ID   HTPG_MYCVP              Reviewed;         651 AA.
AC   A1T639;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Mvan_1817;
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000511; ABM12639.1; -; Genomic_DNA.
DR   RefSeq; WP_011779057.1; NC_008726.1.
DR   AlphaFoldDB; A1T639; -.
DR   SMR; A1T639; -.
DR   STRING; 350058.Mvan_1817; -.
DR   EnsemblBacteria; ABM12639; ABM12639; Mvan_1817.
DR   KEGG; mva:Mvan_1817; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_11; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000009159; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..651
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014934"
FT   REGION          1..353
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          354..569
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          570..651
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   651 AA;  73460 MW;  14B881014279A59C CRC64;
     MAAHVEQLEF QAEARQLLDL MIHSVYSNKD SFLRELVSNA SDALDKLRLE SFRNKDLDVD
     TSDLHIEIDV DKEARTLTVR DNGIGMTRDE VVSLIGTLAK SGTGELRQQL REAKDKDTSE
     ELIGQFGIGF YASFMVADRV ELLTRKAGES EATRWESSGE GTYTIETVDQ AGGEVPQGTS
     VTLHLKPEDR EDELHDYTSE WKIRELVKQY SDFIAWPIRM EVERRTPAPE DGGEESVTVE
     TETLNSMKAL WARPRDEVSD EEYTEFYKHV AHAWDEPLEV IAMKAEGTFE YQALLFIPSH
     APFDLFNQNA AVGVQLYVKR VFIMGDCDQL MPPYLRFVKG VVDAQDMSLN VSREILQQDR
     QIRAIRRRLT KKVLSTITEM QTERPEKYRT FWTQFGRVLK EGLLTDIENQ ETLLRVCSFA
     STHSEDEPTT LAEYVERMPD GQSQIFYAAG ESRQQLLHSP HLEAFKAKGY EVLLLTDPVD
     EVWVESVHEF DGKPLQSVAK GEVDLDSDAD NDGQDAERQE REQGFADLIA WLKEALSDHV
     KEVRLSTRLT DSPACLITDT FGITPALARM YRASGQPVPV EKRILELNPN HPLITGLREA
     HKSRGADAEL VGTAELLYGT ALLAEGGVLE DPARFAGLLA DRLTRTVGDQ T