ARCD_LATSK
ID ARCD_LATSK Reviewed; 475 AA.
AC O53092;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Arginine/ornithine antiporter {ECO:0000250|UniProtKB:A2RNI5};
GN Name=arcD;
OS Latilactobacillus sakei (Lactobacillus sakei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Latilactobacillus.
OX NCBI_TaxID=1599;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9696763; DOI=10.1128/jb.180.16.4154-4159.1998;
RA Zuniga M., Champomier-Verges M.-C., Zagorec M., Perez-Martinez G.;
RT "Structural and functional analysis of the gene cluster encoding the
RT enzymes of the arginine deiminase pathway of Lactobacillus sakei.";
RL J. Bacteriol. 180:4154-4159(1998).
CC -!- FUNCTION: Catalyzes electroneutral exchange between L-arginine and L-
CC ornithine. {ECO:0000250|UniProtKB:A2RNI5}.
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:0000250|UniProtKB:A2RNI5};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
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; AJ001330; CAA04686.1; -; Genomic_DNA.
DR PIR; T46745; T46745.
DR AlphaFoldDB; O53092; -.
DR SMR; O53092; -.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0043858; F:arginine:ornithine antiporter activity; IEA:InterPro.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR GO; GO:1903826; P:L-arginine transmembrane transport; IEA:InterPro.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR004754; Amino_acid_antiprt.
DR InterPro; IPR022461; Arg/Orn_antiprt_ArcD.
DR Pfam; PF13520; AA_permease_2; 1.
DR TIGRFAMs; TIGR00905; 2A0302; 1.
DR TIGRFAMs; TIGR03810; arg_ornith_anti; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Antiport; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..475
FT /note="Arginine/ornithine antiporter"
FT /id="PRO_0000054238"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 475 AA; 51881 MW; 8E91A01F6A2203CC CRC64;
MTEEKPAKKI GLLALIALVI SSSIGSGVFG LTSDLASASA PGPVLIAWVI VGFGILMLAL
SLNNLLMKEP ELEGIFSYAE KGFGPFAGFI SGWGYWLSAW LGNVTFATIL MSALGYFFPI
FKSRQNLPSI LVASVLSWSL TYFVNRGVEG AAAINTLVTI CKLIPLFVFI IFGIVLFKGH
LFTQAFWNNM SSSFVAGDVM SQIKNCMMVM MWVFVGIEGA SMLSARAEKK SDAGKATILG
LVSLLAIYIL ASVLPYGYLT QDQLASIKQP AMLYIFEQMV GTWGGYFIGV GLIISILGAW
LSWTMLPAET MLLMAKQNLL PAYFGRVNKK KAPTFALVVT AGLIQVFLFT LLFTTKAYNF
AYSLCTASII VCYMLVAAYQ IKYSWAHLQE KGNRQQLLIG VLALLFEIAG ILMAGVSYLL
LCFIAYIPGI YFYGRARKNN GHQHFLSKGE WLITTIIVIG AIIGIWLVVS GKIVI