ID   HTPG_MAGSA              Reviewed;         623 AA.
AC   Q2VZ28;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   25-MAY-2022, entry version 92.
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=amb4343;
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=342108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE53147.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AP007255; BAE53147.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_043745639.1; NC_007626.1.
DR   AlphaFoldDB; Q2VZ28; -.
DR   SMR; Q2VZ28; -.
DR   STRING; 342108.amb4343; -.
DR   PRIDE; Q2VZ28; -.
DR   EnsemblBacteria; BAE53147; BAE53147; amb4343.
DR   KEGG; mag:amb4343; -.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000007058; 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..623
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000236997"
FT   REGION          1..326
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          327..543
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          544..623
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   623 AA;  69044 MW;  CAB9EF85CE5E8927 CRC64;
     MAEEKRQFQA EVGKLLDIVV HSLYSNKEIF LRELISNASD SCDRLRYGAI TEPDLLDGDS
     EFRIRLVPDK DAGTLTIIDN GQGMSHDELI ANLGTIAKSG TSEFLARLTG DAKKDVSLIG
     QFGVGFYSAF MVAEEVTVTS RKAGEAKGWK WVSDGKGEFT VSPAEDAARG AAITLKLREG
     ETEFLDAFRL KSIVKRYSDH IAIPVTLKDA DKDEETINSA SALWTRSKSE ITPEQYKEFY
     HHVAHAFDEP WSTLHYKAEG AIEYTGLLFI PSSKPLDIFH PDRKQHVKLY VRRVFITDDC
     EELLPPYLRF VRGVVDSQDL PLNVSREMLQ HNPVLSKIRT GLVKRILGEL KKKSEDAEGK
     YDEFWAAFGP VLKEGIYEDF ERKTDILELC RFRSTHGDGL TTLADYVARM KDGQDAIYTI
     TGDDLDQLKK SPQLEGFAAK GVEVLLLTDP IDEFWVSAVR SYAEKDFRSV AAAGADLSKV
     KAPEGAEDKK ADEAPADELT TLIEAVKLAL GERVKDVRPS ERLTESAVCL VAAEGEMSMH
     LEKMLRAHNQ APGERARILE INPRHALIKG LAARVKAGGT DAGLEDAAFL LLDQARIIEG
     EPPADPAAFA RRMVSVMEKG LLG