ID   HTPG_PSEMY              Reviewed;         634 AA.
AC   A4XV81;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=Pmen_2491;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-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; CP000680; ABP85247.1; -; Genomic_DNA.
DR   RefSeq; WP_012018789.1; NC_009439.1.
DR   AlphaFoldDB; A4XV81; -.
DR   SMR; A4XV81; -.
DR   STRING; 399739.Pmen_2491; -.
DR   EnsemblBacteria; ABP85247; ABP85247; Pmen_2491.
DR   KEGG; pmy:Pmen_2491; -.
DR   PATRIC; fig|399739.8.peg.2517; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
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_1000014940"
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;  71503 MW;  536A2B82DA39C93D CRC64;
     MSVETQKETL GFQTEVKQLL HLMIHSLYSN KEIFLRELIS NASDAADKLR FEALAKPELL
     EGGAELKIRL SFDKDAKTVT LEDNGIGMSR DEVIAHLGTI AKSGTADFLK NLSGDQKKDS
     HLIGQFGVGF YSAFIVADKV DVFTRRAGLS AAEGVHWSSK GEGEFEVATV EKAERGTRIV
     LHLKSGEEEF ADGWRLRNIV KKYSDHIALP IELPKEHYGE EKDKPAEVEW ETVNRASALW
     TRPRAEVKDE EYQEFYKHVA HDFENPLTWS HNKVEGKLEY TSLLYVPGRA PFDLYHREAP
     KGLKLYVQRV FIMDQADEFL PLYLRFIKGV VDSNDLSLNV SREILQKDPV IDSMKSALTK
     RVLDMLEKLA KDKPEEYKAF WKAFGQVLKE GPAEDFANKE KIAGLLRFAS TAGEGDEQSV
     SLADYLGRVK DGQDKIYYLT GESYAQIKNS PHLEVFRKKG IEVLLLTDRI DEWLMSYLTE
     FDGKQFVDVA RGDLDLGKLD SEEDKKAQEE VAKAKEGLIE RLKGALGEQV KEVRVSHRLT
     DSPAILAIGE QDLGLQMRQI LEASGQKVPE SKPIFEFNPS HPLIERLDAE ADEDRFVDLT
     HILFDQAALA AGDSLKDPAA YVQRLNKLLV ELSA