ID   HTPG_BUCAI              Reviewed;         624 AA.
AC   P57555;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 113.
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=BU483;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13180.1; -; Genomic_DNA.
DR   RefSeq; NP_240294.1; NC_002528.1.
DR   RefSeq; WP_009874437.1; NC_002528.1.
DR   AlphaFoldDB; P57555; -.
DR   SMR; P57555; -.
DR   STRING; 107806.10039146; -.
DR   PRIDE; P57555; -.
DR   EnsemblBacteria; BAB13180; BAB13180; BAB13180.
DR   KEGG; buc:BU483; -.
DR   PATRIC; fig|107806.10.peg.492; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000001806; 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..624
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000062975"
FT   REGION          1..336
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          337..552
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          553..624
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   624 AA;  72816 MW;  75039E0B64F6C469 CRC64;
     MKTQKKEVYN FQSETKKLLH LMIHSLYSNK EIFLRELISN SSDAIDKLRF ESISSPELYE
     NDSDVKIQIS INKAQRTLII SDNGIGMTKE DTIENLGTIA KSGTKSFLQS LEQKQNKKNE
     LIGEFGVGFY SSFIVSEKVS VRTRFAGLES NKGILWESSG EGEYNITNIV KKTRGTEITL
     FLKKEEEEFL ETWRIKNIIS KYSDHITIPI HIQDYDKKNK TYFWEQINKA KALWTLNKSS
     ITEEEYKDFY KHLTNDQNDP LIWSHNHVEG NQEYISLLYI PEKAAWDIWN RDNKHGLKLY
     VKRVYIMDNS QAFLPNYLRF IKGLIDSSDL PLNISREILQ DNSITEKLRK SLIKKSLSML
     EKLAQKNNEK YQIFWNQFGL VLKEGPAEDH ENLNKIANLL RFTSMKSNNS EQKMSLKEYI
     SNMNEQQEKI YYITADSYSS ANNSPHLELF KKNNIDVLLL SDRIDEWMMN YLSEFEGKKF
     QSISKEDISL NKLTKEKKIK NKDVSTEMIE FLKKVKNILG NQVKDVRLTH RLTETPCVLL
     SDSTEMTTQM AKLFSAAGQS VPELKYIFEI NPDHILIKKI CTINNENELH QWIKLLLDQA
     LLAEKGNLEN PHKFISRMNK LLIK