ID   HTPG_POLNA              Reviewed;         629 AA.
AC   A1VTA5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=Pnap_3587;
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
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; CP000529; ABM38883.1; -; Genomic_DNA.
DR   RefSeq; WP_011802953.1; NC_008781.1.
DR   AlphaFoldDB; A1VTA5; -.
DR   SMR; A1VTA5; -.
DR   STRING; 365044.Pnap_3587; -.
DR   EnsemblBacteria; ABM38883; ABM38883; Pnap_3587.
DR   KEGG; pna:Pnap_3587; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000644; 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..629
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014938"
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..629
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   629 AA;  69812 MW;  E15DD3ECAFD013AA CRC64;
     MQKQTLSFQA EVAQLLKLVT HSLYSNPDIF LRELISNASD ACDKLRFEAL NDAGLYENDS
     ELKVRVSFDK AAKTLTITDN GIGMSQQEAI EHLGTIAKSG TRDFVAKLSG DQKNDAQLIG
     QFGVGFYSGF IVADKITVES RRAGLPAAQG VRWVSEGTGE FDVSETLRAE RGTSIILHLK
     DDAADYLNAW KLKGIINKYS DHISLPILMP KEEWKEGEND QPGEMAFTGE WETVNQAAAL
     WTRPKKDITP EHYAEFYKQI SYDSEAPLAT THNRVEGATE YTQLLFIPAK APMDMYNRDK
     AAGVKLYVKR VFIMDDAQAL LPTYLRFVKG VVDSSDLPLN VSRELLQESR AVKAIREGCT
     KRVLSMIEDL ANNEPEKFKT FYAEFGAVLK EGLGEDFANR ERLAKLLRFA SSTTDTTTVS
     FADYKARMKD GQDAIYYITA DTLAAAKSSP QLEIFRKKGI EVLLMADRVD EWALNYLNEF
     DGTPLQSVAK GAVDLGKLQD EDEKKAAEEA QTQFKPILDK LKEALKDKAS DVRATSRLVD
     SPACLVVQDG DMSTQLARML KQAGQTVPEV KPILEVNAQH PLVRKLEASS ELASFDDLAN
     ILFDQALLAE GGMPTDPAAY VRRVNALLV