HTPG_MYCTA
ID HTPG_MYCTA Reviewed; 647 AA.
AC A5U4Y2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=MRA_2316;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
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; CP000611; ABQ74082.1; -; Genomic_DNA.
DR RefSeq; WP_003411855.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U4Y2; -.
DR SMR; A5U4Y2; -.
DR STRING; 419947.MRA_2316; -.
DR EnsemblBacteria; ABQ74082; ABQ74082; MRA_2316.
DR GeneID; 45426279; -.
DR KEGG; mra:MRA_2316; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_11; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR Proteomes; UP000001988; 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_1000014932"
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