ID   HTPG_NITMU              Reviewed;         639 AA.
AC   Q2YA09;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=Nmul_A1109;
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) 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; CP000103; ABB74412.1; -; Genomic_DNA.
DR   RefSeq; WP_011380453.1; NZ_FNVK01000008.1.
DR   AlphaFoldDB; Q2YA09; -.
DR   SMR; Q2YA09; -.
DR   STRING; 323848.Nmul_A1109; -.
DR   EnsemblBacteria; ABB74412; ABB74412; Nmul_A1109.
DR   KEGG; nmu:Nmul_A1109; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000002718; 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..639
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000236999"
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..639
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   639 AA;  72907 MW;  69A5FF3A1AF6DF10 CRC64;
     MEATATKEHL NFQTEVKQLL KLMIHSLYSN KEIFLRELIS NASDAADKLR FEALTDGALY
     ESDSDLKIRV SYDKEARTIT VADNGIGMSR QEVIDHIGTI AKSGTREFFD ALTGDQAKDA
     HLIGQFGVGF YSAFIVADKV TLTTRRAGLT HEHGVRWESG GEGDYTLETI DKPGRGTEVT
     LHLREGEDEL LNGWRLRSII RKYSDHITLP IVMKKEEWSQ EKNENTVTEE DETINQASAL
     WARPKNEISE EQYNEFYKHV AHDFEPPLAY VHARVEGKQE YTQLLYVPSR APFDLYDRES
     RHGIKLYVRR VFIMDDAKQL LPNYLRFVRG IIDSNDLPLN VSREILQESK DIEAMRAGSV
     KKVLGLLDDL AQSETDEGKA KFKTFWKEFG QVMKEGVAED YANRERIAKL LRFVSTHSDS
     EEQDVSLSDY VGRMKDGQEK IYYVTADSLT AAKSSPHLEI FRKKDIEVIL LFDRVDEWLV
     ANLPEFEGKH LQSVAKGSLD LGKLEDEAEK KEQEKEAGEY KELTEKIKEV LGEQVKDVRI
     TLRLTESPAC LVTETHDMSG NLERLLKSAG QKVTHTKPIL EINPYHPMVE RLKSEETHFA
     DWSHILFDQA LLAEGGQLED PASFVKRINQ LFLSTGSKE