HTPG_DESHY
ID HTPG_DESHY Reviewed; 614 AA.
AC Q24VT7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=DSY2066;
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51;
RX PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE83855.1; -; Genomic_DNA.
DR RefSeq; WP_011460040.1; NC_007907.1.
DR AlphaFoldDB; Q24VT7; -.
DR SMR; Q24VT7; -.
DR STRING; 138119.DSY2066; -.
DR EnsemblBacteria; BAE83855; BAE83855; DSY2066.
DR KEGG; dsy:DSY2066; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_1_9; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR Proteomes; UP000001946; 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; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
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..614
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000258509"
FT REGION 1..324
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 325..537
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 538..614
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 614 AA; 70141 MW; 5F82BA3FFDB14882 CRC64;
MSQIETKEFQ TEIRQLLDIV INSLYTDREI FLRELISNAA DASEKVRYMQ LSGQNVKDQE
LPLEIRITPD ENAKTLTIAD AGIGMTKEDL IENIGTIAHS GSKAFVQRLA EAGDKKDVNL
IGQFGVGFYS AFMVADKVSL TSRSYEPDAQ GYRWESDGRG SYSISEEMDL PRGTSITLHL
KEDAHSFAQA DTVKRIIKQY SSFVPYPVYV GEEKINTVQA LWTKNKNEIS EEEYKEFYKY
IANAYDEPLM RMHFSSDAPI NLNALLFVPK SNMEKFGFGR MEAGVNLYCK KVLIQEKAKD
IVPEWLRFAR GVVDSEELPL NISRETMQDS ALIAKLNKVV TSRFLKFLDD QAKNEPEIFK
EFWNEFSIFL KEGAANDFTH RQEILKLLRF ESSKTGEGEL ISLGDYVGRM KEGQEAIYFI
NGPTRQIIEE GPYLEVFKNK DYEVIYTYDG IDDYVFDMIR EYDGKRLLSA DHGDLNLADE
DGASAEEKLL SEEELKEFND WLKEVLGEKV TEVRESKRLV DSPAIILSHY GTHSMQRMMQ
LMNRDLQDVP AGILEINPKH VLIQRLNDLR KQEDSFAPLA AEQLFANAQI AAGIIVDPRS
MVSRLNEILE KALR