HTPG_WOLPM
ID HTPG_WOLPM Reviewed; 635 AA.
AC P61189;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=WD_1277;
OS Wolbachia pipientis wMel.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=163164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C.,
RA McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R.,
RA Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F.,
RA Nelson W.C., Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R.,
RA Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H.,
RA O'Neill S.L., Eisen J.A.;
RT "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a
RT streamlined genome overrun by mobile genetic elements.";
RL PLoS Biol. 2:327-341(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; AE017196; AAS14921.1; -; Genomic_DNA.
DR AlphaFoldDB; P61189; -.
DR SMR; P61189; -.
DR STRING; 163164.WD_1277; -.
DR EnsemblBacteria; AAS14921; AAS14921; WD_1277.
DR KEGG; wol:WD_1277; -.
DR eggNOG; COG0326; Bacteria.
DR OMA; MRRMKEM; -.
DR Proteomes; UP000008215; 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; 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; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
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..635
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000063025"
FT REGION 1..337
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 338..556
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 557..635
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 635 AA; 72668 MW; C88BA6F0CC773F5E CRC64;
MELKMHNVQE TENLKFDAEV GKVLNIVIHS LYTNKDIFLR ELISNASDAC DKLRYESQLN
PNLLDLSDEL KITISSNKDK NELYITDNGI GMNRQDLIDN LGTIASSGTQ KFLDAIKNSK
DSSQTVELIG KFGVGFYSSF MVASEVIVES RKAGEEESWI WQSKGDGEYS ISKSDNQVPR
GTKITLIMHP EENEFLDKFR VENIVTTYSD HINFPVEFID EEGKSEKLNS KAAIWTKPKN
DVTQEEHNDF FRSVAHVGGE PWMILHNKNE GAIEYTNLLY VPSIKPFDLF HPDRRCSVKL
YVNKVFITED NVQIIPQYLR FLKGIVDSPD LPLNISRETL QNNRVVEQIR KSLTKRAISE
LGKKAKENLE EYTKFWTNFG AVLKEGLCEA MPTDEREALL SICRFHSTGD EKLVSIDDYI
SRMKPEQEHI YYLTGNSLDS VKNSPQLEGF VSKGLEVLLF VDPVDDFWTS VIHEYKDQKI
KSVTRADVDL EKFSSEEDKT DEENKSNEEK TEETILQYFT TVLGDSVKSV KISKKLTDSP
VCLAVDEGAM DLRMERFLRE QKQLNYRTPK VLEINTKHPL IKSIMKSYAE SGENPTLEDM
IHLLFYQACI VEGEEMDDVS LFAKRLNNLL GKISV