HTPG_MAGMM
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