ARCD_SHIFL
ID ARCD_SHIFL Reviewed; 460 AA.
AC P0AAE7; P77429;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Putative arginine/ornithine antiporter {ECO:0000250|UniProtKB:P18275};
GN Name=ydgI; OrderedLocusNames=SF1626, S1758;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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}.
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DR EMBL; AE005674; AAN43209.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17097.1; -; Genomic_DNA.
DR RefSeq; NP_707502.1; NC_004337.2.
DR RefSeq; WP_000412379.1; NZ_WPGW01000024.1.
DR AlphaFoldDB; P0AAE7; -.
DR SMR; P0AAE7; -.
DR STRING; 198214.SF1626; -.
DR EnsemblBacteria; AAN43209; AAN43209; SF1626.
DR EnsemblBacteria; AAP17097; AAP17097; S1758.
DR GeneID; 1024796; -.
DR GeneID; 66674504; -.
DR KEGG; sfl:SF1626; -.
DR KEGG; sfx:S1758; -.
DR PATRIC; fig|198214.7.peg.1920; -.
DR HOGENOM; CLU_007946_1_2_6; -.
DR OMA; FNSDNRV; -.
DR OrthoDB; 527053at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..460
FT /note="Putative arginine/ornithine antiporter"
FT /id="PRO_0000054243"
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
