ID   HTPG_AROAE              Reviewed;         648 AA.
AC   Q5P1C5;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=AZOSEA27640;
GN   ORFNames=ebA4865;
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1;
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
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; CR555306; CAI08889.1; -; Genomic_DNA.
DR   RefSeq; WP_011238572.1; NC_006513.1.
DR   AlphaFoldDB; Q5P1C5; -.
DR   SMR; Q5P1C5; -.
DR   STRING; 76114.ebA4865; -.
DR   EnsemblBacteria; CAI08889; CAI08889; ebA4865.
DR   KEGG; eba:ebA4865; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000006552; 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..648
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224195"
FT   REGION          1..349
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          350..570
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          571..648
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   648 AA;  72508 MW;  F72154AE62D55A0B CRC64;
     MTTEHAAGAQ TLNFQAEVKQ LLHLMIHSLY SNREIFLREL VSNASDACDK LRFEALDKPE
     LFEGDSELAI RVGFDSEAKT VTVSDNGIGM SRDEVITHLG TIAKSGTKEF FSQLTGDQKK
     DAHLIGQFGV GFYSAFIVAD KVTVVTRRAG LAAAEGVKWE CAMTGDAAGE YTVEAIEKAA
     RGTEITLHLR EGQEDLLSGW KLRGLIRKYS DHIVQPILMK KEEWDKDKNE QVTTDEDETV
     NQANALWTRS RNDITEEEYK GFYKHVGHDF DEPLAWTHAR VEGRHEYTQL LYIPSHAPFD
     MWDRNARHGI KLYVKRVFIM DDAEKLMPAY LRFVRGVVDS SDLPLNVSRE ILQESKDIDT
     IRSGCTKKVL GLLESLATSD EAADREKYAT FWKEFGPVLK EGVGEDFANK DKIAGLLRFA
     STHADTPDEV VSLADYLARM KEGQDKIYYV TAESFNAAKN SPHLEIFRKK GIEVLLLTDR
     VDEWVIGNLP EFDGKALVSV AKGGLDLGKL EDEAEKKETE KAADEYKELL EKMKASLGER
     VKEVRVTHRL TDSPACLVAD EHDVGMNLAR ILKAAGQQAP ASKPILEINP QHPAVMRLKY
     EERQFDDWAA VLFDQALLAE GGTLDDPATF VKRINQLMMA MGGSAGTD