HTPG_DESVH
ID HTPG_DESVH Reviewed; 637 AA.
AC Q728G0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=DVU_2643;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
CC -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-
CC Rule:MF_00505}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00505}.
CC -!- INTERACTION:
CC Q728G0; Q728L5: DVU_2588; NbExp=2; IntAct=EBI-10066697, EBI-10066767;
CC Q728G0; Q72BU5: glpX; NbExp=4; IntAct=EBI-10066697, EBI-10066693;
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; AE017285; AAS97115.1; -; Genomic_DNA.
DR RefSeq; WP_010939912.1; NC_002937.3.
DR RefSeq; YP_011855.1; NC_002937.3.
DR AlphaFoldDB; Q728G0; -.
DR SMR; Q728G0; -.
DR IntAct; Q728G0; 4.
DR STRING; 882.DVU_2643; -.
DR PaxDb; Q728G0; -.
DR PRIDE; Q728G0; -.
DR EnsemblBacteria; AAS97115; AAS97115; DVU_2643.
DR KEGG; dvu:DVU_2643; -.
DR PATRIC; fig|882.5.peg.2393; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_7; -.
DR OMA; MRRMKEM; -.
DR PhylomeDB; Q728G0; -.
DR Proteomes; UP000002194; 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; 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 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..637
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000236992"
FT REGION 1..330
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 331..551
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 552..637
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 637 AA; 71660 MW; 71DEA234138A36B8 CRC64;
MATAPASHAF RTEVRKMLHI ITHSLYTNRE IFLRELVSNA SDALDKLRFI RSRGDAVVAP
DLAPGIDISV DKEARILTIA DTGVGMTRQE LMDNLGTIAR SGSEQFVADL AAAENAKDAD
AASIIGRFGV GFYAVFMVAD RVEVTSRSYI EGEAAHTWTS DGLGEFTVEE ATGDIPQRGT
VIKAHLREDA AEFLEKYRIE GILRKHSQFI SFPIRVDGEQ VNTTPALWRE PKFSITDEQY
ADFYKHLTFD TEAPLRTLHV SVDAPVQFTG LVFVPPHGQE VFSMGRDRWG LDLYVRRVLI
QRENKDLLPE YLGFLKGIVD TEDLPLNISR ETLQENVVVR KIGQTLTKQV LADLARLAAD
DAEAYATFWR QHGKVFKLGY SDYANREKFA PLLRFNSSHH DDAQGLTSLD DYISRAREGQ
KEIWYIAAPG REAARLDPRV EVFRRKGLEV LYLLEPIDEF VLETLDSYSD FSFKAVEHAD
GEKLAQFEDT GPARDVTPLT EDEDAAFARL IERMKALLGD AVEDVRISHR LADSPACLVQ
PGGASTSSMD RLLRVLHKDE SVPRKVFEVN RDHPILRNLL KVFTSDASDP LVEDTTRQLF
ATSLMLDGYL KDPHELAAMM HRLMEKSGDW YKAVRGL