HTPG_LEGPL
ID HTPG_LEGPL Reviewed; 623 AA.
AC Q5WWX9;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=lpl1320;
OS Legionella pneumophila (strain Lens).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lens;
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; CR628337; CAH15560.1; -; Genomic_DNA.
DR RefSeq; WP_011215391.1; NC_006369.1.
DR AlphaFoldDB; Q5WWX9; -.
DR SMR; Q5WWX9; -.
DR EnsemblBacteria; CAH15560; CAH15560; lpl1320.
DR KEGG; lpf:lpl1320; -.
DR LegioList; lpl1320; -.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OMA; MRRMKEM; -.
DR Proteomes; UP000002517; 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..623
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000224212"
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; 71094 MW; F0E906E698604D26 CRC64;
MVSKQQTMGF QTEVKQMLHL VVHSLYSNKE IFLRELISNA SDALDKLRFL ALSNGSLFEN
DSDLKISIQI NEKLQTITIS DNGIGLSWEE AVENLGTIAK SGTKEFISQL TGEQAKDSQL
IGQFGVGFYS AFIVADKVTV KSRRAGLQPE DGIVWESKGD GEFTIGYEKK STRGTEITLH
LKPENDEFLS DWRIRGIISK YSDHICWPIV MKKLSEEGKE SKEFETVNKA TALWTLQKSE
IGEEDYKQLY KHISHDYMDP LTWSHNHVEG KHEYITLLYI PAHAPFDLWQ HEAKHGLKLY
VKRVFIMDEA TQFLPRYLRF IKGIVDASDL PLNISREILQ DNKQVESIRA ACTKRVLSML
EKMATNDKET YQKFWNEFGL VLKEGPIEDF ANKEAIAKLL RFSTTASGSE KQEVSLEEYV
SRMKEGQDKI YYITASSYNA AKNSPHLEIF RKKGIEVLLL SDKVDEWLVG YMNEFTGKKL
QSISKGKVEL GDDETSEQIK EQEKTLEPLI KHIKSVLNER VKDVLLTNRL TDSPACVVAD
EQDMGLEMQR ILQAAGQQIP VSKPIFEINP EHALIKRLHD IQDDNQFELW VTMLFEQAVL
AEGGQLDNPA DFVNRVNRLL VSS