ID   HTPG_BORAP              Reviewed;         616 AA.
AC   Q0SMU9; G0IQB0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-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};
GN   OrderedLocusNames=BAPKO_0589, BafPKo_0575;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
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; CP000395; ABH01829.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL69780.1; -; Genomic_DNA.
DR   RefSeq; WP_011601089.1; NC_017238.1.
DR   AlphaFoldDB; Q0SMU9; -.
DR   SMR; Q0SMU9; -.
DR   STRING; 390236.BafPKo_0575; -.
DR   PRIDE; Q0SMU9; -.
DR   EnsemblBacteria; AEL69780; AEL69780; BafPKo_0575.
DR   KEGG; baf:BAPKO_0589; -.
DR   KEGG; bafz:BafPKo_0575; -.
DR   PATRIC; fig|390236.22.peg.553; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_12; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000005216; 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_1000014897"
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;  71404 MW;  A9CF7FA32049DFEC CRC64;
     MKKQFDTEVN DLLYLIIHSL YSHKEIFLRE LISNASDAID KLKFLSLTNE KFKNIALEPK
     IEITFDDKSI LIKDNGIGMN EQELTNHLGV IAKSGTKEFI NNLKQDEKKS ANLIGQFGVG
     FYSAFIVSEK VEVTSKKALE SDAYIWSSDG KTGYEIEKAK KEDPGTEIKL YLNKEGLEYA
     NKWKIQEIVK KYSNHINYPI YIKYNEPIMK DGKQEGIEEK EEKLNETTAL WTKNKSEIKT
     EEYNEFYKNT TFDYENPLMY IHTKAEGNLE YTNLFYIPSK APYDLYYPNT KPGVKLFINR
     IFITDSEGSL LPNYLRFIKG IIDCQDLPLN VSREILQQNK ILSKIKSSSV KKILSELEKL
     SKKNPEKFSE FSKEFGRCIK EGVYSDFENR EKLISLIRFK SSSVDGFVSF KEYKERMNEG
     QKSIYYITGG KENILKENPI VTAYKEKGFE ILIMDDELDE AILNLIPEYE GLKLKAINKN
     ETSNELKDEN FKKIEEEFKD TLTRVKEILK DQIKEVNLSA TLIKEPSAII VDSNDPTYQM
     QKIMLSMGQE VKEIKPILEL NPNNKIVQNL KNLEPEKLEK ISILLFEEAL LTSGMPSKNP
     RKFINIINEF LEKDLL