ID   HTPG_HAHCH              Reviewed;         641 AA.
AC   Q2SKD0;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=HCH_02063;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(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; CP000155; ABC28894.1; -; Genomic_DNA.
DR   RefSeq; WP_011395965.1; NC_007645.1.
DR   AlphaFoldDB; Q2SKD0; -.
DR   SMR; Q2SKD0; -.
DR   STRING; 349521.HCH_02063; -.
DR   PRIDE; Q2SKD0; -.
DR   EnsemblBacteria; ABC28894; ABC28894; HCH_02063.
DR   KEGG; hch:HCH_02063; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000238; 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..641
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000236996"
FT   REGION          1..348
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          349..565
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          566..641
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   641 AA;  73296 MW;  0929D3F850E2C67E CRC64;
     MTTATEKQTL GFQAEVKQLL HLMIHSLYSN KEIFLRELVS NASDALDKLR FQALSKEDLY
     EGDNDLKVRL EFDDKAQTIT LSDNGIGMSR DEVVTNLGTI AKSGTAEFLS TLTGDQKQDS
     RLIGQFGVGF YSAFIVADKV EVYTRRAGLK PDEAVHWESS GEGDFSIETV TKEERGTRIV
     LHLKDEEKEF ANGWRLRSLV KKYSDHISFP VEMIKENMDV GEEEEGKEKA EPAPEFESVN
     EATALWTLPR NEIKDEDYKE FYKHIAHDFS DPLLWAHNRV EGKLDYTSLL YVPAKAPYDL
     WNREAPRGLK LYIQRVFIMD DAEQFLPLYL RFVKGVVDSN DLSLNVSREI LQNDKAVESM
     RSALTKRVLD MLSKLAADDA EKYQSFWDEF GRVLKEGPAE DFINREKIAK LMRFSSTHQD
     DDKQTQSLED YVSRMKQGQD KIYYITAESY SAGVKSPHLE IFRKKGIEVL VMHDRIDEWL
     MSHLNEFDGK HFQDIAKGEL DLGEVEDKEE KEKQEEVSKE AEPLLNRLKE VLKDHVEEVR
     VTHRLTDSPA CLVVGAYDMG VQMRRIMEAA GQALPESKPT FEINPDHPLV KKLGEEQGAR
     FEDLTWVLFD QARLAGGENL KDPAGYVSRL NKLLLELSNA G