ARCD2_LACLM
ID ARCD2_LACLM Reviewed; 497 AA.
AC A2RNI1;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Arginine/ornithine antiporter ArcD2 {ECO:0000305};
DE AltName: Full=Arginine/ornithine exchanger {ECO:0000303|PubMed:26324452};
GN Name=arcD2 {ECO:0000303|PubMed:23144255};
GN OrderedLocusNames=llmg_2307 {ECO:0000312|EMBL:CAL98871.1};
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 [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 [2]
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 [3]
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). Can also efficiently translocate L-alanine
CC (PubMed:26324452). May function in vivo as a L-arginine/L-alanine
CC exchanger in a pathway together with the arcT gene, which is found
CC adjacent to the arcD2 gene in the ADI gene cluster (PubMed:26324452).
CC {ECO:0000269|PubMed:23144255, 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4 uM for L-arginine {ECO:0000269|PubMed:26324452};
CC KM=29 uM for L-ornithine {ECO:0000269|PubMed:26324452};
CC Vmax=22 nmol/min/mg enzyme toward L-arginine
CC {ECO:0000269|PubMed:26324452};
CC Vmax=128 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 does not affect the growth enhancement
CC observed in the presence of high L-arginine in different growth media,
CC and uptake activities are slightly reduced.
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; AM406671; CAL98871.1; -; Genomic_DNA.
DR RefSeq; WP_011835980.1; NZ_WJVF01000005.1.
DR AlphaFoldDB; A2RNI1; -.
DR SMR; A2RNI1; -.
DR STRING; 416870.llmg_2307; -.
DR EnsemblBacteria; CAL98871; CAL98871; llmg_2307.
DR KEGG; llm:llmg_2307; -.
DR eggNOG; COG0531; Bacteria.
DR HOGENOM; CLU_007946_1_2_9; -.
DR OMA; THDFWGE; -.
DR PhylomeDB; A2RNI1; -.
DR BioCyc; LLAC416870:LLMG_RS11565-MON; -.
DR SABIO-RK; A2RNI1; -.
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..497
FT /note="Arginine/ornithine antiporter ArcD2"
FT /id="PRO_0000437970"
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 127..147
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 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 497 AA; 53897 MW; 659567D399AB88F8 CRC64;
MENKKTKGIS LFALLAIIIS GAIGGGVFNL ANDLARGSTP GGVVISWLFI GFGILMLVLS
FNRLITIKPD LSGVSDYARA GFGDFVGFLS GWGYWISAWT GTIGFAVLMM TSADYFFPSK
FANSNGSLTI LSVIIVSIIS WILMLLVDRG VETAAAVNAI VMIAKLIPLV VFSITGIILF
KANVFTQHFW QTFTTNFAAD GSVKDFVWHA MTVSGLLSQI KGSLMVMVWV FVGIEGATMM
GNRAKKKSDT AKATVIGLAV LLVIYVLLSL LPYGYMDQAS LANVKAPGLV YILNEMVGGW
GGSLMAVGLM ISLLGAWLSW TMLPVEATQQ LAEQKLLPSW FGKLNKYHAP SNSLLITQLM
IQIFIIITYF VANAYNVFIY MATAVIMICY ALVGAYLFKI GLKEASVKNI LIGFFTFAFQ
ALALYLSGWQ YVWLAMILYT IGFLLFIGAK KESHQSISVK EWLGMLVVTV LGVLAIVVLI
CGAKAGTAFD LRGLLGF
