ID   HTPG_MYCLE              Reviewed;         656 AA.
AC   O33012;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 123.
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=ML1623;
GN   ORFNames=MLCB250.19c;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; Z97369; CAB10613.1; -; Genomic_DNA.
DR   EMBL; AL583922; CAC30574.1; -; Genomic_DNA.
DR   PIR; A87112; A87112.
DR   RefSeq; NP_302118.1; NC_002677.1.
DR   RefSeq; WP_010908439.1; NC_002677.1.
DR   AlphaFoldDB; O33012; -.
DR   SMR; O33012; -.
DR   STRING; 272631.ML1623; -.
DR   EnsemblBacteria; CAC30574; CAC30574; CAC30574.
DR   KEGG; mle:ML1623; -.
DR   PATRIC; fig|272631.5.peg.3058; -.
DR   Leproma; ML1623; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_11; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000000806; 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; Reference proteome;
KW   Stress response.
FT   CHAIN           1..656
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000062994"
FT   REGION          1..359
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          360..575
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          576..656
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   656 AA;  73866 MW;  A526690CA66E03FF CRC64;
     MSAQVEQLEF QAEARQLLDL MVHSVYSNKD AFLRELISNA SDALDKLRLE AFRNKDLDPR
     TVDTSDLHIE IEVDKNTRIL TVRDNGIGMT RAEVVDLIGT LAKSGTAKLR QKLHAAKNLK
     DTAASEGLIG QFGIGFYSSF MVANKVELLT RKAGETAATR WSSDGEATYT IESVDEAPQG
     TSVTLHLKPE DFEDELHDYT SEWKIRELVK KYSDFIAWPI RMEVERRAPA TSDGEGADGE
     EQVTIETQTI NSMKALWTKS KDEVSEDEYK EFYKHIAHAW DDPLEVIAMK AEGTFEYQAL
     LFIPSHAPFD LFNSDAKIGM QLYVKRVFIM SDCDQLMPMY LRFVKGVVDA EDMSLNVSRE
     ILQQNRQINA IRRRLTKKVL SAIKDLQAER PQDYRTFWTQ FGKVLKEGLM SDSDNRDTLL
     HISSFASTHS DEEPTTLAQY VERMKDGQDQ IFYATGESRQ QVMNSPHLEA FKAKGYEVLL
     LTDPVDEVWV GMAPEFDGKP LKSVARGEVD LESEEEKTAH EAERKEQEQN FAGLVNWLKE
     TLSDHVKEVR LSTRLTESPA CLITDAFGIT PALARIYRAS GQDVPFGKRI LELNPNHPLI
     TGLQQAHENG GDDTHLRQLS ETAELLYGTA LLAEGGALEN PAKFAGLLAD LLSRSM