ID   HTPG_NITEU              Reviewed;         640 AA.
AC   Q82TV8;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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}; Synonyms=hptG;
GN   OrderedLocusNames=NE1762;
OS   Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS   14298).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=228410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX   PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA   Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA   Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA   Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT   "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT   chemolithoautotroph Nitrosomonas europaea.";
RL   J. Bacteriol. 185:2759-2773(2003).
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; AL954747; CAD85673.1; -; Genomic_DNA.
DR   RefSeq; WP_011112313.1; NC_004757.1.
DR   AlphaFoldDB; Q82TV8; -.
DR   SMR; Q82TV8; -.
DR   STRING; 228410.NE1762; -.
DR   PRIDE; Q82TV8; -.
DR   EnsemblBacteria; CAD85673; CAD85673; NE1762.
DR   KEGG; neu:NE1762; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   PhylomeDB; Q82TV8; -.
DR   Proteomes; UP000001416; 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..640
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000062998"
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;  73146 MW;  3D7D34CAB6C186E0 CRC64;
     MQTAENIEHL NFQAEANQLL KLMIHSLYSN KEIFLRELIS NASDAADKLR FEGLSDAALY
     ESDPDLKIRI AYDKEARTIT IIDNGIGMSR QEVINNIGTI AKSGTREFFD SLTGDQAKDA
     NLIGQFGVGF YSAFIVADKV TLTTRRAGLT IEHGVRWESG GEGEYTLETV EKPDRGTEIV
     LHLREGEDEL LSSFQLRSII RKYSDHITLP IVMKKEVWDD ESKSYRLSDE DETINQASAI
     WARPKNEITQ EQYDEFYKHV AHDFEPPLAH VHARVEGKQE YIQLLYIPAH APFDLFDREH
     RHGLKLYVRR VFIMDDAEKL LPGYLRFVRG IIDSSDLPLN VSREILQESK DIDSIRAGSV
     KKVLGLIEDL AMSDKSEDQE KFKTFWREFG QVLKEGIAED YSNRERIAKL LRFTSTHDER
     EEQTVSLDDY IARMKPEQEK IYYITADGLK AAQSSPHLEI FRKKGIEVLL LCDRIDEWLV
     ANLNEYTGKS LQSIAKGNLD LGKLEDEEEK KEHEKEAGDF QELTNKMKEV LGEQVKDVRI
     TYRLTESPAC LVADTHDVSG NLGRLLKSAG QKVPDSKPFL EINPHHPMIQ RLKYEEAKFA
     DWSHILFDQA LLAEGGQLED PAGFVKRLND LLLQNILSGK