ID   HTPG_VEREI              Reviewed;         662 AA.
AC   A1WF62;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=Veis_0484;
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL   Submitted (DEC-2006) 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; CP000542; ABM56269.1; -; Genomic_DNA.
DR   RefSeq; WP_011808285.1; NC_008786.1.
DR   AlphaFoldDB; A1WF62; -.
DR   SMR; A1WF62; -.
DR   STRING; 391735.Veis_0484; -.
DR   EnsemblBacteria; ABM56269; ABM56269; Veis_0484.
DR   KEGG; vei:Veis_0484; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000374; 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; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
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; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..662
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014962"
FT   REGION          1..352
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          353..594
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          382..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..662
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   662 AA;  73208 MW;  3F2D4FCBE76FC1FB CRC64;
     MSKQTLSFQA EVAQLLHLVT HSLYSNQEIF LRELISNASD ACDKLRFAGL NQPALFEDAP
     QLEVRVSFDQ TARTLTITDN GIGMSQQEAI EHLGTIAKSG TKDFMGQLSG DQKQDAQLIG
     QFGVGFYSGF IVADKITVES RRAGLPASEG VRWASGGTGD FEVETIDRPA RGTSVILHLR
     DSAEEYLNNW KLKSIISRYS DHISLPILME KQEWKDGELI NPGDEKGGRQ PGAMVKTGDW
     ETVNQASALW ARPKKDVSDA QYAEFYKTIS HDPLAPLTWA HNRVEGSTEY TQLLYIPAKA
     PFDLWNRDKK AGVKLYVKRV FIMDDAEALL PTYLRFVKGV IDSADLPLNV SRELLQESRD
     VRAIREGSTK RVLSMLEDLA RHDRHDSPAP QPAEGADRVS DVVDADDKAK EGKYSQFYAE
     FGAVLKEGLG EDFANRERLA RLLRFASTSS DQASVGLADY KARMKEGQEA IYYITADTLA
     AAKHSPQLEV FKKKGIEVLL MTDRVDEWAL NYLHEFDGTP LQSVAKGAVD LGKLQDEAEK
     KAAEEAAEAF KPLLARLKET LKDKAEDVRV TTRLVDSPAC LVVHGDGMST QLARLLKQAG
     QQAPETKPVL EVNASHALVR KLDGSQHFDD LAHILFDQAL LAEGGLPADP AAYVKRVNAL
     LV