ID   HTPG_ACTP7              Reviewed;         625 AA.
AC   B3GXX7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=APP7_1040;
OS   Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=537457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP76;
RA   Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA   Tegetmeyer H., Singh M., Gerlach G.F.;
RT   "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001091; ACE61692.1; -; Genomic_DNA.
DR   RefSeq; WP_005617462.1; NC_010939.1.
DR   AlphaFoldDB; B3GXX7; -.
DR   SMR; B3GXX7; -.
DR   PRIDE; B3GXX7; -.
DR   EnsemblBacteria; ACE61692; ACE61692; APP7_1040.
DR   KEGG; apa:APP7_1040; -.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   BioCyc; APLE537457:APP7_RS05290-MON; -.
DR   Proteomes; UP000001226; 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..625
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000127023"
FT   REGION          1..337
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          338..554
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          555..625
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   625 AA;  71056 MW;  AF7189EB02B89ECD CRC64;
     MSTNQETRGF QSEVKQLLQL MIHSLYSNKE IFLRELISNA SDAADKLRFK ALSNPALYEG
     DGELRVRVSF DETLGTLTIS DNGIGMNREQ VIDHLGTIAK SGTKEFLNSL GTDQAKDSQL
     IGQFGVGFYS AFIVADKVTV KTRAAGETQA VLWESAGEGD YTVADIEKAT RGTDVILHLR
     EEEKEFLSEW RLREIIGKYS DHIGLPVEIQ TTEYDEEGKV SGQKWEKINK AQALWTRSKI
     EISDEEYQEF YKHLSHDYND SLIWAHNKVE GKQDYTSLLY VPAKAPWDLF NRDQKHGLKL
     YVQRVFIMDD AEVFMPNYLR FMRGLLDTND LPLNVSREIL QENKITASLR AALTKRALQL
     LEKLAKDDQA KYQTFWNEFG LVLKEGVGED FANKQQIASL FRFASTQTDS SEQTVSLADY
     VGRMKEGQKA IYFLTADSYV AAKNSPHLEL FNKKGIEVLL LSDRIDEWVV GHLTEFDGKP
     LQSITKSDLD LGDLADKEQE ESQKAQQAEF GSFLERAQSY FGERVKKVVL THRLTDTPAV
     VSTDNDEMTT QMAKLFAAMG QKAPEVKYTF ELNPDHRMVK KIADLTDETE FNDWIELLFE
     QALLAERGSL ENPAAFIKRM NKLLG