ID   HTPG_RHIEC              Reviewed;         630 AA.
AC   Q2JZH2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 103.
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=RHE_PF00122;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OG   Plasmid p42f.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000138; ABC94014.1; -; Genomic_DNA.
DR   RefSeq; WP_011428431.1; NC_007766.1.
DR   AlphaFoldDB; Q2JZH2; -.
DR   SMR; Q2JZH2; -.
DR   EnsemblBacteria; ABC94014; ABC94014; RHE_PF00122.
DR   KEGG; ret:RHE_PF00122; -.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000001936; Plasmid p42f.
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; IPR036890; HATPase_C_sf.
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   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Plasmid;
KW   Reference proteome; Stress response.
FT   CHAIN           1..630
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258520"
FT   REGION          1..336
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          337..551
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          552..630
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   630 AA;  70274 MW;  E6F6C5DC89F3AD00 CRC64;
     MTTTVEQTAE SHVFEADVAR LLHMMVHSVY SDKGVFLREL ISNGADACEK LRYEAIETPS
     LLAADAESRI MLRLDEESRQ LVVEDNGIGM RRDEMIEALG TIARSGTRAF MERIAENKAA
     EGAQFIGQFG VGFYSCFMVA EHVDVISRRA GSEEAWKWSS DGKGSYSVEA ANLVEAPARG
     TRIVLHLMED AKTYTSRWTV ERIVKEQSGH VPVAIRIVDK PGGEPVQITD GTALWTKSKS
     EVSKEDYTDF YRGLSGQYDE PALTVHFRAE GRHEYTALAF VPGTQPFDMF DPERKGRMKL
     YVKRVFITDD AELMPRYLRF VRGLIDTADL PLNVSREMIQ ESPILAAIRK GVTNRVITAI
     EKLADGESET YLTFWKNFGP VLKEGIYEDY ERRAQLMALA RFHTSASPEG HRSLAEYVKD
     AKEGQDAIYY LAGGSLDQLK ASPQLEGFRA RGIEVLLLTD SVDSFWVVNA PEFEGKAFKS
     ITQGTADLAQ FPRLDNQTPP EQDSAGLATF IGFAREKLAG QVADVRASDR LTESAVCLVA
     PEDGYDRQME KILQNAGRLQ GATKPILEIN LAHPVIKAIA AVEDDASYQE DATFLLLDQA
     RILDGERPQD PRKFAQRLAR VFERSVRSEG