ID   HTPG_CAMHC              Reviewed;         612 AA.
AC   A7I226;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=CHAB381_1006;
OS   Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS   CH001A).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360107;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT   commensal isolated from the human gastrointestinal tract.";
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; CP000776; ABS51952.1; -; Genomic_DNA.
DR   RefSeq; WP_012108863.1; NC_009714.1.
DR   AlphaFoldDB; A7I226; -.
DR   SMR; A7I226; -.
DR   STRING; 360107.CHAB381_1006; -.
DR   EnsemblBacteria; ABS51952; ABS51952; CHAB381_1006.
DR   KEGG; cha:CHAB381_1006; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_7; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000002407; 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; 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..612
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014906"
FT   REGION          1..335
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          336..539
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          540..612
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   612 AA;  69884 MW;  8D7E456C837B9EE9 CRC64;
     MAKRKFKTEV NQLLNLMINS LYSNKEIFLR ELISNASDAL DKLNYLALTK DEYKKLTYTP
     KIEITLDKEA KTLTISDTGI GMDENELENN LGTIARSGTK GFIEQLSGDA KKDSNLIGQF
     GVGFYSAFMV ADKIEVLTKK PLSDEAFSWK SDANDYTIEK AEKADFGTQI TLYLKDDEFL
     DSYRLENIIK KYSNHIPYPI FLQKEKYVAS QKEGEEGHYE SEISQVNKAN ALWRLPKSNL
     KEQDYFDFYK QISHDSSDPL LYIHTKAEGV HEYTTLFFVP SVQPFDLFRV DYQSGVKLYV
     KRVFITDDAK ELLPPYLRFV RGIIDIEDLP LNVSREILQE NRIMQTVKAA SVKKILGELE
     KIKNSDKEKY AKFYKLFGKV LKEGLWGFST EKDEILKLCL FKSSKTGELI DLAEYKKSMA
     AEQKEIYYIS GGKAETLKNS PLLEEFNAKN IEVLICDDEI DTIIMPMIGE FDKTPIKSVM
     DADFSDDKGE ISAQDLEIAE KIKENLKDKV KDVKISKRLK NALGVLVFDK NDPNYAMQAI
     YKQMGQENLP EVLPILEINK DHEIIKKLIA NQSEIAKISN IIFDLAKLSE GQNIDDASEF
     AKNVSEIIAK AI