ID RPIR_ECOLI Reviewed; 296 AA. AC P0ACS7; P39266; P76791; Q2M6L4; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 124. DE RecName: Full=HTH-type transcriptional regulator RpiR; DE AltName: Full=Als operon repressor; GN Name=rpiR; Synonyms=alsR, yjcY; OrderedLocusNames=b4089, JW4050; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=8576032; DOI=10.1128/jb.178.4.1003-1011.1996; RA Soerensen K.I., Hove-Jensen B.; RT "Ribose catabolism of Escherichia coli: characterization of the rpiB gene RT encoding ribose phosphate isomerase B and of the rpiR gene, which is RT involved in regulation of rpiB expression."; RL J. Bacteriol. 178:1003-1011(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=7610040; DOI=10.1093/nar/23.12.2105; RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.; RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region RT from 92.8 through 100 minutes."; RL Nucleic Acids Res. 23:2105-2119(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP FUNCTION IN ALS REPRESSION. RX PubMed=9401019; DOI=10.1128/jb.179.24.7631-7637.1997; RA Kim C., Song S., Park C.; RT "The D-allose operon of Escherichia coli K-12."; RL J. Bacteriol. 179:7631-7637(1997). CC -!- FUNCTION: Regulatory protein involved in rpiB gene repression. Also CC involved in als operon repression. {ECO:0000269|PubMed:9401019}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA96988.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X82203; CAA57687.1; -; Genomic_DNA. DR EMBL; U14003; AAA96988.1; ALT_INIT; Genomic_DNA. DR EMBL; U00096; AAC77050.2; -; Genomic_DNA. DR EMBL; AP009048; BAE78092.1; -; Genomic_DNA. DR PIR; S56317; S56317. DR RefSeq; NP_418513.4; NC_000913.3. DR RefSeq; WP_000083216.1; NZ_STEB01000014.1. DR AlphaFoldDB; P0ACS7; -. DR SMR; P0ACS7; -. DR BioGRID; 4262682; 173. DR IntAct; P0ACS7; 5. DR STRING; 511145.b4089; -. DR jPOST; P0ACS7; -. DR PaxDb; 511145-b4089; -. DR DNASU; 948603; -. DR EnsemblBacteria; AAC77050; AAC77050; b4089. DR GeneID; 948603; -. DR KEGG; ecj:JW4050; -. DR KEGG; eco:b4089; -. DR PATRIC; fig|511145.12.peg.4216; -. DR EchoBASE; EB2353; -. DR eggNOG; COG1737; Bacteria. DR HOGENOM; CLU_055769_0_5_6; -. DR InParanoid; P0ACS7; -. DR OMA; EDMILWN; -. DR OrthoDB; 8582409at2; -. DR PhylomeDB; P0ACS7; -. DR BioCyc; EcoCyc:G7821-MONOMER; -. DR PRO; PR:P0ACS7; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central. DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:EcoCyc. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR CDD; cd05013; SIS_RpiR; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR000281; HTH_RpiR. DR InterPro; IPR047640; RpiR-like. DR InterPro; IPR035472; RpiR-like_SIS. DR InterPro; IPR001347; SIS_dom. DR InterPro; IPR046348; SIS_dom_sf. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR PANTHER; PTHR30514; GLUCOKINASE; 1. DR PANTHER; PTHR30514:SF1; HTH-TYPE TRANSCRIPTIONAL REGULATOR HEXR-RELATED; 1. DR Pfam; PF01418; HTH_6; 1. DR Pfam; PF01380; SIS; 1. DR SUPFAM; SSF46689; Homeodomain-like; 1. DR SUPFAM; SSF53697; SIS domain; 1. DR PROSITE; PS51071; HTH_RPIR; 1. DR PROSITE; PS51464; SIS; 1. PE 1: Evidence at protein level; KW DNA-binding; Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1..296 FT /note="HTH-type transcriptional regulator RpiR" FT /id="PRO_0000068620" FT DOMAIN 14..90 FT /note="HTH rpiR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00390" FT DOMAIN 134..274 FT /note="SIS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797" FT DNA_BIND 50..69 FT /note="H-T-H motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00390" SQ SEQUENCE 296 AA; 32362 MW; 7946848F0798E200 CRC64; MSQSEFDSAL PNGIGLAPYL RMKQEGMTEN ESRIVEWLLK PGNLSCAPAI KDVAEALAVS EAMIVKVSKL LGFSGFRNLR SALEDYFSQS EQVLPSELAF DEAPQDVVNK VFNITLRTIM EGQSIVNVDE IHRAARFFYQ ARQRDLYGAG GSNAICADVQ HKFLRIGVRC QAYPDAHIMM MSASLLQEGD VVLVVTHSGR TSDVKAAVEL AKKNGAKIIC ITHSYHSPIA KLADYIICSP APETPLLGRN ASARILQLTL LDAFFVSVAQ LNIEQANINM QKTGAIVDFF SPGALK //