ID   HTPG_AERHH              Reviewed;         641 AA.
AC   A0KL53;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=AHA_2490;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC   2358 / NCIMB 9240 / NCTC 8049;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(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; CP000462; ABK38983.1; -; Genomic_DNA.
DR   RefSeq; WP_011706320.1; NC_008570.1.
DR   RefSeq; YP_857004.1; NC_008570.1.
DR   AlphaFoldDB; A0KL53; -.
DR   SMR; A0KL53; -.
DR   STRING; 380703.AHA_2490; -.
DR   EnsemblBacteria; ABK38983; ABK38983; AHA_2490.
DR   KEGG; aha:AHA_2490; -.
DR   PATRIC; fig|380703.7.peg.2489; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000000756; 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..641
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000060520"
FT   REGION          1..351
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          352..568
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          569..641
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   641 AA;  71860 MW;  84F69D0BCEF8BDB7 CRC64;
     MTQSVHAETH GFQTEVKQLL SLMAHSLYSN KEVFLRELIS NASDAADKLR FKALSDASLF
     ENDGQLRVRL VVDKENRTLT ISDNGIGMTR DQVIEHLGTI AKSGTAEFFK NLSGDQGRDS
     QLIGQFGVGF YSAFIVADKV TVVSRAAGTA PEQGVQWESE GEGSFTVADV TKAGRGTDVI
     LHLRAEEDEF LDDWRLRSVV SKYSDHISVP VEMYKEGTPD SVGEGEEDGE TIVGTPGEWE
     QVNRATALWT RNPKEIKDEE YQEFYKHVAH DFEDPLLWGH NRVEGAQEYT SLLYVPARAP
     FDLYNRDQKH GLKLYVQRVF IMDDAEQFMP AYLRFVKGVL DSNDLPLNVS REILQDNKVT
     VSLRKACSKR VLTMLAKLAK DDAEKYAKFW SEFGNVLKEG PAEDYANREE IAKLLRFAST
     AGEGEAQTVS LEDYVGRMKE GQQKIYYITA DSYAAAKNSP HLEIFRKKGV EVLLMWERVD
     EWLMSHLTEF DGKQLVSVTR GELDLGDLED EASKQAQEEA EKANAGLVER VKQSLGEAVK
     EVRVTHRLTD SPSCIVTDAH GMSTQMIKLM RAAGQPVPEQ KYILELNPDH ALVKKLGAIE
     DEALFGEWVT LLHEQAQLAE QGGLNDPASF VSRINRLLLQ A