ID HTPG_MYCTU Reviewed; 647 AA.
AC P64411; L0TC38; Q50667;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 01-MAY-2013, entry version 59.
DE RecName: Full=Chaperone protein HtpG;
DE AltName: Full=Heat shock protein HtpG;
DE AltName: Full=High temperature protein G;
GN Name=htpG; OrderedLocusNames=Rv2299c, MT2356; ORFNames=MTCY339.11;
OS Mycobacterium tuberculosis.
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1773;
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.,
RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the
RT complete genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
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.,
RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA 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 (By
CC similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
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DR EMBL; BX842579; CAB00972.1; -; Genomic_DNA.
DR EMBL; AE000516; AAK46641.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45081.1; -; Genomic_DNA.
DR PIR; G70733; G70733.
DR RefSeq; NP_216815.1; NC_000962.3.
DR RefSeq; NP_336827.1; NC_002755.2.
DR RefSeq; YP_006515724.1; NC_018143.1.
DR ProteinModelPortal; P64411; -.
DR SMR; P64411; 6-643.
DR STRING; 83332.Rv2299c; -.
DR PaxDb; P64411; -.
DR PRIDE; P64411; -.
DR EnsemblBacteria; AAK46641; AAK46641; MT2356.
DR GeneID; 13318994; -.
DR GeneID; 887501; -.
DR GeneID; 924065; -.
DR KEGG; mtc:MT2356; -.
DR KEGG; mtu:Rv2299c; -.
DR KEGG; mtv:RVBD_2299c; -.
DR PATRIC; 18126928; VBIMycTub22151_2574.
DR TubercuList; Rv2299c; -.
DR eggNOG; COG0326; -.
DR HOGENOM; HOG000031989; -.
DR KO; K04079; -.
DR OMA; LTDSPAC; -.
DR ProtClustDB; PRK05218; -.
DR GO; GO:0005618; C:cell wall; IDA:MTBBASE.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0071451; P:cellular response to superoxide; IEP:MTBBASE.
DR GO; GO:0006457; P:protein folding; IEA:HAMAP.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1; -.
DR InterPro; IPR003594; HATPase_ATP-bd.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR001404; Hsp90.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATP_bd_ATPase; 1.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW Nucleotide-binding; Reference proteome; Stress response.
FT CHAIN 1 647 Chaperone protein HtpG.
FT /FTId=PRO_0000062996.
FT REGION 1 353 A; substrate-binding (By similarity).
FT REGION 354 567 B (By similarity).
FT REGION 568 647 C (By similarity).
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
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