ID   HTPG_ACIF2              Reviewed;         629 AA.
AC   B7JAR2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=AFE_3158;
OS   Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS   / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=243159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455;
RX   PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA   Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II,
RA   Eisen J.A., Holmes D.S.;
RT   "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT   industrial applications.";
RL   BMC Genomics 9:597-597(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; CP001219; ACK80199.1; -; Genomic_DNA.
DR   RefSeq; WP_012537630.1; NC_011761.1.
DR   AlphaFoldDB; B7JAR2; -.
DR   SMR; B7JAR2; -.
DR   STRING; 243159.AFE_3158; -.
DR   PaxDb; B7JAR2; -.
DR   EnsemblBacteria; ACK80199; ACK80199; AFE_3158.
DR   GeneID; 66434091; -.
DR   KEGG; afr:AFE_3158; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001362; 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..629
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000127021"
FT   REGION          1..337
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          338..554
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          555..629
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   629 AA;  71121 MW;  466B94268FA55B74 CRC64;
     MAASKETMQF QTEINQLLQL MIHSLYSNKE IFLRELISNA SDACDKLRFE ALADPALLTG
     DSELKVEVDF DPEAGTITVR DNGIGMNRDE VIANIGTIAK SGTREFFERL SGDQTKDAKL
     IGQFGVGFYS AFIVADRVSL NTRRAGMEAE HGVRWESDGT GTYTLETLDL PARGTEIVLH
     LREEERQDLL SAWRLRSIIN KYSDHIPLSI RMRKIGEGGK PGDEWETVNK ASALWQRSKS
     EISDDEYKEF YRYVSHDYGD PLTWSHNHVE GRLEYTSLLF IPAKAPFDLW DHNHPHGIKL
     YVQRVFIMDD AEQLLPRYLR FVRGVIDSSD LPLNVSREIL QGNRVIDQMR SGSVKRILGL
     LEEMAEKEPE KYQTFWNEFG RVLKEGPGED YSNREQIARL LRFASTHTDT DTQNVSLADY
     LARMAEGQDK IYYITADSFL AAKNSPQLEL LRKKGIEVLL LSDRVDEWLT SHLPEFEGKA
     LTSVAKGALD LGAIETEEER KSQEETEKDA EGLVERIKNA LGERVETVRV SHRLTSSPAC
     IVLGERDMAL YMQQLLKQAG HEISSTKPVL EINPTHPMLA RIEGEKDDTR FAEWSALLLD
     QAILAEGGQL EDPAGFVARI NQLMLALAG