ID   HTPG_MYCUA              Reviewed;         648 AA.
AC   A0PRT4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=MUL_2744;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
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; CP000325; ABL05053.1; -; Genomic_DNA.
DR   RefSeq; WP_011740667.1; NC_008611.1.
DR   AlphaFoldDB; A0PRT4; -.
DR   SMR; A0PRT4; -.
DR   STRING; 362242.MUL_2744; -.
DR   PRIDE; A0PRT4; -.
DR   EnsemblBacteria; ABL05053; ABL05053; MUL_2744.
DR   KEGG; mul:MUL_2744; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_11; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000000765; 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; Stress response.
FT   CHAIN           1..648
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014933"
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..648
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   648 AA;  72942 MW;  D7CA99963CDC19F0 CRC64;
     MNARVEQLEF QAEARQLLDL MIHSVYSNKD SFLRELISNA SDALDKLRIE AFRNKDLEVD
     TSDLHIETEA DKGARTLTVR DNGIGMTRAE VVDLIGTLAK SGTAELRAQL REAKNDAASE
     ELIGQFGIGF YSSFMVADKV ELLTRKAGES EATKWESSGE GTYTIESVEG APQGTSVTLH
     LKPEDAEDEL YDYTADWKLR HLIKKYSDFI AWPIRMEVEK RVPAPHEEGE EPGEETVVLE
     TETLNSMKAL WARPKDEVSA DEYNEFYKHI AHAWDDPMEV IAMKAEGTFE YQALLFIPSH
     AQHDLFNRDA VFGIQLYVKR VFIMGDCDQL MPEYLRFVKG VVDAQDMSLN VSREILQQDR
     QIKAIRRRLT KKVLSTIKDL QSERPEDYRT FWTQFGKVVK EGLLADFDNR ETLLEISSFA
     STHSEEEPTT LAGYVERMKE DQTQIFFATG DSRQQILKSP HLEAFRAKGY EVLLLTEPVD
     EVWVGVVNEF DGKPLQSVAK GEVDLDSDGE GSEAEREEQQ KEFADLLGWL KETLGEQVKE
     VRLSTRLTES PACLITDTFG ITPALARIYR ATGQDVPVGK RTLELNPTHP LVIGLRQAQA
     SADDDAKKEA VSETAELLYG TALLAEGGAP DDPARFAELL ADRLTRTL