ID ADEP_ECOLI Reviewed; 445 AA.
AC P31466; P76741; Q2M832;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 27-MAR-2024, entry version 155.
DE RecName: Full=Adenine permease AdeP;
GN Name=adeP; Synonyms=purP, yieG; OrderedLocusNames=b3714, JW3692;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
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 FUNCTION.
RX PubMed=6198438; DOI=10.1099/00221287-129-11-3505;
RA Burton K.;
RT "Transport of nucleic acid bases into Escherichia coli.";
RL J. Gen. Microbiol. 129:3505-3513(1983).
RN [5]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=8165228; DOI=10.1098/rspb.1994.0022;
RA Burton K.;
RT "Adenine transport in Escherichia coli.";
RL Proc. R. Soc. B 255:153-157(1994).
RN [6]
RP SUBCELLULAR LOCATION [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 [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TOPOLOGY,
RP GENE NAME, AND MUTAGENESIS OF THR-38; ALA-91; ASP-267; THR-271; ASP-298;
RP ILE-317; GLU-318 AND SER-319.
RC STRAIN=K12;
RX PubMed=24214977; DOI=10.1074/jbc.m113.523340;
RA Papakostas K., Botou M., Frillingos S.;
RT "Functional identification of the hypoxanthine/guanine transporters YjcD
RT and YgfQ and the adenine transporters PurP and YicO of Escherichia coli K-
RT 12.";
RL J. Biol. Chem. 288:36827-36840(2013).
CC -!- FUNCTION: High-affinity transporter for adenine.
CC {ECO:0000269|PubMed:24214977, ECO:0000269|PubMed:6198438,
CC ECO:0000269|PubMed:8165228}.
CC -!- ACTIVITY REGULATION: Internal adenine may inhibit transport.
CC {ECO:0000269|PubMed:8165228}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 uM for adenine {ECO:0000269|PubMed:24214977};
CC Vmax=1.7 nmol/min/mg enzyme {ECO:0000269|PubMed:24214977};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:24214977}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:24214977}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. Azg-like subfamily. {ECO:0000305}.
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DR EMBL; L10328; AAA62065.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76737.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77574.1; -; Genomic_DNA.
DR PIR; C65174; C65174.
DR RefSeq; NP_418170.1; NC_000913.3.
DR RefSeq; WP_000019348.1; NZ_SSZK01000035.1.
DR AlphaFoldDB; P31466; -.
DR SMR; P31466; -.
DR BioGRID; 4262172; 283.
DR STRING; 511145.b3714; -.
DR TCDB; 2.A.40.7.6; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR jPOST; P31466; -.
DR PaxDb; 511145-b3714; -.
DR DNASU; 948224; -.
DR EnsemblBacteria; AAC76737; AAC76737; b3714.
DR GeneID; 948224; -.
DR KEGG; ecj:JW3692; -.
DR KEGG; eco:b3714; -.
DR PATRIC; fig|1411691.4.peg.2987; -.
DR EchoBASE; EB1675; -.
DR eggNOG; COG2252; Bacteria.
DR HOGENOM; CLU_024508_0_1_6; -.
DR InParanoid; P31466; -.
DR OMA; RKGSYFF; -.
DR OrthoDB; 9808458at2; -.
DR PhylomeDB; P31466; -.
DR BioCyc; EcoCyc:EG11724-MONOMER; -.
DR BioCyc; MetaCyc:EG11724-MONOMER; -.
DR SABIO-RK; P31466; -.
DR PRO; PR:P31466; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015207; F:adenine transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015295; F:solute:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0015853; P:adenine transport; IDA:EcoCyc.
DR InterPro; IPR045018; Azg-like.
DR InterPro; IPR026033; Azg-like_bact_archaea.
DR InterPro; IPR006043; NCS2.
DR PANTHER; PTHR43337; XANTHINE/URACIL PERMEASE C887.17-RELATED; 1.
DR PANTHER; PTHR43337:SF1; XANTHINE_URACIL PERMEASE C887.17-RELATED; 1.
DR Pfam; PF00860; Xan_ur_permease; 1.
DR PIRSF; PIRSF005353; PbuG; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..445
FT /note="Adenine permease AdeP"
FT /id="PRO_0000169638"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..62
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..100
FT /note="Discontinuously helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..112
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..181
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..250
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..310
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..326
FT /note="Discontinuously helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..356
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 382..417
FT /note="Discontinuously helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 38
FT /note="T->A: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 38
FT /note="T->H: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 91
FT /note="A->G,S: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 267
FT /note="D->A,N: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 267
FT /note="D->E: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 271
FT /note="T->A,S: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 271
FT /note="T->D: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 271
FT /note="T->N: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 298
FT /note="D->E: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 298
FT /note="D->N: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 317
FT /note="I->A: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 317
FT /note="I->E: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 318
FT /note="E->D: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 318
FT /note="E->Q: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 319
FT /note="S->A,N: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
SQ SEQUENCE 445 AA; 46866 MW; 899FC4A38FD62E2A CRC64;
MSHQHTTQTS GQGMLERVFK LREHGTTART EVIAGFTTFL TMVYIVFVNP QILGVAGMDT
SAVFVTTCLI AAFGSIMMGL FANLPVALAP AMGLNAFFAF VVVQAMGLPW QVGMGAIFWG
AIGLLLLTIF RVRYWMIANI PVSLRVGITS GIGLFIGMMG LKNAGVIVAN PETLVSIGNL
TSHSVLLGIL GFFIIAILAS RNIHAAVLVS IVVTTLLGWM LGDVHYNGIV SAPPSVMTVV
GHVDLAGSFN LGLAGVIFSF MLVNLFDSSG TLIGVTDKAG LADEKGKFPR MKQALYVDSI
SSVTGSFIGT SSVTAYIESS SGVSVGGRTG LTAVVVGLLF LLVIFLSPLA GMVPGYAAAG
ALIYVGVLMT SSLARVNWQD LTESVPAFIT AVMMPFSFSI TEGIALGFIS YCVMKIGTGR
LRDLSPCVII VALLFILKIV FIDAH
//
