HTPG_METNO
ID HTPG_METNO Reviewed; 611 AA.
AC B8IU50;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=Mnod_0044;
OS Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=460265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060.";
RL Submitted (JAN-2009) 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; CP001349; ACL55095.1; -; Genomic_DNA.
DR RefSeq; WP_012634334.1; NC_011894.1.
DR AlphaFoldDB; B8IU50; -.
DR SMR; B8IU50; -.
DR STRING; 460265.Mnod_0044; -.
DR EnsemblBacteria; ACL55095; ACL55095; Mnod_0044.
DR KEGG; mno:Mnod_0044; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_5; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR Proteomes; UP000008207; 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; 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; Reference proteome;
KW Stress response.
FT CHAIN 1..611
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000146008"
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; 67373 MW; FA758649B6328124 CRC64;
MSETLERHAF GAEVGRLLDL VVHALYSERE IFLRELVANA ADAVDRRRFG ALTDPALALP
AEAKVRIRPD KAARTLTISD PGIGMGKEDL AQNLGTIARS GTRAFSQSLA EAKPDERPSL
IGQFGVGFYS AFMVADRVEV TSRRAGSDEA WTWASDGEGE YTLSPATREE PGTDVVLHMK
ADADEYLEPL RIETIVRKWA DHITVPITLL RDGEEVSGNE GTALWRKPKA EITEETYTAF
YRHLTHNFDT PWATLHWRAE GALDFSALLF IPSMKPFLAV EEERESKVRL HVRRMFITDE
AGLLPSWLRF VQGVVDTEDL PLNVSREMLQ ATPVLARIRR AVTAKVLSEL KSRAKDADGY
ASFWQAFGPV LKEGIWEDAE QRDDIAGLIR FRSSAVEGWT SFADYVSRMK PNQEAIYILV
GDDTKALASS AQIEGFRARG IEVLLLSDHV DAFWPERLDK FDGKPIRSIT QSADDLSAFA
PEGESEGEAA DLADLVPKLK EILKDDVTDV RASQRLVESA VLLSASSGGP DLQMQRLLRR
AGRGFGAGLP VLELNPRHAL VRRLAERAKT GEDIAEAAQT LLDLAHVQGG DAPRDPVAFA
RRVATALAAQ G