HTPG_IDILO
ID HTPG_IDILO Reviewed; 637 AA.
AC Q5QWR2;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=IL1846;
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(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 -!- 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; AE017340; AAV82678.1; -; Genomic_DNA.
DR RefSeq; WP_011235078.1; NC_006512.1.
DR AlphaFoldDB; Q5QWR2; -.
DR SMR; Q5QWR2; -.
DR STRING; 283942.IL1846; -.
DR EnsemblBacteria; AAV82678; AAV82678; IL1846.
DR KEGG; ilo:IL1846; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR Proteomes; UP000001171; 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 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; Reference proteome;
KW Stress response.
FT CHAIN 1..637
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000224211"
FT REGION 1..348
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 349..565
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 566..637
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 637 AA; 72890 MW; 83F2AFDD374B7CEC CRC64;
MAEAGQMEKH GFQTEVKQLL HLMIHSLYSN KEIFLRELVS NASDAADKLR FKALSDNSLY
GDDSDLHVRV SVDKDSRTIT ISDNGVGMTR DDVMNNLGTI AKSGTAEFFG QLSGDEAKDS
KLIGQFGVGF YSAFIVADEV TVRTRSALDK DARGVEWRSQ GEGDFEIADI DKARRGTDII
LHLKDDADEF LDENRLRGII NKYSEHLSIP VQMWKEPVPE SEDDEGNKVE GQPGEWETVN
SGQALWTREK SDITDEEYKE FYKTVAHDFD EPLLWSHNKV EGTTEYTNLL YIPKRAPWDL
WNREQQHGVK LYVKRVFIMD DAEQLMPTYL RFVRGLVDSN DLPLNVSREI LQDNKITRAM
RNGSTKKVLQ MLKKLAKDDK EQYQQFWDTF GNVLKEGPAE DHTNRERIAE LLRFASTHND
GAVQSVSLDD YIERMKEGQD KIFYIVADSY EAARNNPALE IFNKKGIEVL LLSERIDEWL
MSHLTEFKEK QLQSVTRGDL DLGELDDEED KAEQEKAEEA FKENLERFEK ALGDKVKKVR
VTNRLTNSPA CIITDDNDMS TQMAKLMEAA GQAVPETKYI FEVNPEHPLV QRMLTKEDDT
FKEWAEVLLD QATLAERGNL KDPASFVTRL NKLMLNA