(data stored in ACNUC10821 zone)

SWISSPROT: C8U1D5_ECO10

ID   C8U1D5_ECO10            Unreviewed;       292 AA.
AC   C8U1D5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   SubName: Full=DNA-binding transcriptional dual regulator AraC {ECO:0000313|EMBL:BAI28943.1};
GN   Name=araC {ECO:0000313|EMBL:BAI28943.1};
GN   OrderedLocusNames=ECO103_0065 {ECO:0000313|EMBL:BAI28943.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28943.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28943.1, 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS01083045}.
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DR   EMBL; AP010958; BAI28943.1; -; Genomic_DNA.
DR   RefSeq; WP_001300811.1; NC_013353.1.
DR   SMR; C8U1D5; -.
DR   EnsemblBacteria; BAI28943; BAI28943; ECO103_0065.
DR   KEGG; eoh:ECO103_0065; -.
DR   HOGENOM; HOG000276603; -.
DR   KO; K02099; -.
DR   OMA; GFEDQLY; -.
DR   BioCyc; ECOL585395:ECO103_RS00330-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   InterPro; IPR003313; AraC-bd.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR037923; HTH-like.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR018062; HTH_AraC-typ_CS.
DR   InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR   Pfam; PF02311; AraC_binding; 1.
DR   Pfam; PF12833; HTH_18; 1.
DR   PRINTS; PR00032; HTHARAC.
DR   SMART; SM00342; HTH_ARAC; 1.
DR   SUPFAM; SSF46689; SSF46689; 2.
DR   SUPFAM; SSF51215; SSF51215; 1.
DR   PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE   4: Predicted;
DR   PRODOM; C8U1D5.
DR   SWISS-2DPAGE; C8U1D5.
KW   Activator {ECO:0000256|SAAS:SAAS00976682};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS01082989};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00048696,
KW   ECO:0000313|EMBL:BAI28943.1};
KW   Transcription {ECO:0000256|SAAS:SAAS00048810};
KW   Transcription regulation {ECO:0000256|SAAS:SAAS00048643}.
FT   DOMAIN      180    279       HTH araC/xylS-type. {ECO:0000259|PROSITE:
FT                                PS01124}.
SQ   SEQUENCE   292 AA;  33384 MW;  C5A737E285A4ECC6 CRC64;
     MAEAQNDPLL PGYSFNAHLV AGLTPIEANG YLDFFIDRPL GMKGYILNLT IRGQGVVKNQ
     GREFVCRPGD ILLFPPGEIH HYGRHPEARE WYHQWVYFRP RAYWHEWLNW PSIFANTGFF
     RPDEAHQPHF SDLFGQIINA GQGEGRYSEL LAINLLEQLL LRRMEAINES LHPPMDNRVR
     EACQYISDHL ADSNFDIASV AQHVCLSPSR LSHLFRQQLG ISVLSWREDQ RISQAKLLLS
     TTRMPIATVG RNVGFDDQLY FSRVFKKCTG ASPSEFRAGC EEKVNDVAVK LS
//

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