ID   HTPG_BORA1              Reviewed;         630 AA.
AC   Q2KYY2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=BAV0447;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N;
RX   PubMed=16885469; DOI=10.1128/jb.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ48052.1; -; Genomic_DNA.
DR   RefSeq; WP_012416144.1; NC_010645.1.
DR   AlphaFoldDB; Q2KYY2; -.
DR   SMR; Q2KYY2; -.
DR   STRING; 360910.BAV0447; -.
DR   PRIDE; Q2KYY2; -.
DR   EnsemblBacteria; CAJ48052; CAJ48052; BAV0447.
DR   GeneID; 41392358; -.
DR   KEGG; bav:BAV0447; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001977; 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..630
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000236985"
FT   REGION          1..341
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          342..558
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          559..630
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   630 AA;  71099 MW;  EC446E1841A59F44 CRC64;
     MTQNATSETL GFQAEVKQLL HLMIHSLYSN KEIFLRELVS NASDACDKLR FEAIDQPELL
     AGDSELAIRV SYDKAARTIT IADNGIGLSR EEAIANLGTI ARSGTREFFS QLTGDKQKDA
     QLIGQFGVGF YSSFIVADRV SVLSRRAGSD EAIRWESDGQ GEFSIASAEK ATRGTDVVLH
     LRADEDEFLN GWKLREVLRR YSDHISLPIL MRKEEWDADK DEQVTRDEWE TVNQANALWT
     RSKSEISDEQ YREFYKTVSH GFDEPLAWTH NRVEGRSEYT QLLYVPRQAP FDLWDRDARR
     GVKLYVKRVF IMDDAEQLLP AYLRFVRGVI DSADLPLNVS REILQESRDV RAIREGSAKR
     ILSLLEDLAE NRKDDYAVFW GEFGQVLKEG VGEDPSNQER IAKLLRFAST HAGDASQTTS
     LQDYLGRLKE GQDKIYYVTA DSYSAASNSP HLEIFRKKGI EVLLLWDRVD EWMLSHLREF
     EGKSLVSVAK GGLDLADLAD EEEKKKQTEV AESFKPLIER LQTALGEQVK EVRVTLRLVD
     SPACVVVGQN DLSPHLLRML KAAGQEVPEV KPVLEINPEH ALIARIRDVS DADFGAWAQL
     LLDQALLAEG AQIADPAAFV KRLNALLLKV