ID   HTPG_GLAP5              Reviewed;         628 AA.
AC   B8F5X3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=HAPS_1111;
OS   Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Glaesserella.
OX   NCBI_TaxID=557723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH0165;
RX   PubMed=19074396; DOI=10.1128/jb.01682-08;
RA   Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA   Jin M., Jin Q., Chen H.;
RT   "Complete genome sequence of Haemophilus parasuis SH0165.";
RL   J. Bacteriol. 191:1359-1360(2009).
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; CP001321; ACL32725.1; -; Genomic_DNA.
DR   RefSeq; WP_010786228.1; NC_011852.1.
DR   AlphaFoldDB; B8F5X3; -.
DR   SMR; B8F5X3; -.
DR   STRING; 557723.HAPS_1111; -.
DR   EnsemblBacteria; ACL32725; ACL32725; HAPS_1111.
DR   GeneID; 66618071; -.
DR   KEGG; hap:HAPS_1111; -.
DR   PATRIC; fig|557723.8.peg.1108; -.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000006743; 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..628
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000146006"
FT   REGION          1..339
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          340..556
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          557..628
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   628 AA;  71292 MW;  DDB98231A00DAC1A CRC64;
     MSTNQETRGF QSEVKQLLQL MIHSLYSNKE IFLRELISNA SDAADKLRFK ALSQPELYEG
     DGELRVRISI DEALGTITIS DNGIGMSREQ VIDHLGTIAK SGTKEFLNAL GSDQAKDSQL
     IGQFGVGFYS SFIVADKVTV RTRAAGSDAS QGVLWESAGE GDYTVADIEK AGRGTDVILH
     LRDDEKEFLS EWRLRDIIGK YSDHIGLAVE IQTKEYDDEG KETGTKWEKI NKAQALWTRS
     KNEISDEEYK EFYKHISHDF ADPLIWSHNK VEGKQEYTSL LYVPSKAPWD LFQREQKHGL
     KLYVQRVFIM DDVEVFMPNY LRFMRGLLDT NDLPLNVSRE ILQENKVTQS LRTALTKRSL
     QMLEKLAKDN IEQYQQFWNA FGLVLKEGVG EDFANKNQVA ALVRFASTHT DSSEQAVSLS
     DYIARMKEGQ KAIYFLTADS YQAAKNSPHL ELFNKKGIEV LLLSDRIDEW FISHLTEFDG
     KPLQSITKSD LDLGDLADKE EEETQKVQEA EFASFLERAK GYLGERVKKV VLTHRLTDTP
     AVVSTDSDEM TTQMAKLFAA MGQQAPEVKY TFELNPEHSM VKRIADIADE AEFNDWIELL
     FEQALLAERG TLENATAFIK RMNKLLGA