HTPG_PSEA7
ID HTPG_PSEA7 Reviewed; 634 AA.
AC A6V7J7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=PSPA7_3678;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) 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; CP000744; ABR81297.1; -; Genomic_DNA.
DR RefSeq; WP_012076289.1; NC_009656.1.
DR AlphaFoldDB; A6V7J7; -.
DR SMR; A6V7J7; -.
DR EnsemblBacteria; ABR81297; ABR81297; PSPA7_3678.
DR KEGG; pap:PSPA7_3678; -.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR Proteomes; UP000001582; 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..634
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000014939"
FT REGION 1..342
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 343..559
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 560..634
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 634 AA; 71555 MW; EA538920A6BC6E29 CRC64;
MSVETQKETL GFQTEVKQLL HLMIHSLYSN KEIFLRELIS NASDAADKLR FEALANPELL
EGGAELKIRV SFDKEANTVT LEDNGIGMSR EDVVTHLGTI AKSGTADFLK NLSGDQKKDS
HLIGQFGVGF YSAFIVADKV DVYSRRAGQP ASEGVHWSSK GEGEFDVATI DKPERGTRIV
LHLKKGEEEF ADGWRLRNVI KKYSDHIALP IELPKEFHGE EAEKPAEPEW ETVNRASALW
TRPRAEVKDE EYQEFYKHVA HDFENPLSWS HNKVEGKLEY TSLLYVPGRA PFDLYHREAP
RGLKLYVQRV FIMDQADEFL PLYLRFIKGV VDSNDLSLNV SREILQKDPV IDSMKSALTK
RVLDMLEKLA KNEPEQYKTF WKNFGQVLKE GPAEDFGNKE KIAGLLRFAS TGGDSGEQSV
ALADYIGRMK EGQDKIYYLT GESYSQVKNS PHLEVFRKKG IEVLLLTDRI DEWLMSYLPD
FDGKSFVDVA RGDLDLGSLD SEEDKKAQEE VAKSKEGLIE RLKKVLDEQA SEVRVSHRLT
DSPAILAIGE QDLGLQMRQI LEASGQKVPE SKPIFEINPQ HPLIEKLDAE PDEDRFGELS
HILFDQAALA AGDSLKDPGA YVRRLNKLLV ELSA
