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HTPG_LEGPC
ID   HTPG_LEGPC              Reviewed;         623 AA.
AC   A5IBL1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=LPC_0785;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000675; ABQ54761.1; -; Genomic_DNA.
DR   RefSeq; WP_011946395.1; NC_009494.2.
DR   AlphaFoldDB; A5IBL1; -.
DR   SMR; A5IBL1; -.
DR   KEGG; lpc:LPC_0785; -.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   BioCyc; LPNE400673:LPC_RS07165-MON; -.
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_1000014926"
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;  71080 MW;  D150E293BFC17ABC 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
     ISEEDYKQLY KHISHDYMDP LTWSHNHVEG KHEYITLLYI PAHAPFDLWQ HEAKHGLKLY
     VKRVFIMDEA TQFLPRYLRF VKGIVDASDL PLNISREILQ DNKQVESIRA ACTKRVLSML
     EKMATNDKET YQKFWNEFGL VLKEGPIEDF ANKEAIAKLL RFSTTASGSE KQEVSLEEYI
     SRMKEGQDKI YYITASSYNA AKNSPHLEIF RKKGIEVLLL SDKVDEWLVG YMNEFAGKKL
     QSISKGKIEL GDDETSEQIK EQEKTLEPLI KHIKSVLNER VKDVLLTNRL TDSPACVVAD
     EQDMGLEMQR ILQAAGQQVP VSKPIFEINP DHALIKRLHD IQDDNQFELW VTMLFEQAVL
     AEGGQLDNPA DFVNRVNRLL VSS
 
 
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