ID   HTPG_POLSJ              Reviewed;         626 AA.
AC   Q12FW8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=Bpro_0614;
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX   NCBI_TaxID=296591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500;
RX   PubMed=18723656; DOI=10.1128/aem.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE42574.1; -; Genomic_DNA.
DR   RefSeq; WP_011481577.1; NC_007948.1.
DR   AlphaFoldDB; Q12FW8; -.
DR   SMR; Q12FW8; -.
DR   STRING; 296591.Bpro_0614; -.
DR   EnsemblBacteria; ABE42574; ABE42574; Bpro_0614.
DR   KEGG; pol:Bpro_0614; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001983; 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..626
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258517"
FT   REGION          1..343
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          344..558
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          559..626
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   626 AA;  69699 MW;  5E1A4AEF85E3FCAB CRC64;
     MHKQTLSFQA EVAQLLNLVT HSLYSNPDIF LRELISNASD ACDKLRFEAL NDAALYEGDS
     ELQVRLRYNK TANTLTITDN GIGLSEREAI ENLGTIAKSG TRDFMAKLSG DQKNDAQLIG
     QFGVGFYSGF IVADRITVES RRAGLPATQG VRWSSEGTGE FEVSEMERAE RGTSIILHLK
     DDARDYLNAW KLKGIINKYS DHISLPILMQ KEEWKEGENG QPGEMVVTGE WETVNQAAAL
     WTRAKKDITP EQYDEFYKQI SYDSQAPLAT THNRVEGGTE YTQLLFIPAK APMDLFNRDK
     AAGVKLYVRR VFIMDDAQAL MPTYLRFVKG VVDSADLPLN VSRELLQESR AVKAIREGNT
     RRVLSMIEDL AANDADKFKA FYAEFGAVLK EGLGEDFANR ERLAKLLRFA SSTTDTVSVG
     FADYKARMKE GQDAIYYVTA DTLAAAKSSP QLEIFRKKGI EVLLMADRVD EWALNYLHEF
     DGTPLQSVAK GAVDLGKLQD EDEKKAAEEA QTHFKPILDK LKEALKDKAK DVRATTRLVD
     SPACLVVQDG DMSTQLARML KQAGQAVPEV KPILEVNAQH PLVKKLEAGE HFDDLAHILF
     DQALLAEGGM PEDPAAYVKR VNALLV