HTPG_AGGAC
ID HTPG_AGGAC Reviewed; 626 AA.
AC P54649;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 107.
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};
OS Aggregatibacter actinomycetemcomitans (Actinobacillus
OS actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=714;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43718 / FDC Y4 Serotype B;
RX PubMed=8972900; DOI=10.1016/s0378-1119(96)00317-4;
RA Winston J.L., Toth S.I., Roe B.A., Dyer D.W.;
RT "Cloning and characterization of the Actinobacillus actinomycetemcomitans
RT gene encoding a heat-shock protein 90 homologue.";
RL Gene 179:199-204(1996).
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; U26968; AAC44732.1; -; Genomic_DNA.
DR PIR; JC5230; JC5230.
DR AlphaFoldDB; P54649; -.
DR SMR; P54649; -.
DR STRING; 714.ACT75_08045; -.
DR eggNOG; COG0326; Bacteria.
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..626
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000062965"
FT REGION 1..339
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 340..555
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 556..626
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 626 AA; 70993 MW; 4F7B2BB8E5700CED CRC64;
MSTNQETRGF QSEVKQLLQL MIHSLYSNKE IFLRELISNA SDAADKLRFK ALSNPDLYAG
DGELRVCISF DSEKGTLTVS DNGIGMTREQ VIDHLGTIAK SGTKEFLAAL GSDQAKDSQL
IGQFGVGFYS AFIVADKVTV KTRAAGEPAD KGVLWESAGE GDYTVADIEK KSRGTDVILH
LRDDEKEFLN EWRLRGIIGK YSDHIGLPVE MLTKEYEDEG KEIGEKWEKI NKSDALWTRS
KNEISDEEYK EFYKHLSHDF ADPLLWAHNK VEGNQEYTSL LYVPSKAPWD LFNREHKHGL
KLYVQRVFIM DDAEQFMPNY LRFMRGLIDS NDLPLNVSRE ILQDNKVTAA LRKALTKRSL
QMLEKLAKDD AEKYQQFWKE FGLVLKEGPA EDFANKEAIA KLLRFASTHN DSSEQNVSLE
DYVSRMKEGQ KAIYYITADS YVAARNSPHL ELFNKKGIEV LLLSDRIDEW MLSYLTEFDG
KPLQSITKAD LDLGDLADKE AEEQKAQDES FGSFVERVKT LLGGRVKEVR LTHRLTDTPA
VVSTDNDQMT TQMAKLFAAA GQPVPEVKYT FELNPEHHLV KKVAEIADEA QFADWVELLL
EQAMLAERGS LENPAAFIKR INKLLG
