ID   ARGBP_PSEAE             Reviewed;         259 AA.
AC   G3XD47;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=L-arginine-binding protein {ECO:0000305};
DE   Flags: Precursor;
GN   Name=aotJ {ECO:0000303|PubMed:9791103};
GN   OrderedLocusNames=PA0888 {ECO:0000312|EMBL:AAG04277.1};
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2]
RP   OPERON STRUCTURE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=9791103; DOI=10.1128/jb.180.21.5559-5566.1998;
RA   Nishijyo T., Park S.-M., Lu C.-D., Itoh Y., Abdelal A.T.;
RT   "Molecular characterization and regulation of an operon encoding a system
RT   for transport of arginine and ornithine and the ArgR regulatory protein in
RT   Pseudomonas aeruginosa.";
RL   J. Bacteriol. 180:5559-5566(1998).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1, and PAK;
RX   PubMed=18833300; DOI=10.1371/journal.pgen.1000211;
RA   Johnson D.A., Tetu S.G., Phillippy K., Chen J., Ren Q., Paulsen I.T.;
RT   "High-throughput phenotypic characterization of Pseudomonas aeruginosa
RT   membrane transport genes.";
RL   PLoS Genet. 4:e1000211-e1000211(2008).
RN   [4]
RP   FUNCTION AS A BINDING PROTEIN.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=31627455; DOI=10.3390/ijms20205156;
RA   Fernandez M., Rico-Jimenez M., Ortega A., Daddaoua A., Garcia Garcia A.I.,
RA   Martin-Mora D., Torres N.M., Tajuelo A., Matilla M.A., Krell T.;
RT   "Determination of Ligand Profiles for Pseudomonas aeruginosa Solute Binding
RT   Proteins.";
RL   Int. J. Mol. Sci. 20:5156-5156(2019).
CC   -!- FUNCTION: Binds L-arginine with high affinity. Shows no measurable
CC       affinity for L-ornithine. {ECO:0000269|PubMed:31627455}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- INDUCTION: Part of the aot operon that encodes proteins involved in the
CC       uptake of arginine and ornithine. Expression of the aot operon is
CC       strongly induced by arginine, via the HTH-type transcriptional
CC       regulator ArgR. {ECO:0000269|PubMed:9791103}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the aotJQMOP genes greatly reduces
CC       arginine and ornithine uptake (PubMed:9791103). Disruption mutant has a
CC       reduced capacity to use arginine and ornithine as sole carbon source
CC       for growth (PubMed:18833300). {ECO:0000269|PubMed:18833300,
CC       ECO:0000269|PubMed:9791103}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC       {ECO:0000305}.
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DR   EMBL; AE004091; AAG04277.1; -; Genomic_DNA.
DR   PIR; T44454; T44454.
DR   RefSeq; NP_249579.1; NC_002516.2.
DR   RefSeq; WP_003085932.1; NZ_QZGE01000007.1.
DR   AlphaFoldDB; G3XD47; -.
DR   SMR; G3XD47; -.
DR   STRING; 287.DR97_1055; -.
DR   PaxDb; G3XD47; -.
DR   PRIDE; G3XD47; -.
DR   DNASU; 879210; -.
DR   EnsemblBacteria; AAG04277; AAG04277; PA0888.
DR   GeneID; 879210; -.
DR   KEGG; pae:PA0888; -.
DR   PATRIC; fig|208964.12.peg.923; -.
DR   PseudoCAP; PA0888; -.
DR   HOGENOM; CLU_019602_18_0_6; -.
DR   InParanoid; G3XD47; -.
DR   OMA; GSIHERF; -.
DR   PhylomeDB; G3XD47; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005615; C:extracellular space; IDA:PseudoCAP.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005768; Lys_Arg_Orn-bd.
DR   InterPro; IPR018313; SBP_3_CS.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   SMART; SM00062; PBPb; 1.
DR   TIGRFAMs; TIGR01096; 3A0103s03R; 1.
DR   PROSITE; PS01039; SBP_BACTERIAL_3; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Periplasm; Reference proteome; Signal; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..259
FT                   /note="L-arginine-binding protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5003459634"
SQ   SEQUENCE   259 AA;  28010 MW;  894FC868CBC3EC15 CRC64;
     MKKLALLGAL ALSVLSLPTF AADKPVRIGI EAAYPPFSLK TPDGQLAGFD VDIGNALCEE
     MKVQCKWVEQ EFDGLIPALK VRKIDAILSS MTITDERKRS VDFTNKYYNT PARFVMKEGA
     SLNDPKADLK GKKAGVLRGS TADRYASAEL TPAGVEVVRY NSQQEANMDL VAGRLDAVVA
     DSVNLEDGFL KTDAGKGYAF VGPQLTDAKY FGEGVGIAVR KGDSELAGKF NAAIDALRAN
     GKYKQIQDKY FSFDVYGSN