOM; CLU_006684_3_0_9; -.
DR OMA; MRRMKEM; -.
DR Proteomes; UP000002333; 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_1000206568"
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 553..626
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 626 AA; 72862 MW; 01AEB8ACBCAE5C9E 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
EYVSRMPEEQ KYIYYAVGES NERIEKLPQI EGVLDKGYEV LYFTDDIDEF AIKMLMNYKE
KEFKSVSSGD LGIEGEEKEN TSNSDDKKNK ELFESMKDIL SGKVKDVRAS KRLKNHPVCL
ANEGELSIEM EKVLNAMPNN QNIKADKVLE ININHDVFKS LKEAYEGDKE KLKLYTDLLY
NQALLIEGLA INDPVEFTNN ICKIMK
