ID   HTPG_CAMJR              Reviewed;         608 AA.
AC   Q5HVP5;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=CJE0625;
OS   Campylobacter jejuni (strain RM1221).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM1221;
RX   PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA   Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA   Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA   Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA   Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA   Nelson K.E.;
RT   "Major structural differences and novel potential virulence mechanisms from
RT   the genomes of multiple Campylobacter species.";
RL   PLoS Biol. 3:72-85(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}.
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DR   EMBL; CP000025; AAW35862.1; -; Genomic_DNA.
DR   RefSeq; WP_011049730.1; NC_003912.7.
DR   AlphaFoldDB; Q5HVP5; -.
DR   SMR; Q5HVP5; -.
DR   KEGG; cjr:CJE0625; -.
DR   HOGENOM; CLU_006684_3_0_7; -.
DR   OMA; MRRMKEM; -.
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_0000224201"
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;  69640 MW;  EA8E5F51ECE512B5 CRC64;
     MQFQTEVNQL LQLMIHSLYS NKEIFLRELI SNASDALDKL NFLSVSDDKY KSLKFEPKIE
     IKIDKDKKTL SISDNGIGMD KDDLINNLGT IAKSGTKSFL ENLSGDAKKD SQLIGQFGVG
     FYSAFMVASK IEVLSKKALD DKAYLWSSDA NGYEINDASK EEQGTSITLY LKDDEFANTY
     KIESIIEKYS 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 KFIAINQVED
     KNELSDEEKN TFAPLVAKFK ELLKDQVEDV RLTSRLKDSP SCIVYDKNKP DFAMQQLLKQ
     MGQEQNFKPI LEINPKHAIF TGLKNNESFS ADIATLVLNM AKLSEGMGVD NPAEFNASLT
     KIINKAFS