ARGO_SALPA
ID ARGO_SALPA Reviewed; 211 AA.
AC Q5PJI9;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Arginine exporter protein ArgO {ECO:0000255|HAMAP-Rule:MF_01901};
GN Name=argO {ECO:0000255|HAMAP-Rule:MF_01901}; OrderedLocusNames=SPA2937;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
CC -!- FUNCTION: Involved in the export of arginine. Important to control the
CC intracellular level of arginine and the correct balance between
CC arginine and lysine. {ECO:0000255|HAMAP-Rule:MF_01901}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginine(in) = L-arginine(out); Xref=Rhea:RHEA:32143,
CC ChEBI:CHEBI:32682; Evidence={ECO:0000255|HAMAP-Rule:MF_01901};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32144;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01901};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01901}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01901}.
CC -!- SIMILARITY: Belongs to the LysE/ArgO transporter (TC 2.A.75) family.
CC {ECO:0000255|HAMAP-Rule:MF_01901, ECO:0000305}.
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DR EMBL; CP000026; AAV78775.1; -; Genomic_DNA.
DR RefSeq; WP_000626872.1; NC_006511.1.
DR AlphaFoldDB; Q5PJI9; -.
DR EnsemblBacteria; AAV78775; AAV78775; SPA2937.
DR KEGG; spt:SPA2937; -.
DR HOGENOM; CLU_087840_0_1_6; -.
DR OMA; FARPRAW; -.
DR Proteomes; UP000008185; 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:0061459; F:L-arginine transmembrane transporter activity; IEA:InterPro.
DR HAMAP; MF_01901; ArgO; 1.
DR InterPro; IPR023445; Arg_export_ArgO_enterobac.
DR InterPro; IPR001123; LeuE-type.
DR InterPro; IPR004777; Lys/arg_exporter.
DR PANTHER; PTHR30086; PTHR30086; 1.
DR Pfam; PF01810; LysE; 1.
DR TIGRFAMs; TIGR00948; 2a75; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..211
FT /note="Arginine exporter protein ArgO"
FT /id="PRO_0000204164"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01901"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01901"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01901"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01901"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01901"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01901"
SQ SEQUENCE 211 AA; 23248 MW; 75F211F1290D9B8B CRC64;
MISYYFQGFA LGVAMILPLG PQNAFVMNQG IRRQYHLMIA LLCALSDLVL ISAGIFGGSA
LLMQSPWLLA LVTWGGVAFL LWYGFGALKT AMSSNLELAS AEVMKQGRWK IIATMLAVTW
LNPHVYLDTF VVLGSLGGQL AMEPKRWFAL GTISASFLWF FGLALLAAWL APRLRTAKAQ
RIINILVGVV MWLIAFQLAR EGVAHMHALF N