ARGO_ECOLI
ID ARGO_ECOLI Reviewed; 211 AA.
AC P11667; Q2M9R9;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Arginine exporter protein ArgO {ECO:0000255|HAMAP-Rule:MF_01901, ECO:0000305};
GN Name=argO {ECO:0000255|HAMAP-Rule:MF_01901, ECO:0000303|PubMed:15150242};
GN Synonyms=yggA; OrderedLocusNames=b2923, JW2890;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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=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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-211.
RC STRAIN=K12 / CS520;
RX PubMed=2546007; DOI=10.1111/j.1365-2958.1989.tb00221.x;
RA Alefounder P.R., Perham R.N.;
RT "Identification, molecular cloning and sequence analysis of a gene cluster
RT encoding the class II fructose 1,6-bisphosphate aldolase, 3-
RT phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate
RT dehydrogenase of Escherichia coli.";
RL Mol. Microbiol. 3:723-732(1989).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=15150242; DOI=10.1128/jb.186.11.3539-3546.2004;
RA Nandineni M.R., Gowrishankar J.;
RT "Evidence for an arginine exporter encoded by yggA (argO) that is regulated
RT by the LysR-type transcriptional regulator ArgP in Escherichia coli.";
RL J. Bacteriol. 186:3539-3546(2004).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
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 [6]
RP SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, AND MUTAGENESIS OF GLY-20;
RP GLN-22; ASP-47; ILE-51; ALA-60; ASP-128; VAL-132; SER-156 AND PHE-160.
RX PubMed=27645388; DOI=10.1128/jb.00423-16;
RA Pathania A., Gupta A.K., Dubey S., Gopal B., Sardesai A.A.;
RT "The topology of the L-arginine exporter ArgO conforms to an Nin-Cout
RT configuration in Escherichia coli: requirement for the cytoplasmic N-
RT terminal domain, functional helical interactions, and an aspartate pair for
RT ArgO function.";
RL J. Bacteriol. 198:3186-3199(2016).
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. May also be involved in the export of canavanine
CC (a plant-derived antimetabolite). {ECO:0000269|PubMed:15150242}.
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 ECO:0000269|PubMed:15150242};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32144;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01901,
CC ECO:0000269|PubMed:15150242};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:27645388}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01901, ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:27645388}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01901, ECO:0000269|PubMed:27645388}.
CC -!- INDUCTION: Transcriptionally regulated by ArgP in response to the
CC accumulation of intracellular arginine or canavanine. Lysine has a
CC negative effect on the expression of argO.
CC {ECO:0000269|PubMed:15150242}.
CC -!- DOMAIN: The cytoplasmic N-terminal domain is important for ArgO
CC function in vivo, but not the periplasmic C-terminal region. A pair of
CC conserved aspartate residues, located near the opposing edges of the
CC cytoplasmic membrane, may play a pivotal role in facilitating
CC transmembrane arginine flux. {ECO:0000269|PubMed:27645388}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant is supersensitive to the
CC arginine analog canavanine. {ECO:0000269|PubMed:15150242}.
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; U28377; AAA69090.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75960.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76987.1; -; Genomic_DNA.
DR EMBL; X14436; CAA32607.1; -; Genomic_DNA.
DR PIR; B65077; QQEC5A.
DR RefSeq; NP_417398.1; NC_000913.3.
DR RefSeq; WP_000493352.1; NZ_SSZK01000003.1.
DR AlphaFoldDB; P11667; -.
DR BioGRID; 4263380; 12.
DR STRING; 511145.b2923; -.
DR TCDB; 2.A.75.1.2; the l-lysine exporter (lyse) family.
DR PaxDb; P11667; -.
DR PRIDE; P11667; -.
DR EnsemblBacteria; AAC75960; AAC75960; b2923.
DR EnsemblBacteria; BAE76987; BAE76987; BAE76987.
DR GeneID; 947418; -.
DR KEGG; ecj:JW2890; -.
DR KEGG; eco:b2923; -.
DR PATRIC; fig|1411691.4.peg.3809; -.
DR EchoBASE; EB1148; -.
DR eggNOG; COG1279; Bacteria.
DR HOGENOM; CLU_087840_0_1_6; -.
DR InParanoid; P11667; -.
DR OMA; FARPRAW; -.
DR PhylomeDB; P11667; -.
DR BioCyc; EcoCyc:YGGA-MON; -.
DR BioCyc; MetaCyc:YGGA-MON; -.
DR PRO; PR:P11667; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR GO; GO:1903826; P:L-arginine transmembrane transport; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..211
FT /note="Arginine exporter protein ArgO"
FT /id="PRO_0000204158"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27645388"
FT TRANSMEM 39..58
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:27645388"
FT TOPO_DOM 59..63
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:27645388"
FT TRANSMEM 64..91
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:27645388"
FT TOPO_DOM 92..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27645388"
FT TRANSMEM 103..130
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:27645388"
FT TOPO_DOM 131..140
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:27645388"
FT TRANSMEM 141..170
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:27645388"
FT TOPO_DOM 171..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27645388"
FT TRANSMEM 174..200
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:27645388"
FT TOPO_DOM 201..211
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:27645388"
FT MUTAGEN 20
FT /note="G->C: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:27645388"
FT MUTAGEN 22
FT /note="Q->R: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:27645388"
FT MUTAGEN 47
FT /note="D->A: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:27645388"
FT MUTAGEN 47
FT /note="D->E: Retains transport activity."
FT /evidence="ECO:0000269|PubMed:27645388"
FT MUTAGEN 51
FT /note="I->T: Retains transport activity."
FT /evidence="ECO:0000269|PubMed:27645388"
FT MUTAGEN 60
FT /note="A->P: Retains transport activity."
FT /evidence="ECO:0000269|PubMed:27645388"
FT MUTAGEN 128
FT /note="D->A,Y: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:27645388"
FT MUTAGEN 128
FT /note="D->E: Retains transport activity."
FT /evidence="ECO:0000269|PubMed:27645388"
FT MUTAGEN 132
FT /note="V->A: Retains transport activity."
FT /evidence="ECO:0000269|PubMed:27645388"
FT MUTAGEN 156
FT /note="S->F: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:27645388"
FT MUTAGEN 160
FT /note="F->S: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:27645388"
SQ SEQUENCE 211 AA; 23176 MW; 2DAFE27B6A9BE822 CRC64;
MFSYYFQGLA LGAAMILPLG PQNAFVMNQG IRRQYHIMIA LLCAISDLVL ICAGIFGGSA
LLMQSPWLLA LVTWGGVAFL LWYGFGAFKT AMSSNIELAS AEVMKQGRWK IIATMLAVTW
LNPHVYLDTF VVLGSLGGQL DVEPKRWFAL GTISASFLWF FGLALLAAWL APRLRTAKAQ
RIINLVVGCV MWFIALQLAR DGIAHAQALF S
