ID   HTPG_ECOUT              Reviewed;         624 AA.
AC   Q1RF62;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=UTI89_C0501;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE06002.1; -; Genomic_DNA.
DR   RefSeq; WP_000678211.1; NC_007946.1.
DR   AlphaFoldDB; Q1RF62; -.
DR   SMR; Q1RF62; -.
DR   PRIDE; Q1RF62; -.
DR   EnsemblBacteria; ABE06002; ABE06002; UTI89_C0501.
DR   KEGG; eci:UTI89_C0501; -.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000001952; 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; Stress response.
FT   CHAIN           1..624
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258510"
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;  71437 MW;  72CB4DD14230560E CRC64;
     MKGQETRGFQ SEVKQLLHLM IHSLYSNKEI FLRELISNAS DAADKLRFRA LSNPDLYEGD
     GELRVRVSFD KDKRTLTISD NGVGMTRDEV IDHLGTIAKS GTKSFLESLG SDQAKDSQLI
     GQFGVGFYSA FIVADKVTVR TRAAGEKPEN GVFWESAGEG EYTVADITKE DRGTEITLHL
     REGEDEFLDD WRVRSIISKY SDHIALPVEI EKREEKDGET VISWEKINKA QALWTRNKSE
     ITDEEYKEFY KHIAHDFNEP LTWSHNRVEG KQEYTSLLYI PSQAPWDMWN RDHKHGLKLY
     VQRVFIMDDA EQFMPNYLRF VRGLIDSSDL PLNVSREILQ DSTVTRNLRN ALTKRVLQML
     EKLAKDDAEK YQTFWQQFGL VLKEGPAEDF ANQEAIAKLL RFASTHTDSS AQTVSLEDYV
     SRMKEGQEKI YYITADSYAA AKSSPHLELL RKKGIEVLLL SDRIDEWMMN YLTEFDGKPF
     QSVSKVDESL EKLADEVDES AKEAEKALTP FIDRVKALLG ERVKDVRLTH RLTDTPAIVS
     TDADEMSTQM AKLFAAAGQK VPEVKYIFEL NPDHVLVKRA ADTEDEAKFS EWVELLLDQA
     LLAERGTLED PNLFIRRMNQ LLVS