ID   HTPG_MYCGI              Reviewed;         651 AA.
AC   A4TFF4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=Mflv_4650;
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL   Submitted (APR-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; CP000656; ABP47118.1; -; Genomic_DNA.
DR   RefSeq; WP_011895486.1; NC_009338.1.
DR   AlphaFoldDB; A4TFF4; -.
DR   SMR; A4TFF4; -.
DR   STRING; 350054.Mflv_4650; -.
DR   EnsemblBacteria; ABP47118; ABP47118; Mflv_4650.
DR   KEGG; mgi:Mflv_4650; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_11; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
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; Stress response.
FT   CHAIN           1..651
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000081520"
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;  73566 MW;  0F228CFC4F92AD4F CRC64;
     MAPHVEQLEF QAEARQLLDL MIHSVYSNKD SFLRELISNA SDALDKLRLE AFRNKDLDVD
     TSDLHIEIVV DKEARTLTVR DNGIGMSRDE VVRLIGTLAK SGTAELRQQL REAKDANANE
     ELIGQFGIGF YASFMVADRV ELLTRKAGES EATRWESTGE GSYTIETVDQ AGGEVPQGTS
     VTLHLKPEDR EDELHDYTSE WKIRELVKQY SDFIAWPVRM DVERRTPASE EGGEETVTVE
     TQTLNSMKAL WARPRDEVSD EEYTEFYKHV AHAWDEPLET IAMRAEGTFE YQALLFIPSH
     APFDLFQQNA TVGVQLYVKR VFIMGDCDQL MPPYLRFVKG VVDAQDMSLN VSREILQQDR
     QIRAIRRRLT KKVLSTIAEM QAERPEKYRT FWTQFGRVLK EGLLSDTDNQ ETLLRVSSFA
     STRSDDEPTT LAEYVERMPE GQTQIFYAAG ESRQQLLNSP HLEAFKAKGY EVLLLTDPVD
     EVWVESIHEF DGKPLQSVAK GEVDLDSEAD KEAQETERQQ REKEFADVIA WLTEVLGDHV
     KEVRLSTRLT DSPACLITDT FGITPALARM YRASGQPVPV EKRILELNPT HPLVVGLREA
     HESRGADDEL AGTAELLYGT ALLAEGGALE DPARFAGLLA DRLTRMVGEQ S