ID   HTPG_AERS4              Reviewed;         637 AA.
AC   A4SLY0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=ASA_1826;
OS   Aeromonas salmonicida (strain A449).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=382245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A449;
RX   PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA   Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA   Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA   Brown L.L.;
RT   "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT   the evolution of a fish pathogen.";
RL   BMC Genomics 9:427-427(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; CP000644; ABO89902.1; -; Genomic_DNA.
DR   RefSeq; WP_005315218.1; NC_009348.1.
DR   AlphaFoldDB; A4SLY0; -.
DR   SMR; A4SLY0; -.
DR   STRING; 382245.ASA_1826; -.
DR   EnsemblBacteria; ABO89902; ABO89902; ASA_1826.
DR   KEGG; asa:ASA_1826; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000225; 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; Stress response.
FT   CHAIN           1..637
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000060521"
FT   REGION          1..347
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          348..564
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          565..637
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   637 AA;  71729 MW;  E09A7C2157BA2A73 CRC64;
     MTQSVHAETH GFQTEVKQLL SLMAHSLYSN KEVFLRELIS NASDAADKLR FKALSDASLF
     ENDGQLRVRL VVDKENRTLT ISDNGIGMTR DQVIEHLGTI AKSGTAEFFK NLSGDQGRDS
     QLIGQFGVGF YSAFIVADKV TVVSRAAGTA PEQGVQWESE GEGSFTVADV TKEGRGTDVI
     LHLRAEEEEF LDDWRLRAVV AKYSDHISVP VEMFKEGTPD REEDGETVVG TPGEWEQVNR
     ATALWTRNPK EIKDEEYQEF YKHVAHDFED PLLWGHNRVE GAQEYTSLLY VPARAPFDLY
     NREQKHGLKL YVQRVFIMDD AEQFMPTYLR FVKGVLDSND LPLNVSREIL QDNKVTVSLR
     KACSKRVLTM LAKLAKDDAE KYAKFWSEFG NVLKEGPAED YANREEIAKL LRFASTAGEG
     EAQTVSLEDY VGRMKEGQQK IYYITADSFA AAKNSPHLEI FRKKGVEVLL MWERVDEWLM
     SHLTEFDGKQ LVSVTRGELD LGDLEDEASK QAQEEAEKAN AGLVERVKTS LGEAVKEVRV
     THRLTDSPSC IVTDNHGMST QMIKLMRAAG QPVPEQKYIL ELNPDHALVK KLDTIEDEAL
     FGEWVTLLHE QAQLAEQGGL NDPASFVSRI NRLLLQA