ID   HTPG_BUCCC              Reviewed;         624 AA.
AC   Q057D9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=BCc_302;
OS   Buchnera aphidicola subsp. Cinara cedri (strain Cc).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=372461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cc;
RX   PubMed=17038625; DOI=10.1126/science.1130441;
RA   Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M.,
RA   Silva F.J., Moya A., Latorre A.;
RT   "A small microbial genome: the end of a long symbiotic relationship?";
RL   Science 314:312-313(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; CP000263; ABJ90760.1; -; Genomic_DNA.
DR   RefSeq; WP_011672679.1; NC_008513.1.
DR   AlphaFoldDB; Q057D9; -.
DR   SMR; Q057D9; -.
DR   STRING; 372461.BCc_302; -.
DR   EnsemblBacteria; ABJ90760; ABJ90760; BCc_302.
DR   KEGG; bcc:BCc_302; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000669; 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; 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; 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..624
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014898"
FT   REGION          1..338
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          339..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;  73125 MW;  E56C45944C8100CB CRC64;
     MNNKNKITHT FQSEVKELLH LMIHSLYSNK EIFLRELISN ASDAIEKIRF EKLYSLKKYR
     ENLYTPKIKI SIKKDEKKII ISDNGIGMTY KEVIKNLGTI AKSGTKSFLN KIQNIEKKEK
     NDFIGQFGVG FYSSFIVSNS VSVYTRHAKE KKNIGTLWIS EGKGKYSVEK ISKEEHGTIV
     ELSLKSSEKE FLEIWKIKNI IKKYSDHISI PIEIENYDEK TKTISWEKIN KAQALWTINK
     NNITKKKYQD FYKYLTNDSE KPLLWSHNKV EGTQEYINLL YIPKKATWDI WHQENKHGLK
     LYVKHVFIMD EATQFLPNYL RFVKGIIDSQ DLPLNISREI LQDSSITHIL RKSLTKRILN
     ILNNLSENNI KKYQKFWNVF GIIIKEGIAE DSENKTILSN LLRFSSIKKG NIEQTLSLNE
     YIKNMKKNQK KIYFITSDSY KSALNSPNLE IFKENDIDVL ILSEKIDEWM MNYLTEFNNI
     KFQSVSKLDD TIDSLLLKKN VSNEKNTFNE FIEKTKKILK NKVKDVKITY RLKNTPAIVL
     TDTNDMSTQM AKIFSAAGQP IPKIKYILEI NPLHPLIKKI EKIKNEKDFS NWIKIIFDQS
     ILSEKGSLEN PHKFIQRINN FFIS