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