HTPG_ENT38
ID HTPG_ENT38 Reviewed; 624 AA.
AC A4W7F7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=Ent638_0953;
OS Enterobacter sp. (strain 638).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA Vangronsveld J., Newman L., Monchy S.;
RT "Genome sequence of the plant growth promoting endophytic bacterium
RT Enterobacter sp. 638.";
RL PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP59637.1; -; Genomic_DNA.
DR RefSeq; WP_012016357.1; NC_009436.1.
DR AlphaFoldDB; A4W7F7; -.
DR SMR; A4W7F7; -.
DR STRING; 399742.Ent638_0953; -.
DR EnsemblBacteria; ABP59637; ABP59637; Ent638_0953.
DR KEGG; ent:Ent638_0953; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR Proteomes; UP000000230; 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; PF02518; HATPase_c; 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; Stress response.
FT CHAIN 1..624
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000060527"
FT REGION 1..336
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 337..552
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 553..624
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 624 AA; 71255 MW; 68C215B73FB29033 CRC64;
MKGQETRGFQ SEVKQLLHLM IHSLYSNKEI FLRELISNAS DAADKLRFRA LSNPDLYEGD
GELRVRVSFD KDNRTLTIAD NGIGMNRDEV IDHLGTIAKS GTKSFLESMG SDQAKDSQLI
GQFGVGFYSA FIVADKVTVR TRAAGDSAEN GVFWESHGEG EYTVDDITKA DRGTEITLHL
REGEDDFLND WRVRSIISKY SDHIALPVEI EKREEQDGET VVSWEKINKA QALWTRNKSE
IKDDEYNEFY KHIAHDFTDP LTWSHNRVEG KQEYTSLLYI PAQAPWDMWN RDHKHGLKLY
VQRVFIMDDA EQFMPNYLRF TRGLIDSNDL PLNVSREILQ DSTVTRNLRN ALTKRTLQML
EKLAKDDAEK YQTFWKQFGL VLKEGPAEDS GNVESIAKLL RFASTHTDSS EQTVSLEDYV
SRMKEGQEKI YYITADSYAA AKSSPHLELL RKKGIEVLLL SDRIDEWMMN YLTEFDGKAF
QSVAKADESI DKLADEVDET AKEAEKALEP FVERVKTLLG DRVKEVRFTH RLTDTPAIVT
TDADEMGTQM AKLFAAAGQA MPEVKYIFEL NPDHPLVKRA ADTQDEARFS EWVELLLDQS
LLAERGTLED PNQFIKRVNA LLLG