ARAC_ECO57
ID ARAC_ECO57 Reviewed; 292 AA.
AC P0A9E1; P03021; Q47056;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Arabinose operon regulatory protein;
GN Name=araC; OrderedLocusNames=Z0073, ECs0068;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Transcription factor that regulates the expression of several
CC genes involved in the transport and metabolism of L-arabinose.
CC {ECO:0000250|UniProtKB:P0A9E0}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A9E0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9E0}.
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DR EMBL; AE005174; AAG54368.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33491.1; -; Genomic_DNA.
DR PIR; D85488; D85488.
DR PIR; D90637; D90637.
DR RefSeq; NP_308095.1; NC_002695.1.
DR RefSeq; WP_001300811.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A9E1; -.
DR BMRB; P0A9E1; -.
DR SMR; P0A9E1; -.
DR STRING; 155864.EDL933_0066; -.
DR PRIDE; P0A9E1; -.
DR EnsemblBacteria; AAG54368; AAG54368; Z0073.
DR EnsemblBacteria; BAB33491; BAB33491; ECs_0068.
DR GeneID; 66671647; -.
DR GeneID; 913473; -.
DR KEGG; ece:Z0073; -.
DR KEGG; ecs:ECs_0068; -.
DR PATRIC; fig|386585.9.peg.168; -.
DR eggNOG; COG4977; Bacteria.
DR HOGENOM; CLU_000445_88_6_6; -.
DR OMA; GFEDQLY; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 GO; GO:0019568; P:arabinose catabolic process; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Activator; Arabinose catabolism; Carbohydrate metabolism; Cytoplasm;
KW DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..292
FT /note="Arabinose operon regulatory protein"
FT /id="PRO_0000194500"
FT DOMAIN 180..279
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 198..219
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 246..269
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT BINDING 8
FT /ligand="alpha-L-arabinopyanose"
FT /ligand_id="ChEBI:CHEBI:46987"
FT /evidence="ECO:0000250|UniProtKB:P0A9E0"
FT BINDING 24
FT /ligand="alpha-L-arabinopyanose"
FT /ligand_id="ChEBI:CHEBI:46987"
FT /evidence="ECO:0000250|UniProtKB:P0A9E0"
FT BINDING 38
FT /ligand="alpha-L-arabinopyanose"
FT /ligand_id="ChEBI:CHEBI:46987"
FT /evidence="ECO:0000250|UniProtKB:P0A9E0"
FT BINDING 82
FT /ligand="alpha-L-arabinopyanose"
FT /ligand_id="ChEBI:CHEBI:46987"
FT /evidence="ECO:0000250|UniProtKB:P0A9E0"
FT BINDING 93
FT /ligand="alpha-L-arabinopyanose"
FT /ligand_id="ChEBI:CHEBI:46987"
FT /evidence="ECO:0000250|UniProtKB:P0A9E0"
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
