ID   HTPG_SACD2              Reviewed;         635 AA.
AC   Q21IX0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=Sde_2099;
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
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; CP000282; ABD81359.1; -; Genomic_DNA.
DR   RefSeq; WP_011468577.1; NC_007912.1.
DR   AlphaFoldDB; Q21IX0; -.
DR   SMR; Q21IX0; -.
DR   STRING; 203122.Sde_2099; -.
DR   PRIDE; Q21IX0; -.
DR   EnsemblBacteria; ABD81359; ABD81359; Sde_2099.
DR   KEGG; sde:Sde_2099; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001947; 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..635
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258527"
FT   REGION          1..343
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          344..560
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          561..635
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   635 AA;  72349 MW;  517B1A041F3EA59A CRC64;
     MTAEATVETR GFETEAKQLL HLMIHSLYSN KEIFLRELVS NASDAADKLR FEALKQPELL
     EQDSELKITI DFDKEAKTLS ITDNGIGMNR DEVIANLGTI ARSGTAQFMA NLSGDQKKDS
     QLIGQFGVGF YSAFIVADKV EVLTRRAGSE PSEGVRWVSE GEAEYSIENI EKAARGTTII
     LHLKKDQEEF ADGWRLRSII KKYSDHISLP VEMPKEAAPG EDKEEKAEVE YEVINTAKAL
     WARSRSDVTD EEYKEFYKHV SHDYTDPLSW SHNRVEGKLD YTSLIYIPSK APFDMYNREK
     PRGVKLYVQR TFIMDDAEQF LPLYLRFIKG VVDSNDLSLN VSREILQQDP NIDSMRSALT
     KRVLDMLEKM AKKEPEKYAT FWKEFGEVLK EGPAEDFANK EKIAKLLRFA TTHKNTNEQD
     QSLDAYIERM KEGQDKIYYV VAENFNTAKN SPHLEVFRKK GIEVLLLSNR IDDWLMGHLM
     EYDGKQFQDV GKGSLDLGKL DSEEDKKEQE KVEEAMAPFV ERMKAALAEQ VEEVRITHRL
     TESPACLVVG EHDMGAQMRR LLEAAGQAVP ESKPIIEINP THPLVQKLDQ EQDEDRFKDL
     SHILFDQASL AEGGSLKDPA AYVSRLNKLL LELSN