ID   HTPG_PHOLL              Reviewed;         630 AA.
AC   Q7N0P4;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 111.
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=plu3837;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571871; CAE16209.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7N0P4; -.
DR   SMR; Q7N0P4; -.
DR   STRING; 243265.plu3837; -.
DR   EnsemblBacteria; CAE16209; CAE16209; plu3837.
DR   KEGG; plu:plu3837; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000002514; 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; Reference proteome;
KW   Stress response.
FT   CHAIN           1..630
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000063001"
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..630
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   630 AA;  72307 MW;  E8892652ED066775 CRC64;
     MKGQETRGFQ SEVKQLLQLM IHSLYSNKEI FLRELISNAS DAADKLRFRA LSVPKLYEND
     GELRVRLSFD KEKRCITISD NGIGMTRDEV IDNLGTIAKS GTKAFLESIG SDQAKDSQLI
     GQFGVGFYSA FIVSDKVTVR TRAAGASIDQ GVFWESAGEG DYTIADIEKE TRGTEITLHL
     REGEDEFLND WRLRSVISKY SDHIALPVEI ETKNKSEEEG EEDTVTWEKI NKAQALWTRG
     KSEITDEEYK EFYKHISHDF TDPLIWSHNR VEGKQEYTSM LYIPSQAPWD MWNREHKHGL
     KLYVQRVFIM DDAEQFMPNY LRFVRGLIDS NDLPLNVSRE ILQDNSITRN LRNALTKRAL
     QMLDKLAKDD AEKYQQFWQQ FGLVMKEGPA EDSTNKEAIA KLLRFASTHN DSSAQTVSLE
     EYVSRMTEGQ DKIYYITADS YAAAKNSPHL ELFRKKGIEV LLLSERIDEW MMGYLTDFDG
     KKFQSVSKAD ESLDKLADEN KAEQEEIEKQ LEPFVERVKT LLGDRVKEVK LTHRLTDTPA
     IVTTNVDEMS TQMAKLFAAA GQQVPDVKYN FELNPDHQLV KLAADISDEV QFADWIELLL
     DQALFAERGT LEDPNQFIRR MNQLLLSEKA