ID   HTPG_BORGP              Reviewed;         616 AA.
AC   Q660W4;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=BG0570;
OS   Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS   PBi) (Borrelia bavariensis).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=290434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX   PubMed=15547252; DOI=10.1093/nar/gkh953;
RA   Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA   Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT   "Comparative analysis of the Borrelia garinii genome.";
RL   Nucleic Acids Res. 32:6038-6046(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; CP000013; AAU07407.1; -; Genomic_DNA.
DR   RefSeq; WP_011193867.1; NZ_CP028872.1.
DR   AlphaFoldDB; Q660W4; -.
DR   SMR; Q660W4; -.
DR   STRING; 290434.BG0570; -.
DR   EnsemblBacteria; AAU07407; AAU07407; BG0570.
DR   KEGG; bga:BG0570; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_12; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000002276; 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..616
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224198"
FT   REGION          1..333
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          334..542
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          543..616
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   616 AA;  71271 MW;  FF6D542187AE528B CRC64;
     MKKQFDTEVN DLLYLIIHSL YSHKEIFLRE LISNASDAID KLKFLSLTNE KFKNIALEPK
     IEITFDDKSI LIKDNGIGMN EQDLTNHLGV IAKSGTKEFI NNLKQDEKKS ASLIGQFGVG
     FYSAFIVSEK VEVTSKKALE SDAYIWFSDG KTGYEIEKAK KEESGTEIKL YLNKEGLEYA
     NKWKIQEIIK KYSNHINYPI YIKYSEPIMK DGKQEGIEEK EEKLNETTAL WTKNKSEIKA
     EEYNEFYKNT TFDYENPLMH VHTKAEGNLE YTNLFYIPSK APYDLYYPNT KPGVKLFINR
     IFITDSEGSL LPNYLRFIKG IIDCQDLPLN VSREILQQNK ILSKIKSSSV KKILSELEKL
     SKKNPEKFSK FSKEFGRCIK EGVYSDFENR EKLISLIRFK SSSVDGFVSF KEYKERMKES
     QKSIYYITGG KENILKENPI VSAYKEKGFE ILIMDDELDE AILNLIPEYE GLKLKAINKN
     ETSNELKDEN FKKIEEEFKD ILTKVKEILK DHIKEVNLSA TLIKEPSAII VDSNDPTYQM
     QKIMLSMGQE VKEIKPILEL NPNNKIVQNL KNLESEKLEK ISILLFEEAL LTSGMPSKNP
     GKFINIINEF LEKELL