ID   HTPG_HAES1              Reviewed;         626 AA.
AC   Q0I2A3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-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=HS_0450;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129Pt;
RX   PubMed=17172329; DOI=10.1128/jb.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT   129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT   influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(2007).
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; CP000436; ABI24727.1; -; Genomic_DNA.
DR   RefSeq; WP_011608606.1; NC_008309.1.
DR   AlphaFoldDB; Q0I2A3; -.
DR   SMR; Q0I2A3; -.
DR   STRING; 205914.HS_0450; -.
DR   EnsemblBacteria; ABI24727; ABI24727; HS_0450.
DR   KEGG; hso:HS_0450; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
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..626
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014922"
FT   REGION          1..339
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          340..555
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          556..626
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   626 AA;  71553 MW;  B06664CDCA2368B6 CRC64;
     MSTNQETRGF QSEVKQLLQL MIHSLYSNKE IFLRELISNA SDAADKLRFK ALSAPELYEG
     DGDLKVRISF DAEKGTLTIS DNGIGMTREQ VIDHLGTIAK SGTKEFLAAL GQEQAKDSQL
     IGQFGVGFYS AFIVADKVTV KTRAAGEPID KAVLWESAGE GEYSVADIEK KERGTEITLH
     LREEEKEFAN EWRVREIIGK YSDHIGLPVE ILAKEYDEEG KETGIKWEKI NKAQALWTRS
     KGEISDEEYK EFYKHLSHDF ADPLLWTHNK VEGNQEYTSL LYVPSKAPWD LFNREHKHGL
     KLYVQRVFIM DDAEQFMPNY LRFMRGLIDS NDLPLNVSRE ILQDNKVTAA LRKALTKRSL
     QMLEKLAKDD EEKYLQFWKE FGLVLKEGPS EDFANKENIA KLLRFASSKN DSSEQTVSLE
     DYVARMKEGQ KAIYYITADS YIAAKNSPHL ELFNKKDIEV LLLSDRIDEW MLSYLTEFDG
     KQLQPITKAD LDLGDLADKE QEEQKEQDKT FSSFIERVKT LLGERVKDVR LTHRLTDTPA
     VVSTDNDQMT TQMAKLFAAA GQPVPEVKYT FELNPEHHLV KKVADLADED EFANWIELLL
     EQAMLAERGS LENPTAFIKR VNSLLS