ID   HTPG_CAMJD              Reviewed;         608 AA.
AC   A7H4M0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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};
GN   OrderedLocusNames=JJD26997_1413;
OS   Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS   269.97).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1458 / RM4099 / 269.97;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT   isolated from human blood.";
RL   Submitted (JUL-2007) 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; CP000768; ABS43789.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7H4M0; -.
DR   SMR; A7H4M0; -.
DR   EnsemblBacteria; ABS43789; ABS43789; JJD26997_1413.
DR   KEGG; cjd:JJD26997_1413; -.
DR   HOGENOM; CLU_006684_3_0_7; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000002302; 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..608
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014907"
FT   REGION          1..332
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          333..536
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          537..608
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   608 AA;  69676 MW;  C98CC0F5B43B2D6D CRC64;
     MQFQTEVNQL LQLMIHSLYS NKEIFLRELI SNASDALDKL NFLSVSDDKY KSLKFEPKIE
     IKIDKDKKTL SISDNGIGMD KNDLINNLGT IAKSGTKSFL ENLSGDAKKD SQLIGQFGVG
     FYSAFMVASK IEVLSKKALD DKAYLWSSDA NGYEINDASK EEQGTSITLY LKDDEFAHAY
     KIENIIEKYS NHIQFPIFME KEEFTPAKEG EEEGKTELKI SQINKANALW RMQKSSLKAE
     DYERFYEQNF HDSNKPLLYL HTKSEGKLEY NSLFFIPQNA PFDLFRVDYQ SGLKLYVKRV
     FISDDDKELL PTYLRFVRGI IDVEDLPLNV SREILQENQI LKGVKEASVK KILGELEKLK
     NNDKEKYLSF FKTFGKVLKE GLYGFGGEKD SLLKLMLYKS TKGENLRSLE EYKNDLQGEQ
     KEIFYIAGNN ESLLRTSPLL EEYKQKNIEV LLMDDEIDSL VTPMLEFEGL KFVAINQVED
     KNELSDEEKN TFAPLVAKFK ELLKDQVEDV RLTSRLKDSP SCIVYDKNKL DFAMQQLLKQ
     MGQEQNFKPI LEINPKHAIF TGLKNNETFS ADIATLVLNM AKLSEGMGVD NPAEFNASLT
     KIINKAFS