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