ID   HTPG_PORGI              Reviewed;         684 AA.
AC   P0C938; Q9S3Q2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=PG_0045;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
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; AE015924; AAQ65296.1; -; Genomic_DNA.
DR   RefSeq; WP_005873540.1; NC_002950.2.
DR   AlphaFoldDB; P0C938; -.
DR   SMR; P0C938; -.
DR   STRING; 242619.PG_0045; -.
DR   EnsemblBacteria; AAQ65296; AAQ65296; PG_0045.
DR   KEGG; pgi:PG_0045; -.
DR   PATRIC; fig|242619.8.peg.41; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_2_10; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   BioCyc; PGIN242619:G1G02-41-MON; -.
DR   Proteomes; UP000000588; 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; IPR019805; Heat_shock_protein_90_CS.
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.
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..684
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000063002"
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"
SQ   SEQUENCE   684 AA;  78220 MW;  8384A999F32378B6 CRC64;
     MSKKGTIGVT SDNIFPVIKK FLYSDHEIFL 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 HPLIDRVLSG EKESVEPSLT ELRAKIAELK
     AEEAKLLDEE KGKKPEEIPV ATKEAKENNA VEQAKTEGSI NDQLTKYAQD NELIGQLIDL
     ALLGSGLLTG EALAEFIRRS QRLL