ID   HTPG_MAGMM              Reviewed;         642 AA.
AC   A0L8B0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Mmc1_1694;
OS   Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetococcus.
OX   NCBI_TaxID=156889;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX   PubMed=19465526; DOI=10.1128/aem.02874-08;
RA   Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA   Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT   "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT   coccus strain MC-1.";
RL   Appl. Environ. Microbiol. 75:4835-4852(2009).
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; CP000471; ABK44203.1; -; Genomic_DNA.
DR   RefSeq; WP_011713351.1; NC_008576.1.
DR   AlphaFoldDB; A0L8B0; -.
DR   SMR; A0L8B0; -.
DR   STRING; 156889.Mmc1_1694; -.
DR   PRIDE; A0L8B0; -.
DR   EnsemblBacteria; ABK44203; ABK44203; Mmc1_1694.
DR   KEGG; mgm:Mmc1_1694; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000002586; 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..642
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014927"
FT   REGION          1..349
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          216..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..570
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          571..642
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   COMPBIAS        221..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   642 AA;  72968 MW;  CF8F8202D009E315 CRC64;
     MSAATETEVR EFQTEVSQLL DLMIHALYSN KEIFLRELIS NASDANDKLR FAGLSDDSLF
     EGDSELTIKL EFDKEAGTFS IMDNGIGMSR DEVISNIGTI AKSGTKEFFK SLTGDQQRDA
     HLIGQFGVGF YSSFIVADKV TLETRKAGAG AEQGVRWISA GDGSYTLENM EKAERGTRIT
     LHMREDEKEF LDAWRLRSIV RKFSDHVTWP VKMLEELPPA PPAKEGEEPE PPKTPEWETV
     NKASALWTLS KNDITEDEYK EFYKHVGHDF EDPMEWVHAR MEGRMEYTLL LYIPGRAPFD
     LWDRDRRGGL KLFVRRVFIM DTSEELLPRY LRFVRGVIDS ADLPLNVSRE ILQQNRQVEA
     IKKGLVHKVL GMLEEMLKND PEKYATFWKE FGMVLKEGMI EDFANKERIA KLCRFSTTHD
     GERVPKIALA DYVERMKEGQ EAIYYVTGES FEACSSSPHL EIFRKKGIEV LLLSDRVDEW
     TVTHLTEFDG KPLQAITKGE LDLSKFAGGE EEAKDEEAEK AQEEALKPIT ERMAKVLEGQ
     VKEVRLSHRL TESPACLVGD AHDMSATLER LLKEAGQEVP TAKRILEINP SHALLKRLAD
     EADEEKFGEL THVLHDQALL AEGGQLKDPS QFVKRLNKLL MG