HTPG_METS4
ID HTPG_METS4 Reviewed; 611 AA.
AC B0UN89;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=M446_0044;
OS Methylobacterium sp. (strain 4-46).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4-46;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium sp. 4-46.";
RL Submitted (FEB-2008) 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; CP000943; ACA14632.1; -; Genomic_DNA.
DR RefSeq; WP_012330050.1; NC_010511.1.
DR AlphaFoldDB; B0UN89; -.
DR SMR; B0UN89; -.
DR STRING; 426117.M446_0044; -.
DR EnsemblBacteria; ACA14632; ACA14632; M446_0044.
DR KEGG; met:M446_0044; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_5; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
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; 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.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT CHAIN 1..611
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000127032"
FT REGION 1..326
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 327..536
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 537..611
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 611 AA; 67209 MW; 1D5B0B5A06155AFA CRC64;
MSETLERHAF GAEVGRLLDL VVHALYSERE IFLRELVANA ADAVDRRRFG ALTDPALSLP
ADAKVRIRPD KAARTLAISD PGIGMSKEDL AQNLGTIARS GTRAFSQSLA DAKPDERPSL
IGQFGVGFYS AFMVADRVEV TSRKAGSDEA WTWASEGQGE YTLSPATRAE PGTDVVLHIK
ADADEYLEPL RLETIVRKWA DHITVPITLL RDGEEVSGNE GTALWRKPKS EVSEEAYTAF
YRHVTHNFDA PWATLHWRAE GALDFTALLF IPGMKPFLAV EEERESRVRL HVRRMFITDE
AGLLPSWLRF VQGVVDTEDL PLNVSREMLQ ATPVLARIRR AVTGKVMAEL KSRAKDAESY
ATFWQAFGPV LKEGIWEDAE HRDDIAALLR FRSTAVEGWT SFADYVSRMK PNQEAIYILV
GDDAAALARS AQIEGFRARG IEVLLLSDHV DAFWPERLDK FDGKPIRSIT QSADDLSAFA
PEGEAAGEAA DLTELLPKLK EILKDDVAEV RASQRLVESA VLLSASSGGP DLQMQRLLRR
AGRGFGAGLP VLELNPRHAL VRRIAERARA GEDVGEAAQT LLDLAHVQGG DPPRDPVAFA
RRVAAALAAQ A