ID   HTPG_METEP              Reviewed;         626 AA.
AC   A9W1H7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Mext_1028;
OS   Methylorubrum extorquens (strain PA1) (Methylobacterium extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=419610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA1;
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., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Marx C., Richardson P.;
RT   "Complete sequence of Methylobacterium extorquens PA1.";
RL   Submitted (DEC-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; CP000908; ABY29433.1; -; Genomic_DNA.
DR   RefSeq; WP_012252718.1; NC_010172.1.
DR   AlphaFoldDB; A9W1H7; -.
DR   SMR; A9W1H7; -.
DR   STRING; 419610.Mext_1028; -.
DR   PRIDE; A9W1H7; -.
DR   EnsemblBacteria; ABY29433; ABY29433; Mext_1028.
DR   KEGG; mex:Mext_1028; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   BioCyc; MEXT419610:MEXT_RS05160-MON; -.
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; 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   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..626
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000127029"
FT   REGION          1..331
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          332..544
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          545..626
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   626 AA;  69338 MW;  9B165F2A3C9A052C CRC64;
     MSETVERHEF GAEVGRLLDL VVHALYSDRE IFLRELVANA ADATDRRRFE ALTNEALALP
     SDARVLIAPD KAARTLTISD AGIGMSKEDL AQNLGTIARS GTRAFSQALG ERAAEGGEDQ
     RPSLIGQFGV GFYSAFMVAD RVTVTSRRAG SEEAWTWASD GKGSYTLEPA SREQPGTDIV
     LHMKEDADEY LESYRLDHVV RKWADNIAVP IAIRDAEGKE EAANRGTALW RKPKSEITEE
     QYKEFYRTVS HGFDEPWATL HWRAEGALEF TGLLFVPSMK PFMPMEDDRR SKVRLHVRRM
     FITDEAELLP NWLRFVHGVV DTDDLPLNVS REMLQSTPTL QKIRRAVTTR VINELSSRSK
     NAEKAEEYQK FFENFGPVLK EGIYEDFERR GEIAPLLRFR SSTEGGWTSL PEYVARMKPE
     QEAIYYLVAD DVEALKNSAQ LEGFRARGVE VLLLSDHVDA FWPEQLGKFE DKPLRSVTQG
     SADLAKLKPE GETAEAAPAL DTLVAALKLA LEPDVSDVRT TDRLVDSAVV LATSGMGPDL
     QMQRLLRRAG RGFGGSAPIL EINPRHALIR SLNERAEAGE DLKAEAGTLL DLARVQDGDT
     PRDPVAFARA VAAALAGTAA KPAESA