ID   HTPG_NITEC              Reviewed;         640 AA.
AC   Q0AHI5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, 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=Neut_0937;
OS   Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=335283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 101675 / C91 / Nm57;
RX   PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA   Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA   Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.;
RT   "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas
RT   eutropha C91: implications for niche adaptation.";
RL   Environ. Microbiol. 9:2993-3007(2007).
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; CP000450; ABI59197.1; -; Genomic_DNA.
DR   RefSeq; WP_011634021.1; NC_008344.1.
DR   AlphaFoldDB; Q0AHI5; -.
DR   SMR; Q0AHI5; -.
DR   STRING; 335283.Neut_0937; -.
DR   EnsemblBacteria; ABI59197; ABI59197; Neut_0937.
DR   KEGG; net:Neut_0937; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001966; 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; 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; Stress response.
FT   CHAIN           1..640
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014935"
FT   REGION          1..343
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          344..564
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          565..640
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   640 AA;  73212 MW;  20E3D6829C3B49B3 CRC64;
     MQTAENVEHL NFQAEAKQLL RLMIHSLYSN KEIFLRELIS NASDAADKLR FEGLSDTALY
     ESDPDLKIRI AYDKEARTIT ISDNGIGMSR QEVIDNIGTI AKSGTREFID SLTGDQARDA
     NLIGQFGVGF YSAFIVADKV TLTTRRAGLT TEHGVRWESS GEGEYTLETV EKRDRGTEVV
     LHLREDEDEL LSSFQLRSII RKYSDHITLP IIMKKEVWDD ESKAYKISDE EETVNQASAI
     WARPKNEITQ EQYDEFYKHV AHDFEPPLAH VHARVEGKQE YIQLLYIPAH APFDLFDREH
     RHGLKLYIKR VFIMDDAEKL LPGYLRFVRG IIDSNDLPLN VSREILQESK DIDSIRAGSV
     KKVLGLIEDL ATSDKSEDQE KFKIFWREFG QVLKEGVAED YSNRERIAKL LRFTSTHDEQ
     EEQTVSLDDY IARMKPEQEK IYYITADGLK AAQSSPHLEI FRKKGIEVLL LHDRIDEWLT
     ANLNEYAGKS LQSIAKGDLD LGKLEDEVEK QEHEKEAGDF QELTAKMKEV LGELVKDVRI
     TYRLTESPAC LVADTHDMSG NLGRLLKSAG QKVPDSKPFL EINPHHPMVQ RLKYEEAKFA
     DWSHILFDQA LLAEGGQLED PASFVRRLND LLLQNILSGK