ID   HTPG_MYCTO              Reviewed;         647 AA.
AC   P9WMJ6; L0TC38; P64411; Q50667;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 41.
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=MT2356;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK46641.1; -; Genomic_DNA.
DR   PIR; G70733; G70733.
DR   RefSeq; WP_003411855.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMJ6; -.
DR   SMR; P9WMJ6; -.
DR   EnsemblBacteria; AAK46641; AAK46641; MT2356.
DR   GeneID; 45426279; -.
DR   KEGG; mtc:MT2356; -.
DR   PATRIC; fig|83331.31.peg.2536; -.
DR   HOGENOM; CLU_006684_3_0_11; -.
DR   Proteomes; UP000001020; 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..647
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000427292"
FT   REGION          1..353
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          354..567
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          568..647
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   647 AA;  72961 MW;  FE2C7C6F2398D741 CRC64;
     MNAHVEQLEF QAEARQLLDL MVHSVYSNKD AFLRELISNA SDALDKLRIE ALRNKDLEVD
     TSDLHIEIDA DKAARTLTVR DNGIGMAREE VVDLIGTLAK SGTAELRAQL REAKNAAASE
     ELIGQFGIGF YSSFMVADKV QLLTRKAGES AATRWESSGE GTYTIESVED APQGTSVTLH
     LKPEDAEDDL HDYTSEWKIR NLVKKYSDFI AWPIRMDVER RTPASQEEGG EGGEETVTIE
     TETLNSMKAL WARPKEEVSE QEYKEFYKHV AHAWDDPLEI IAMKAEGTFE YQALLFIPSH
     APFDLFDRDA HVGIQLYVKR VFIMGDCDQL MPEYLRFVKG VVDAQDMSLN VSREILQQDR
     QIKAIRRRLT KKVLSTIKDV QSSRPEDYRT FWTQFGRVLK EGLLSDIDNR ETLLGISSFV
     STYSEEEPTT LAEYVERMKD GQQQIFYATG ETRQQLLKSP HLEAFKAKGY EVLLLTDPVD
     EVWVGMVPEF DGKPLQSVAK GEVDLSSEED TSEAEREERQ KEFADLLTWL QETLSDHVKE
     VRLSTRLTES PACLITDAFG MTPALARIYR ASGQEVPVGK RILELNPSHP LVTGLRQAHQ
     DRADDAEKSL AETAELLYGT ALLAEGGALE DPARFAELLA ERLARTL