ID   HTPG_PASMU              Reviewed;         631 AA.
AC   Q9CM20;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 126.
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=PM1024;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03108.1; -; Genomic_DNA.
DR   RefSeq; WP_010906976.1; NC_002663.1.
DR   AlphaFoldDB; Q9CM20; -.
DR   SMR; Q9CM20; -.
DR   STRING; 747.DR93_945; -.
DR   EnsemblBacteria; AAK03108; AAK03108; PM1024.
DR   KEGG; pmu:PM1024; -.
DR   PATRIC; fig|272843.6.peg.1037; -.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000000809; 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..631
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000063000"
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..631
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   631 AA;  71852 MW;  74D08271651E7480 CRC64;
     MSTNQETRGF QSEVKQLLQL MIHSLYSNKE IFLRELISNA SDAADKLRFK ALSVPELYEG
     DGDLKVRIRF DEEKGTLTIS DNGIGMTRDE VIDHLGTIAK SGTKEFLSAL GQDQAKDSQL
     IGQFGVGFYS AFIVADKVTV KTRAAGVSAD KAVLWESAGE GEYSVADIDK KERGTEITLH
     LREDEKAFLN DWRLREIIGK YSDHIGLPVE ILAKEYDDEG KETGIKWEKI NKAQALWTRA
     KNEISEEEYQ EFYKHLSHDF TDPLLWAHNK VEGNQEYTSL LYVPAKAPWD LFNREHKHGL
     KLYVQRVFIM DDAQVFMPNY LRFMRGLLDS NDLPLNVSRE ILQDNKVTSA LRKALTKRAL
     QMLEKLAKDD AEKYQRFWQE FGLVLKEGPA EDFANKETIA KLLRFASTHN DSSQQSVSLE
     DYVARMKEGQ KAIYYITADT YVAAKNSPHL ELFNKKGIEV LLLSDRIDEW MLSYLTEFDG
     KPLQTISKAD LDLGDLADKE EDSQKAQDEQ YASFVERVKT LLGERVKEVR LTHRLTDTPA
     VVSTGDDQMT TQMAKLFAAA GQAMPEVKYT FELNPEHGLV QKVAEIADEQ QFADWIELLL
     EQAMLAERGS LENPVAFIKR MNTLLSKLTS H