ID   HTPG_RHILO              Reviewed;         628 AA.
AC   Q98JB6;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 110.
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=mlr2017;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB49250.1; -; Genomic_DNA.
DR   RefSeq; WP_010910602.1; NC_002678.2.
DR   AlphaFoldDB; Q98JB6; -.
DR   SMR; Q98JB6; -.
DR   STRING; 266835.14022641; -.
DR   EnsemblBacteria; BAB49250; BAB49250; BAB49250.
DR   KEGG; mlo:mlr2017; -.
DR   PATRIC; fig|266835.9.peg.1621; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000552; 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; 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..628
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000063007"
FT   REGION          1..333
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          334..549
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          550..628
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   628 AA;  69283 MW;  8A92F1EC9C8DF3B9 CRC64;
     MTTDTKATET RAFEADVSRL LHMMVHSVYS DKDVFLRELI SNAADACEKL RFEAVSRPEL
     LGDDPKPRIS ISADPDNKEI TVEDNGIGMS RDDMAEALGT IARSGTRAFI ERVGSGTEDT
     QLIGQFGVGF YSAFMVADRV DVISRLAGSE EAWRWSSDGK GSYEIAPAPL EAAPRRGTRV
     VLHLMDDAVS YTGSYRLEQL AKSQSGHVPV PITLIEKPGA EARDIADGTA LWVRPKSEIK
     PEEYTDFYRS VAGQYDEPAA TIHFRAEGRQ EYSVLAFVPG SRPFDLFDQD RKGRMKLYVR
     RVFITDDADL LPRYLRFVRG LVDSADLPLN VSREMIQESP LLASIRKGLT NRVLGDLAKL
     AENEAEAYAK VWENFGVVLK EGLYEDYERR EQLLKLARFH STASGEGWRG LADYVAAMKE
     GQKAIFFMAG DDRARLEASP QLEGFKARGI EVLLLTDPVD SFWVTMAPDF DGKPFKSVTQ
     GVAELSDIPL LDDAKKPDTA AAPEVDGFLA FVKSALGDAV SDVKASDRLT ESAVCLVAPE
     HGPDRQFERL MNAAGRLDKA AKPILEINPR HERVLALAGL GDEDQAFKDD AAHLLYDEAR
     VLDGDKPADA RAFSERLARL IARGIAKG