ID   ARCD_ECOLI              Reviewed;         460 AA.
AC   P0AAE5; P77429;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=Putative arginine/ornithine antiporter {ECO:0000250|UniProtKB:P18275};
GN   Name=ydgI; OrderedLocusNames=b1605, JW1597;
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 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(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   SUBCELLULAR LOCATION, AND 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).
CC   -!- FUNCTION: Catalyzes electroneutral exchange between arginine and
CC       ornithine to allow high-efficiency energy conversion in the arginine
CC       deiminase pathway. {ECO:0000250|UniProtKB:P18275}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine(out) + L-ornithine(in) = L-arginine(in) + L-
CC         ornithine(out); Xref=Rhea:RHEA:34991, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:46911; Evidence={ECO:0000250|UniProtKB:P18275};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34992;
CC         Evidence={ECO:0000250|UniProtKB:P18275};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. Basic amino acid/polyamine antiporter (APA) (TC 2.A.3.2)
CC       family. {ECO:0000305}.
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DR   EMBL; U00096; AAC74677.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15343.1; -; Genomic_DNA.
DR   PIR; G64916; G64916.
DR   RefSeq; NP_416122.1; NC_000913.3.
DR   RefSeq; WP_000412379.1; NZ_STEB01000003.1.
DR   AlphaFoldDB; P0AAE5; -.
DR   SMR; P0AAE5; -.
DR   BioGRID; 4259127; 251.
DR   DIP; DIP-48049N; -.
DR   IntAct; P0AAE5; 1.
DR   STRING; 511145.b1605; -.
DR   TCDB; 2.A.3.2.8; the amino acid-polyamine-organocation (apc) family.
DR   PaxDb; 511145-b1605; -.
DR   EnsemblBacteria; AAC74677; AAC74677; b1605.
DR   GeneID; 75204449; -.
DR   GeneID; 945159; -.
DR   KEGG; ecj:JW1597; -.
DR   KEGG; eco:b1605; -.
DR   PATRIC; fig|1411691.4.peg.657; -.
DR   EchoBASE; EB3689; -.
DR   eggNOG; COG0531; Bacteria.
DR   HOGENOM; CLU_007946_1_2_6; -.
DR   InParanoid; P0AAE5; -.
DR   OMA; FNSDNRV; -.
DR   OrthoDB; 3185104at2; -.
DR   PhylomeDB; P0AAE5; -.
DR   BioCyc; EcoCyc:ARCD-MONOMER; -.
DR   PRO; PR:P0AAE5; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; ISM:EcoCyc.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR004754; Amino_acid_antiprt.
DR   NCBIfam; TIGR00905; 2A0302; 1.
DR   PANTHER; PTHR42770; AMINO ACID TRANSPORTER-RELATED; 1.
DR   PANTHER; PTHR42770:SF4; ARGININE_ORNITHINE ANTIPORTER-RELATED; 1.
DR   Pfam; PF13520; AA_permease_2; 1.
DR   PIRSF; PIRSF006060; AA_transporter; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Antiport; Cell inner membrane; Cell membrane;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..460
FT                   /note="Putative arginine/ornithine antiporter"
FT                   /id="PRO_0000054241"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..38
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        60..92
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..125
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..201
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..235
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..282
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..331
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        353..357
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        358..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        379..384
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        406..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        427..439
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        440..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   460 AA;  49501 MW;  4E0FE8E1861FA1B3 CRC64;
     MEKKLGLSAL TALVLSSMLG AGVFSLPQNM AAVASPAALL IGWGITGAGI LLLAFAMLIL
     TRIRPELDGG IFTYAREGFG ELIGFCSAWG YWLCAVIANV SYLVIVFSAL SFFTDTPELR
     LFGDGNTWQS IVGASALLWI VHFLILRGVQ TAASINLVAT LAKLLPLGLF VVLAMMMFKL
     DTFKLDFTGL ALGVPVWEQV KNTMLITLWV FIGVEGAVVV SARARNKRDV GKATLLAVLS
     ALGVYLLVTL LSLGVVARPE LAEIRNPSMA GLMVEMMGPW GEIIIAAGLI VSVCGAYLSW
     TIMAAEVPFL AATHKAFPRI FARQNAQAAP SASLWLTNIC VQICLVLIWL TGSDYNTLLT
     IASEMILVPY FLVGAFLLKI ATRPLHKAVG VGACIYGLWL LYASGPMHLL LSVVLYAPGL
     LVFLYARKTH THDNVLNRQE MVLIGMLLIA SVPATWMLVG
//