ID   HTPG_BORBU              Reviewed;         616 AA.
AC   P42555;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 129.
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=BB_0560;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 53899 / 297;
RA   Porcella S.F., Radolf J.D., Norgard M.V.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 497-574.
RC   STRAIN=212;
RX   PubMed=7812434; DOI=10.1099/13500872-140-11-2931;
RA   Ojaimi C., Davidson B.E., Saint-Girons I., Old I.G.;
RT   "Conservation of gene arrangement and an unusual organization of rRNA genes
RT   in the linear chromosomes of the Lyme disease spirochaetes Borrelia
RT   burgdorferi, B. garinii and B. afzelii.";
RL   Microbiology 140:2931-2940(1994).
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; U51878; AAA97469.1; -; Genomic_DNA.
DR   EMBL; AE000783; AAC66919.2; -; Genomic_DNA.
DR   EMBL; L32145; AAC41403.1; -; Genomic_DNA.
DR   PIR; G70169; G70169.
DR   RefSeq; NP_212694.2; NC_001318.1.
DR   RefSeq; WP_002557148.1; NC_001318.1.
DR   AlphaFoldDB; P42555; -.
DR   SMR; P42555; -.
DR   STRING; 224326.BB_0560; -.
DR   PRIDE; P42555; -.
DR   EnsemblBacteria; AAC66919; AAC66919; BB_0560.
DR   GeneID; 56567992; -.
DR   KEGG; bbu:BB_0560; -.
DR   PATRIC; fig|224326.49.peg.951; -.
DR   HOGENOM; CLU_006684_3_0_12; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:CAFA.
DR   GO; GO:0016020; C:membrane; IDA:CAFA.
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; Reference proteome;
KW   Stress response.
FT   CHAIN           1..616
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000062971"
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;  71219 MW;  D676552F48DBEE84 CRC64;
     MKKQFDTEVN DLLYLIIHSL YSHKEIFLRE LISNASDAID KLKFLSLTNE KFKNIALEPK
     IEISFDDKSI LIKDNGIGMD EQDLTNHLGV IAKSGTKEFI NNLKQDEKKS ASLIGQFGVG
     FYSAFIVSEK VEVTSKKALE SDAYIWSSDG KTGYEIEKAK KEESGTEIKL YLNKEGLEYA
     NKWKIQEIIK KYSNHINYPI YIKYSEPIMK DGKQEGIEEK EEKLNETTAL WTKNKSEIKA
     EEYNEFYKNT TFDYENPLMH IHTKAEGNLE YTNLFYVPSK APYDLYYPNT KPGVKLFINR
     IFITDSEGSL LPNYLRFIKG IIDCQDLPLN VSREILQQNK ILSKIKSSSV KKILSELEKL
     SKKNPEKFSE FSKEFGRCIK EGVYSDFENR EKLISLIRFK SSSVDGFVSF KEYKERMNES
     QKSIYYITGG KENILKENPI VAAYKEKGFE ILIMDDELDE AILNLIPEYE GLKLKAINKN
     ETSNELKDEN FKKIEEEFKD TLTKVKEILK DHIKEVNLSA TLIKEPSAII IDSNDPTYQM
     QKIMLSMGQE VKEIKPILEL NPNNKIVQNL KNLEPEKLEK ISILLFEEAM LTSGMPSKNP
     GKFINIINEF IEKDFL