ARCD_ECOL6
ID ARCD_ECOL6 Reviewed; 460 AA.
AC P0AAE6; P77429;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Putative arginine/ornithine antiporter {ECO:0000250|UniProtKB:P18275};
GN Name=ydgI; OrderedLocusNames=c1997;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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:0000250|UniProtKB:P0AAE5}; 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN80457.1; Type=Erroneous initiation; 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; AE014075; AAN80457.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000412379.1; NC_004431.1.
DR AlphaFoldDB; P0AAE6; -.
DR SMR; P0AAE6; -.
DR STRING; 199310.c1997; -.
DR EnsemblBacteria; AAN80457; AAN80457; c1997.
DR GeneID; 66674504; -.
DR KEGG; ecc:c1997; -.
DR eggNOG; COG0531; Bacteria.
DR HOGENOM; CLU_007946_1_2_6; -.
DR OMA; FNSDNRV; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR004754; Amino_acid_antiprt.
DR Pfam; PF13520; AA_permease_2; 1.
DR TIGRFAMs; TIGR00905; 2A0302; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Antiport; Cell inner membrane; Cell membrane;
KW Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..460
FT /note="Putative arginine/ornithine antiporter"
FT /id="PRO_0000054242"
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
