ID   HTPG_CAMJE              Reviewed;         608 AA.
AC   Q9PHZ3; Q0PAZ7;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=Cj0518;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; AL111168; CAL34665.1; -; Genomic_DNA.
DR   PIR; G81397; G81397.
DR   RefSeq; WP_002858566.1; NC_002163.1.
DR   RefSeq; YP_002343950.1; NC_002163.1.
DR   AlphaFoldDB; Q9PHZ3; -.
DR   SMR; Q9PHZ3; -.
DR   IntAct; Q9PHZ3; 6.
DR   STRING; 192222.Cj0518; -.
DR   PaxDb; Q9PHZ3; -.
DR   PRIDE; Q9PHZ3; -.
DR   EnsemblBacteria; CAL34665; CAL34665; Cj0518.
DR   GeneID; 904847; -.
DR   KEGG; cje:Cj0518; -.
DR   PATRIC; fig|192222.6.peg.511; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_7; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000000799; 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..608
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000062978"
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;  69654 MW;  7FE40F4B365DF6B5 CRC64;
     MQFQTEVNQL LQLMIHSLYS NKEIFLRELI SNASDALDKL NFLSVSDDKY KSLKFEPKIE
     IKIDKDKKTL SISDNGIGMD KDDLINNLGT IAKSGTKSFL ENLSGDAKKD SQLIGQFGVG
     FYSAFMVASK IEVLSKKALD DKAYLWSSDA NGYEIDDANK EEQGTSITLY LKDDEFANAY
     KIESIIEKYS NHIQFPIFME KEEFTPAKEG EEEGKTELKI SQINKANALW RMQKSSLKAE
     DYERFYEQNF HDSNKPLLYL HTKSEGKLEY NSLFFIPQNA PFDLFRVDYQ SGLKLYVKRV
     FISDDDKELL PTYLRFVRGI IDVEDLPLNV SREILQENQI LKGIKEASVK KILGELEKLK
     NNDKEKYLSF FKTFGKVLKE GLYGFGGEKD SLLKLMLYKS TKGENLRSLE EYKNDLQGEQ
     KEIFYIAGNN ESLLRTSPLL EEYKQKNIEV LLMDDEIDSL VTPMLEFEGL KFVSINQVED
     KNELSDEEKN TFAPLVAKFK ELLKDQVEDV RLTSRLKDSP SCIVYDKNKP DFAMQQLLKQ
     MGQEQNFKPI LEINPKHAIF TGLKNNESFS ADIATLVLNM AKLSEGMGVD NPAEFNASLT
     KIINKAFS