(data stored in SCRATCH zone)

SWISSPROT: C8U2F9_ECO10

ID   C8U2F9_ECO10            Unreviewed;       624 AA.
AC   C8U2F9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Chaperone protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505, ECO:0000256|SAAS:SAAS00869959};
DE   AltName: Full=Heat shock protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE   AltName: Full=High temperature protein G {ECO:0000256|HAMAP-Rule:MF_00505};
GN   Name=htpG {ECO:0000256|HAMAP-Rule:MF_00505,
GN   ECO:0000313|EMBL:BAI29317.1};
GN   OrderedLocusNames=ECO103_0449 {ECO:0000313|EMBL:BAI29317.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29317.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29317.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Molecular chaperone. Has ATPase activity.
CC       {ECO:0000256|HAMAP-Rule:MF_00505, ECO:0000256|SAAS:SAAS00870027}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00505}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00505}.
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DR   EMBL; AP010958; BAI29317.1; -; Genomic_DNA.
DR   RefSeq; WP_000678194.1; NC_013353.1.
DR   EnsemblBacteria; BAI29317; BAI29317; ECO103_0449.
DR   KEGG; eoh:ECO103_0449; -.
DR   HOGENOM; HOG000031989; -.
DR   KO; K04079; -.
DR   OMA; MRRMKEM; -.
DR   BioCyc; ECOL585395:ECO103_RS02350-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   CDD; cd00075; HATPase_c; 1.
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;
DR   PRODOM; C8U2F9.
DR   SWISS-2DPAGE; C8U2F9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00505};
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_00505};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00505};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT   DOMAIN       27    184       HATPase_c. {ECO:0000259|SMART:SM00387}.
FT   REGION        1    336       A; substrate-binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00505}.
FT   REGION      337    552       B. {ECO:0000256|HAMAP-Rule:MF_00505}.
FT   REGION      553    624       C. {ECO:0000256|HAMAP-Rule:MF_00505}.
FT   COILED      483    507       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   624 AA;  71435 MW;  653FF6D1B73B7AB7 CRC64;
     MKGQETRGFQ SEVKQLLHLM IHSLYSNKEI FLRELISNAS DAADKLRFRA LSNPDLYEGD
     GELRVRVSFD KDKRTLTISD NGVGMTRDEV IDHLGTIAKS GTKSFLESLG SDQAKDSQLI
     GQFGVGFYSA FIVADKVTVR TRAAGEKPEN GVFWESAGEG EYTVADITKE DRGTEITLHL
     REGEDEFLDD WRVRSIISKY SDHIALPVEI EKREEKDGET VISWEKINKA QALWTRNKSE
     ITDEEYKEFY KHIAHDFNDP LTWSHNRVEG KQEYTSLLYI PSQAPWDMWN RDHKHGLKLY
     VQRVFIMDDA EQFMPNYLRF VRGLIDSSDL PLNVSREILQ DSTVTRNLRN ALTKRVLQML
     EKLAKDDADK YQTFWQQFGL VLKEGPAEDF ANQEAIAKLL RFASTYTDSS AQTVSLEDYV
     SRMKEGQEKI YYITADSYAA AKSSPHLELL RKKGIEVLLL SDRIDEWMMN YLTEFDGKPF
     QSVSKVDESL EKLADEVDES AKEAEKALTP FIDRVKALLG ERVKDVRLTH RLTDTPAIVS
     TDADEMSTQM AKLFAAAGQK VPEVKYIFEL NPDHVLVKRA ADTEDEAKFS EWVELLLDQA
     LLAERGTLED PNLFIRRMNQ LLVS
//

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