ID   HTPG_HAEI8              Reviewed;         626 AA.
AC   Q4QP81;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 94.
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=NTHI0185;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=86-028NP;
RX   PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT   influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAX87166.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000057; AAX87166.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_005687637.1; NC_007146.2.
DR   AlphaFoldDB; Q4QP81; -.
DR   SMR; Q4QP81; -.
DR   EnsemblBacteria; AAX87166; AAX87166; NTHI0185.
DR   KEGG; hit:NTHI0185; -.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   Proteomes; UP000002525; 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..626
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224210"
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;  71193 MW;  82F1366C4852CE24 CRC64;
     MSQNQETRGF QSEVKQLLQL MIHSLYSNKE IFLRELISNA SDAADKLRFK ALSNPALYEG
     DGDLRVRVSF DADKGTITIS DNGIGMTREQ VIDHLGTIAK SGTKEFLTAL GQDQAKNSQL
     IGQFGVGFYS AFIVADKVTV KTRAAGEEAD KAVLWESAGE GEYSVADIEK KSRGTDVILH
     LREDEKEFLN EWRLREIIGK YSDHIGLPVE MLTKEYDDEG KECGEKWEKI NKSDALWTRS
     KNDVSDEEYK AFYKHLSHDF VDPVTWAHNK VEGNQAYTSL LYVPAKAPWD LFNREHKHGL
     KLYVQRVFIM DDAEQFMPNY LRFMRGLIDS NDLPLNVSRE ILQDNKITAA LRKALTKRSL
     QMLEKLAKDD AEKYLKFWKE FGLVLKEGPA EDFANKETIA KLLRFASTHN DGSEQTVSLE
     DYILRMKEGQ KAIYYITADS YVAAKNSPHL ELFNKKGIEV LLLSDRIDEW MLSYLTEFDG
     KQLQSITKAD LDLGDLADKE SETQKQQDKA FGSFIERVKN LLGERVKTVR LTHNLTDTPA
     VVSTDNDQMT TQMAKLFAAA GQPVPEVKYT FELNPEHYLV KKVADIADET EFADWVELLL
     EQAMLAERGS LENPAAFIKR INKLLG