RUTG_ECOLI
ID RUTG_ECOLI Reviewed; 442 AA.
AC P75892; Q9R3W5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Putative pyrimidine permease RutG;
GN Name=rutG; Synonyms=ycdG; OrderedLocusNames=b1006, JW5137;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
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 [3]
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 [4]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [5]
RP INDUCTION.
RX PubMed=11121068; DOI=10.1073/pnas.97.26.14674;
RA Zimmer D.P., Soupene E., Lee H.L., Wendisch V.F., Khodursky A.B.,
RA Peter B.J., Bender R.A., Kustu S.;
RT "Nitrogen regulatory protein C-controlled genes of Escherichia coli:
RT scavenging as a defense against nitrogen limitation.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14674-14679(2000).
RN [6]
RP FUNCTION IN PYRIMIDINE CATABOLISM AND NOMENCLATURE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16540542; DOI=10.1073/pnas.0600521103;
RA Loh K.D., Gyaneshwar P., Markenscoff Papadimitriou E., Fong R., Kim K.-S.,
RA Parales R., Zhou Z., Inwood W., Kustu S.;
RT "A previously undescribed pathway for pyrimidine catabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5114-5119(2006).
RN [7]
RP INDUCTION.
RX PubMed=17919280; DOI=10.1111/j.1365-2958.2007.05954.x;
RA Shimada T., Hirao K., Kori A., Yamamoto K., Ishihama A.;
RT "RutR is the uracil/thymine-sensing master regulator of a set of genes for
RT synthesis and degradation of pyrimidines.";
RL Mol. Microbiol. 66:744-757(2007).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=20400551; DOI=10.1128/jb.00201-10;
RA Kim K.S., Pelton J.G., Inwood W.B., Andersen U., Kustu S., Wemmer D.E.;
RT "The Rut pathway for pyrimidine degradation: novel chemistry and toxicity
RT problems.";
RL J. Bacteriol. 192:4089-4102(2010).
CC -!- FUNCTION: May function as a proton-driven pyrimidine uptake system.
CC {ECO:0000269|PubMed:16540542}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Up-regulated by the nitrogen regulatory protein C (NtrC also
CC called GlnG) and repressed by RutR. {ECO:0000269|PubMed:11121068,
CC ECO:0000269|PubMed:17919280}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to grow on the
CC nucleobase uracil as the sole nitrogen source but use the nucleoside
CC uridine normally. {ECO:0000269|PubMed:20400551}.
CC -!- MISCELLANEOUS: The Rut pathway degrades exogenous pyrimidines as the
CC sole nitrogen source at room temperature but not at 37 degrees Celsius,
CC a restriction that is apparently a consequence of an inadequate ability
CC to remove toxic malonic semialdehyde at the higher temperature
CC (RutE/YdfG function).
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. {ECO:0000305}.
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DR EMBL; U00096; AAC74091.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35773.1; -; Genomic_DNA.
DR PIR; D64842; D64842.
DR RefSeq; NP_415526.4; NC_000913.3.
DR RefSeq; WP_001326838.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P75892; -.
DR SMR; P75892; -.
DR BioGRID; 4259546; 9.
DR STRING; 511145.b1006; -.
DR TCDB; 2.A.40.1.3; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR PaxDb; P75892; -.
DR PRIDE; P75892; -.
DR EnsemblBacteria; AAC74091; AAC74091; b1006.
DR EnsemblBacteria; BAA35773; BAA35773; BAA35773.
DR GeneID; 946589; -.
DR KEGG; ecj:JW5137; -.
DR KEGG; eco:b1006; -.
DR PATRIC; fig|511145.12.peg.1044; -.
DR EchoBASE; EB3613; -.
DR eggNOG; COG2233; Bacteria.
DR HOGENOM; CLU_017959_1_1_6; -.
DR InParanoid; P75892; -.
DR OMA; FGLCPKF; -.
DR PhylomeDB; P75892; -.
DR BioCyc; EcoCyc:B1006-MON; -.
DR BioCyc; MetaCyc:B1006-MON; -.
DR PRO; PR:P75892; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005350; F:pyrimidine nucleobase transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015218; F:pyrimidine nucleotide transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015210; F:uracil transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015505; F:uracil:cation symporter activity; IDA:EcoCyc.
DR GO; GO:1904082; P:pyrimidine nucleobase transmembrane transport; IDA:EcoCyc.
DR GO; GO:0006212; P:uracil catabolic process; IMP:EcoCyc.
DR GO; GO:0098721; P:uracil import across plasma membrane; IDA:EcoCyc.
DR InterPro; IPR006043; NCS2.
DR InterPro; IPR019918; Pyrimidine_permease_RutG_pred.
DR InterPro; IPR006042; Xan_ur_permease.
DR Pfam; PF00860; Xan_ur_permease; 1.
DR TIGRFAMs; TIGR00801; ncs2; 1.
DR TIGRFAMs; TIGR03616; RutG; 1.
DR PROSITE; PS01116; XANTH_URACIL_PERMASE; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..442
FT /note="Putative pyrimidine permease RutG"
FT /id="PRO_0000165964"
FT TOPO_DOM 1..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..140
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..196
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..284
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..347
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 442 AA; 45557 MW; 35CC612A4E86DD67 CRC64;
MAMFGFPHWQ LKSTSTESGV VAPDERLPFA QTAVMGVQHA VAMFGATVLM PILMGLDPNL
SILMSGIGTL LFFFITGGRV PSYLGSSAAF VGVVIAATGF NGQGINPNIS IALGGIIACG
LVYTVIGLVV MKIGTRWIER LMPPVVTGAV VMAIGLNLAP IAVKSVSASA FDSWMAVMTV
LCIGLVAVFT RGMIQRLLIL VGLIVACLLY GVMTNVLGLG KAVDFTLVSH AAWFGLPHFS
TPAFNGQAMM LIAPVAVILV AENLGHLKAV AGMTGRNMDP YMGRAFVGDG LATMLSGSVG
GSGVTTYAEN IGVMAVTKVY STLVFVAAAV IAMLLGFSPK FGALIHTIPA AVIGGASIVV
FGLIAVAGAR IWVQNRVDLS QNGNLIMVAV TLVLGAGDFA LTLGGFTLGG IGTATFGAIL
LNALLSRKLV DVPPPEVVHQ EP
