ID   HTPG_PORG3              Reviewed;         684 AA.
AC   B2RGR5; Q9S3Q2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=PGN_0041;
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS   12257 / NCTC 11834 / 2561).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=431947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10722592; DOI=10.1128/iai.68.4.1980-1987.2000;
RA   Lopatin D.E., Combs A., Sweier D.G., Fenno J.C., Dhamija S.;
RT   "Characterization of heat-inducible expression and cloning of HtpG (Hsp90
RT   homologue) of Porphyromonas gingivalis.";
RL   Infect. Immun. 68:1980-1987(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis strain
RT   ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT   rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(2008).
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; AF176245; AAD51118.1; -; Genomic_DNA.
DR   EMBL; AP009380; BAG32560.1; -; Genomic_DNA.
DR   RefSeq; WP_012457189.1; NZ_CP025930.1.
DR   AlphaFoldDB; B2RGR5; -.
DR   SMR; B2RGR5; -.
DR   STRING; 431947.PGN_0041; -.
DR   EnsemblBacteria; BAG32560; BAG32560; PGN_0041.
DR   GeneID; 29255298; -.
DR   KEGG; pgn:PGN_0041; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_2_10; -.
DR   OMA; MRRMKEM; -.
DR   BioCyc; PGIN431947:G1G2V-43-MON; -.
DR   Proteomes; UP000008842; 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; 3.30.565.10; -; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
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; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT   CHAIN           1..684
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000370694"
FT   REGION          1..329
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          330..548
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          549..684
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   CONFLICT        27
FT                   /note="K -> E (in Ref. 1; AAD51118)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        576
FT                   /note="K -> R (in Ref. 1; AAD51118)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        601
FT                   /note="T -> A (in Ref. 1; AAD51118)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   684 AA;  78221 MW;  6D7F328BD2B5FCC0 CRC64;
     MSKKGTIGVT SDNIFPVIKK FLYSDHKIFL REIVSNAVDA TQKLKTLTSV GEFKGETGDL
     RVTVSVDEVA RTITVSDRGV GMTEEEVEKY INQIAFSSAE EFLEKYKDDK AAIIGHFGLG
     FYSAFMVSER VDVITRSFRE DATAVKWSCD GSPEYTLEPA DKADRGTDIV MHIDEENSEF
     LKKEKIEGLL GKYCKFLTVP IIFGKKQEWK DGKMQDTDED NQINDTHPAW TKKPADLKDE
     DYKEFYRSLY PMSEEPLFWI HLNVDYPFNL TGILYFPKIK NNLDLQRNKI QLYCNQVYVT
     DEVQGIVPDF LTLLHGVIDS PDIPLNVSRS YLQSDANVKK ISSHITKKVA DRLEEIFKND
     RPTFEEKWDS LKLFVEYGML TDEKFYERAA KFFLFTDMDG HKYTFDEYRT LVEGVQTDKD
     GQVVYLYATD KHGQYSHVKR ASDKGYSVML LDGQLDPHIV SLLEQKLEKT HFVRVDSDTI
     NNLIRKEERA EVKLSDTERA TLVKLFEARL PRDEKKHFNV AFESLGAEGE AILITQAEFM
     RRMRDMAQLQ PGMSFYGELP DSYNLVLNTD HPLIDKVLSG EKESVEPSLT ELRAKIAELK
     TEEAKLLDEE KGKKPEEIPV ATKEAKENNA VEQAKTEGSI NDQLTKYAQD NELIGQLIDL
     ALLGSGLLTG EALAEFIRRS QRLL