ID   ARCD1_LACLM             Reviewed;         526 AA.
AC   A2RNI5; Q9K574;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Arginine/ornithine antiporter ArcD1 {ECO:0000305};
DE   AltName: Full=Arginine/ornithine exchanger {ECO:0000303|PubMed:26324452};
GN   Name=arcD1 {ECO:0000303|PubMed:23144255};
GN   Synonyms=arcD {ECO:0000312|EMBL:CAB93581.2};
GN   OrderedLocusNames=llmg_2311 {ECO:0000312|EMBL:CAL98875.1};
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MG1363;
RA   Aungpraphapornchai P., Mulholland F., Griffin H.G., Gasson M.J.;
RT   "Cloning, sequencing and analysis of the genes involved in the arginine
RT   deiminase pathway of Lactococus lactis.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
RN   [3]
RP   FUNCTION.
RC   STRAIN=MG1363;
RX   PubMed=23144255; DOI=10.1128/jb.01948-12;
RA   Trip H., Mulder N.L., Lolkema J.S.;
RT   "Cloning, expression, and functional characterization of secondary amino
RT   acid transporters of Lactococcus lactis.";
RL   J. Bacteriol. 195:340-350(2013).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=MG1363;
RX   PubMed=26324452; DOI=10.1128/jb.00526-15;
RA   Noens E.E., Kaczmarek M.B., Zygo M., Lolkema J.S.;
RT   "ArcD1 and ArcD2 arginine/ornithine exchangers encoded in the arginine
RT   deiminase pathway gene cluster of Lactococcus lactis.";
RL   J. Bacteriol. 197:3545-3553(2015).
CC   -!- FUNCTION: Catalyzes electroneutral exchange between L-arginine and L-
CC       ornithine (PubMed:23144255, PubMed:26324452). Can also efficiently
CC       translocate L-histidine and L-lysine (PubMed:26324452). ArcD1 is the
CC       main L-arginine/L-ornithine exchanger in the arginine deiminase (ADI)
CC       pathway (PubMed:26324452). {ECO:0000269|PubMed:23144255,
CC       ECO:0000269|PubMed:26324452}.
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:0000269|PubMed:26324452};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34992;
CC         Evidence={ECO:0000269|PubMed:26324452};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5 uM for L-arginine {ECO:0000269|PubMed:26324452};
CC         KM=1 uM for L-ornithine {ECO:0000269|PubMed:26324452};
CC         Vmax=30 nmol/min/mg enzyme toward L-arginine
CC         {ECO:0000269|PubMed:26324452};
CC         Vmax=45 nmol/min/mg enzyme toward L-ornithine
CC         {ECO:0000269|PubMed:26324452};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Deletion results in loss of the growth advantage
CC       observed in the presence of high L-arginine in different growth media.
CC       {ECO:0000269|PubMed:26324452}.
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; AJ250129; CAB93581.2; -; Genomic_DNA.
DR   EMBL; AM406671; CAL98875.1; -; Genomic_DNA.
DR   RefSeq; WP_011835984.1; NZ_WJVF01000005.1.
DR   AlphaFoldDB; A2RNI5; -.
DR   SMR; A2RNI5; -.
DR   STRING; 416870.llmg_2311; -.
DR   EnsemblBacteria; CAL98875; CAL98875; llmg_2311.
DR   KEGG; llm:llmg_2311; -.
DR   eggNOG; COG0531; Bacteria.
DR   HOGENOM; CLU_007946_1_2_9; -.
DR   OMA; FNSDNRV; -.
DR   PhylomeDB; A2RNI5; -.
DR   SABIO-RK; A2RNI5; -.
DR   Proteomes; UP000000364; 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   1: Evidence at protein level;
KW   Amino-acid transport; Antiport; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..526
FT                   /note="Arginine/ornithine antiporter ArcD1"
FT                   /id="PRO_0000437969"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        466..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        495..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   526 AA;  56406 MW;  C74E7A5FE862704B CRC64;
     MDAENKKGIG LAALVAIIVS GAIGGGVFNL SNDLATNASP GGVVISWIVI GFGILMLVLS
     LNHLVVNKPE LSGVSDYARA GFGNMVGFIS GWGYWLSAWA GNIAFAVLMM TSVDYFFPGV
     FQAKNGSLTI LSVIVVSIVS WGLTLLVMRG VEGAAAINAI VLVAKLIPLF VFVIAGIVTF
     KAGVFSAHFW QNFVANTNAD GVIKSLTWSN MTGGDLFSQV KGSLMVMIWV FVGIEGAAMM
     GDRAKRKSDA GKASIFGLIA LLVIYILLSL LPFGFMSQQE LANTGQPGLV HILNAMVGGW
     GGSLMAIGLV ISLLGAWLSW TMLPVEATQQ LSEQKLLPSW FGKLNDKGAP KNSLLLTQLI
     VQIFLIVTYF VADAYNVFVY LCTAVIMICY ALVGLYLFKL GIQEKKTSNI IIGFIAAAFQ
     ILALYYSGWQ FVWLSLILYA VGFILYALGK KEYGTKMSTT EVIATFILTV LGILAVFGVY
     GNWLGLQDAL GIDGNTLLVA VVPLIVVTFI VYFVVRSDIN KKGIKN