ID   HTPG_BDEBA              Reviewed;         625 AA.
AC   P61184;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   25-MAY-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=Bd1806;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(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; BX842650; CAE79666.1; -; Genomic_DNA.
DR   RefSeq; WP_011164268.1; NC_005363.1.
DR   AlphaFoldDB; P61184; -.
DR   SMR; P61184; -.
DR   STRING; 264462.Bd1806; -.
DR   PRIDE; P61184; -.
DR   EnsemblBacteria; CAE79666; CAE79666; Bd1806.
DR   KEGG; bba:Bd1806; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_7; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000008080; 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   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..625
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000062969"
FT   REGION          1..330
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          331..545
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          546..625
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   625 AA;  71239 MW;  BF4286B07264B891 CRC64;
     MAKQVQNFNA EIKQLLDIVI HSLYSHKEIF LRELLSNASD AIDKLKFNSL THPSLLPENW
     QPAIRLEPNS ETKTLKIIDN GIGMTQEEVV EFIGTIARSG AKAFMQMNAE MKTKPELIGQ
     FGVGFYSAFM VADRVTLHTQ KAGSNDGTVW ESMGDGTYSL DSVPRPEGTG TTITLHMKDF
     KEEDEVQNFT DKWVLKSLVK KYSDFIAHPI KMMGETEEET LNSQKALWLK SPSEVTKEEY
     KEFYQHLTHD WNEPLRTVHY RAEGTMEFNA LLYVPGKKPW NYNMRDMEYG LSLYIKRVFI
     MADCKDLLPP YLRFVKGLVD SSDLSLNVSR ELLQQDRQVT QIRKNVTNKA LSTLKDLLTK
     ERSAYEDFWT EFGATLKEGL PSDAANKEKL QDLLLFHSTS SDKMTTMDEY VARMKETQKD
     IYYITGDSLS QVSNSPYLEK LKEKGFEVLL LVDPVDEWVV DALSEFKGKK LQSIMREGLD
     LDTAEEKQQK EQEKKQAEVT LKPVLESMKK TLESDVKDVV LSDRLTNTPA CLVASSADPS
     AHMQKLMAQM GKEYAGQQVK RIMEINPNHP VFEKMLKASP EQQTKWAEIL YAQALLTEGS
     NLPDPVKFSQ QIAELMVQAA DSTKH