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HTPG_LEGPA
ID   HTPG_LEGPA              Reviewed;         623 AA.
AC   Q5X5J7;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=lpp1323;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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; CR628336; CAH12474.1; -; Genomic_DNA.
DR   RefSeq; WP_011213666.1; NC_006368.1.
DR   AlphaFoldDB; Q5X5J7; -.
DR   SMR; Q5X5J7; -.
DR   KEGG; lpp:lpp1323; -.
DR   LegioList; lpp1323; -.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
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..623
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224213"
FT   REGION          1..336
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          337..550
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          551..623
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   623 AA;  71106 MW;  4B92FBE1DF75484E CRC64;
     MVSKQQTMGF QTEVKQMLHL VVHSLYSNKE IFLRELISNA SDALDKLRFL ALSNGSLFEN
     DSDLKISIQI NEKLQTITIS DNGIGLSWEE AVENLGTIAK SGTKEFISQL TGEQAKDSQL
     IGQFGVGFYS AFIVADKVTV KSRRAGLQPE DGIVWESKGD GEFTIGYEKK LTRGTEITLH
     LKPENDEFLS DWRIRGIISK YSDHICWPIL MKKLSEEGKE SKEFETVNKA TALWTLQKSE
     ISEEEYKQLY KHISHDYMDP LTWSHNHVEG KHEYITLLYI PAHAPFDLWQ HEAKHGLKLY
     VKRVFIMDEA TQFLPRYLRF VKGIVDASDL PLNISREILQ DNKQVESIRA ACTKRVLSML
     EKMATNDKET YQKFWNEFGL VLKEGPIEDF ANKEAIAKLL RFSTTASGSE KQEVSLEEYV
     SRMKEGQDKI YYITASSYNA AKNSPHLEIF RKKGIEVLLL SDKVDEWLVG YMNEFAGKKL
     QSISKGKIEL GDDETSEQIK EQEKTLEPLI KHIKSVLNDR VKDVLLTNRL TDSPACVVAD
     EQDMGLEMQR ILQAAGQQVP VSKPIFEINP DHALIKRLHD IQDDNQFELW VTMLFEQAVL
     AEGGQLDNPA DFVNRVNRLL VSS
 
 
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