ID   HTPG_SALTI              Reviewed;         624 AA.
AC   P58479;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 129.
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};
GN   OrderedLocusNames=STY0531, t2373;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO69964.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAD04972.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL513382; CAD04972.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014613; AAO69964.1; ALT_INIT; Genomic_DNA.
DR   PIR; AB0563; AB0563.
DR   RefSeq; NP_455083.1; NC_003198.1.
DR   AlphaFoldDB; P58479; -.
DR   SMR; P58479; -.
DR   STRING; 220341.16501758; -.
DR   EnsemblBacteria; AAO69964; AAO69964; t2373.
DR   KEGG; stt:t2373; -.
DR   KEGG; sty:STY0531; -.
DR   PATRIC; fig|220341.7.peg.533; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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_0000063012"
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;  71501 MW;  FD24A7B0193CA023 CRC64;
     MKGQETRGFQ SEVKQLLHLM IHSLYSNKEI FLRELISNAS DAADKLRFRA LSNPDLYEGD
     GELRVRVSFD KDKRTLTIAD NGVGMNRDEV IDHLGTIAKS GTKSFLESMG SDQAKDSQLI
     GQFGVGFYSA FIVADKVTVR TRAAGDKPEN GVFWESAGEG EYTVADITKN DRGTEITLHL
     REGEDEFLDD WRVRSIISKY SDHIALPVEI EKREEKDGET VISWEKINKA QALWTRNKSE
     IKDDEYNEFY KHIAHDFTDP LTWSHNRVEG KQEYTSLLYI PSQAPWDLWN RDHKHGLKLY
     VQRVFIMDDA EQFMPNYLRF VRGLIDSNDL PLNVSREILQ DSTVTRNLRS ALTKRVLQML
     EKLAKDDAEK YQTFWKQFGL VLKEGPAEDH ANQEAIAKLL RFASTHTDSS AQTVSLEDYV
     SRMKEGQEKI YYITADSYAA AKNSPHLELL RKKGIEVLLL SDRIDEWMMN YLTEFDGKAF
     QSVAKADESI EKLADEVDEN AKEAEKALEP FVERVKTLLG DRVKEVRLTH RLTDTPAIVT
     TDADEMSTQM AKLFAAAGQS VPEVKYIFEL NPDHVLVKRT ADTKDEAQFK EWVELLLDQA
     LFAERGTLED PNQFIRRMNQ LLVS