ID   HTPG_ALKOO              Reviewed;         626 AA.
AC   A8MGJ3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=Clos_1676;
OS   Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS   OhILAs)).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=350688;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OhILAs;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA   Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT   "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL   Submitted (OCT-2007) 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; CP000853; ABW19216.1; -; Genomic_DNA.
DR   RefSeq; WP_012159528.1; NC_009922.1.
DR   AlphaFoldDB; A8MGJ3; -.
DR   SMR; A8MGJ3; -.
DR   STRING; 350688.Clos_1676; -.
DR   EnsemblBacteria; ABW19216; ABW19216; Clos_1676.
DR   KEGG; aoe:Clos_1676; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_9; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000269; 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; 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; PF00183; HSP90; 2.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
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..626
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000060523"
FT   REGION          1..341
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          342..552
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          553..626
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   626 AA;  73036 MW;  19BDCD23F4678E94 CRC64;
     METKQFKAES KRLLDLMIHS IYTQKEIFLR ELISNASDAI DKIYYRALTD EALNFNKEDY
     YIKIIPDKEK RILRIIDTGI GMTKEELEEN LGVIAKSGSL AFKSAHELKD GYDIIGQFGV
     GFYSSFMVAE TVTVISKSID SESGYKWEST GVDGYTIEPW DKDTVGTEIV LRIKEDTEDE
     NYSEYLEEYR LRNIIKKYSD FIRYPIKMDI HNKRLKENSE DDYEDYVEEQ TINSMVPIWR
     KNKNELTKED YDNFYMEKRY GFDKPVKHIH ISADGAVRYN AILFIPERTP FDYYTKEYEK
     GLELYSNGVL IMNKCSDLLP DYFSFVKGMV DSEDLSLNIS REMLQHDRQL KLIGKNIKNK
     IKNELMSLLK EDRTQYEAFF EAFGRQLKYG IYSEFGSNKD VLQDLLLFYS SKEKKLVTLD
     EYISRMSEEQ KYIYYATGES KERIEKLPQT ELVSEKGFEI LYLTEDIDEF AIKVLMSYKD
     KEFKSVSSSD LGIEDSETEK NTETEELENK ELFEKMTALL SDKVTAVRIS KRLKSHPVCL
     ANEGEISIEM EKILSAMPNN ENIKANKILE INGNHQVFEV LKDAYKNDSE KFGLFTELLY
     NQALLIEGLP INDPVEFSNS ICKLMI