ID   HTPG_DESPS              Reviewed;         622 AA.
AC   Q6ARM0;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=DP0276;
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfocapsaceae; Desulfotalea.
OX   NCBI_TaxID=177439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12343 / LSv54;
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA   Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA   Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT   permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
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; CR522870; CAG35005.1; -; Genomic_DNA.
DR   RefSeq; WP_011187521.1; NC_006138.1.
DR   AlphaFoldDB; Q6ARM0; -.
DR   SMR; Q6ARM0; -.
DR   STRING; 177439.DP0276; -.
DR   EnsemblBacteria; CAG35005; CAG35005; DP0276.
DR   KEGG; dps:DP0276; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_1_7; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000602; 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; 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; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
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..622
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000236990"
FT   REGION          1..322
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          323..539
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          540..622
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   622 AA;  69692 MW;  3EA664FDD854AAD3 CRC64;
     MTEAKNYEFQ AETKKLLDIV INSLYTERDV FVRELISNSA DALEKMRHEA LTCQEVLDED
     LPLEITIDLD EEAHTLTISD SGIGMTEQEL VNNLGVIAHS GSGSFYAELA EAVKKDVNLI
     GQFGVGFYAA FMAGNKVRVQ TRSWDGSQGH EWLSEGAGSF TITPLDGLAR GTRIVVELKD
     DAHEYAQDWK IKNVIEQYSS FVSFPIKLKG EVVNTVQALW SRSKSEISDE EYNEFYKFIG
     NATEDPSYRL HFSADAPLSI KSLLFVPKEN FEVMGFGRVE PGVNLYCQRI LIDQHSENIL
     PGWLRFLKGV VDSEDLPLNI SRQSLQDNAL VSKIRRVVTK RFLKYLAEEA TRDESQYLQF
     WSTFGIYLKE GVTTDYEYQK ELGKLLRFET SKSELGVPVS LADYLLRMNP DQEKIYYING
     ASRAAIEAGP YVEMFKKKDI EIVYTLDPID DFVLSHLQEF EGKKLVSADG ADISLDKEEA
     EDALVDESGV DKAELAELLT WMKEELKDEV GDVLSSHRLV DAPAMIVNAD GFMSASMERV
     LAASRKEQGI AGVDGSKKHL EINGKNPLIK QLAELRKADA GFAGEVAHQI LDNAMIQAGL
     VVDPLKMVAR NYKILDRAVS RA