ID   HTPG_ACISJ              Reviewed;         650 AA.
AC   A1W3A1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Ajs_0475;
OS   Acidovorax sp. (strain JS42).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX   NCBI_TaxID=232721;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS42;
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 Acidovorax sp. JS42.";
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; CP000539; ABM40726.1; -; Genomic_DNA.
DR   RefSeq; WP_011803935.1; NC_008782.1.
DR   AlphaFoldDB; A1W3A1; -.
DR   SMR; A1W3A1; -.
DR   STRING; 232721.Ajs_0475; -.
DR   EnsemblBacteria; ABM40726; ABM40726; Ajs_0475.
DR   KEGG; ajs:Ajs_0475; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000000645; 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; 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; 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.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..650
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014894"
FT   REGION          1..344
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          345..582
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          583..650
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   650 AA;  72274 MW;  D369A3EFF077980D CRC64;
     MSKHTHSFQA EVAQLLHLVT HSLYSNKEIF LRELVSNASD ACDKLRFEAL NNAALYEDAP
     NLEVRVSFDK EARTLTITDN GIGMSEQEAI DHLGTIAKSG TRDFMNRLSG DQKADAQLIG
     QFGVGFYSGF IVADRITVES RRAGLPASEG VRWASGGAGD FEVEAIERAA RGTSVILHLR
     EDAEEFLNAW KIKQVIGKYS DHISLPILME KEEWKESEKE GEPGQMVKTG EWETVNKASA
     LWTRPKKDIT DEQYQDFYKS ISHDFENPLT WSHNRVEGNT EYTQLLYIPA KAPFDLWNRD
     KKAGVKLYVK RVFIMDDAES LMPSYLRFVK GVIDSADLPL NVSRELLQES RDVRLIRDGS
     VKRVLSMLED LAKHDKHEAA AEGADGVQDV VSAEDKAKEG KYTQFYAEFG AVLKEGLGED
     FANRERLAKL LRFASTTSDT PSVSFADYKA RMKEGQEAIY YITADTLAAA KNSPQLEVFK
     KKGIEVLLMT DRVDEWALNY LQDFDGTPLQ SVAKGAVDLG KLQDEAEKKA AEEAAEAFKP
     MLAKLKEALK DKAEDVRVTT RLVDSPACLV VQDGGMSTQL ARLLKQAGQS APDAKPVLEV
     NPEHALVKKL DGSVHFHDLA HILFDQALLA EGGLPEDPAA YVKRVNALLA