ID   HTPG_BUCBP              Reviewed;         626 AA.
AC   Q89A93;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=bbp_427;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27137.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q89A93; -.
DR   SMR; Q89A93; -.
DR   STRING; 224915.bbp_427; -.
DR   EnsemblBacteria; AAO27137; AAO27137; bbp_427.
DR   KEGG; bab:bbp_427; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000000601; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..626
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000062977"
FT   REGION          1..338
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          339..553
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          554..626
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   626 AA;  73225 MW;  B7997D66F5D30FBF CRC64;
     MTANKNQKKT YNFKSETKEL LHLMIHSLYS NREIFFRELI SNAADAIDKL KFNAISAPEL
     YENDTNLYIR IFSNKNNNSL TISDNGIGMK YEDIINNLGT IAKSGTKEFI KTLNKNNKIK
     NDLIGQFGVG FYSSFIVSEK VIVKTRFAGL KENQGVIWTS DGKGTYEVNE INKKERGTEV
     TLYLTKDHYE FLETWKIQNT VSKYSDHISI PIELNTYDEK EKTYFWKQIN QAEAIWTRPK
     SEITELQYKN FYKKIANDTN DPLTWTHNKV EGNQEYTILL FIPSKSAWDI WNRDNKHGLK
     LYVKRVYIMD DAEQFLPNYL RFVKGIIDSN DLPLNVSREI LQDHKLVYNL KKSLTKKVLQ
     VLHSLSQNVS KYEIFWKQFG LILKEGPAED SENRTSISNL IRFSSLLNNT QKPTMSLENY
     VKNMKQNQEK IYFITADNYA SAVSSPHLEF FKKKNIDVLI LSDKIDEWMM NYLIEYNEKK
     FQSVSKDDKS IEKLVHEQNS QNETYQENMN DFLNRAKKTL SDKIKDIRFT HKLTNTPAMV
     ITDSNEMSTQ MAKLFSAAGQ TVPTIKYILE INPNHLLIKK INNEKNEKKF KNWINFLFEQ
     CLLAEKNTLD NPNKFIARIN DLLINN