HTPG_MYCTU
ID HTPG_MYCTU Reviewed; 647 AA.
AC P9WMJ7; L0TC38; P64411; Q50667;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
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=Rv2299c;
GN ORFNames=MTCY339.11;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP45081.1; -; Genomic_DNA.
DR PIR; G70733; G70733.
DR RefSeq; NP_216815.1; NC_000962.3.
DR RefSeq; WP_003411855.1; NZ_NVQJ01000012.1.
DR AlphaFoldDB; P9WMJ7; -.
DR SMR; P9WMJ7; -.
DR STRING; 83332.Rv2299c; -.
DR PaxDb; P9WMJ7; -.
DR DNASU; 887501; -.
DR GeneID; 45426279; -.
DR GeneID; 887501; -.
DR KEGG; mtu:Rv2299c; -.
DR TubercuList; Rv2299c; -.
DR eggNOG; COG0326; Bacteria.
DR OMA; MRRMKEM; -.
DR PhylomeDB; P9WMJ7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0071451; P:cellular response to superoxide; IEP:MTBBASE.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..647
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000062996"
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
