ALLP_ECOLI
ID ALLP_ECOLI Reviewed; 484 AA.
AC P75712; P77127; Q2MBR7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Putative allantoin permease {ECO:0000250|UniProtKB:P94575};
DE AltName: Full=Allantoin transport protein {ECO:0000250|UniProtKB:P94575};
DE AltName: Full=Allantoin transporter {ECO:0000250|UniProtKB:P94575};
GN Name=ybbW; Synonyms=glxB2; OrderedLocusNames=b0511, JW0499;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=K12 / ECL1;
RX PubMed=10601204; DOI=10.1128/jb.181.24.7479-7484.1999;
RA Cusa E., Obradors N., Baldoma L., Badia J., Aguilar J.;
RT "Genetic analysis of a chromosomal region containing genes required for
RT assimilation of allantoin nitrogen and linked glyoxylate metabolism in
RT Escherichia coli.";
RL J. Bacteriol. 181:7479-7484(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Uptake of allantoin into the cell.
CC {ECO:0000250|UniProtKB:P94575}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-allantoin(in) + H(+)(in) = (S)-allantoin(out) + H(+)(out);
CC Xref=Rhea:RHEA:28723, ChEBI:CHEBI:15378, ChEBI:CHEBI:15678;
CC Evidence={ECO:0000250|UniProtKB:P94575};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28725;
CC Evidence={ECO:0000250|UniProtKB:P94575};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: By glyoxylate. {ECO:0000269|PubMed:10601204}.
CC -!- SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family.
CC {ECO:0000305}.
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DR EMBL; U89279; AAB93852.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40263.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73613.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76289.1; -; Genomic_DNA.
DR PIR; F64782; F64782.
DR RefSeq; NP_415044.4; NC_000913.3.
DR RefSeq; WP_000401100.1; NZ_SSZK01000024.1.
DR AlphaFoldDB; P75712; -.
DR SMR; P75712; -.
DR BioGRID; 4262820; 183.
DR STRING; 511145.b0511; -.
DR TCDB; 2.A.39.3.8; the nucleobase:cation symporter-1 (ncs1) family.
DR PaxDb; P75712; -.
DR PRIDE; P75712; -.
DR EnsemblBacteria; AAC73613; AAC73613; b0511.
DR EnsemblBacteria; BAE76289; BAE76289; BAE76289.
DR GeneID; 945138; -.
DR KEGG; ecj:JW0499; -.
DR KEGG; eco:b0511; -.
DR PATRIC; fig|1411691.4.peg.1767; -.
DR EchoBASE; EB3383; -.
DR eggNOG; COG1953; Bacteria.
DR HOGENOM; CLU_021555_0_0_6; -.
DR InParanoid; P75712; -.
DR OMA; GWNWRAV; -.
DR PhylomeDB; P75712; -.
DR BioCyc; EcoCyc:B0511-MON; -.
DR PRO; PR:P75712; -.
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:0015205; F:nucleobase transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015851; P:nucleobase transport; IBA:GO_Central.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR012681; NCS1.
DR InterPro; IPR001248; Pur-cyt_permease.
DR InterPro; IPR045225; Uracil/uridine/allantoin_perm.
DR PANTHER; PTHR30618; PTHR30618; 1.
DR Pfam; PF02133; Transp_cyt_pur; 1.
DR TIGRFAMs; TIGR00800; ncs1; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Purine metabolism;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..484
FT /note="Putative allantoin permease"
FT /id="PRO_0000197930"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..58
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..155
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..224
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..306
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..372
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 484 AA; 52456 MW; AE3DA5FF5043BF62 CRC64;
MEHQRKLFQQ RGYSEDLLPK TQSQRTWKTF NYFTLWMGSV HNVPNYVMVG GFFILGLSTF
SIMLAIILSA FFIAAVMVLN GAAGSKYGVP FAMILRASYG VRGALFPGLL RGGIAAIMWF
GLQCYAGSLA CLILIGKIWP GFLTLGGDFT LLGLSLPGLI TFLIFWLVNV GIGFGGGKVL
NKFTAILNPC IYIVFGGMAI WAISLVGIGP IFDYIPSGIQ KAENGGFLFL VVINAVVAVW
AAPAVSASDF TQNAHSFREQ ALGQTLGLVV AYILFAVAGV CIIAGASIHY GADTWNVLDI
VQRWDSLFAS FFAVLVILMT TISTNATGNI IPAGYQIAAI APTKLTYKNG VLIASIISLL
ICPWKLMENQ DSIYLFLDII GGMLGPVIGV MMAHYFVVMR GQINLDELYT APGDYKYYDN
GFNLTAFSVT LVAVILSLGG KFIHFMEPLS RVSWFVGVIV AFAAYALLKK RTTAEKTGEQ
KTIG
