ARCD_PSEAE
ID ARCD_PSEAE Reviewed; 482 AA.
AC P18275;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Arginine/ornithine antiporter {ECO:0000303|PubMed:2158926};
DE AltName: Full=Arginine-ornithine exchanger {ECO:0000303|PubMed:1311296};
GN Name=arcD {ECO:0000303|PubMed:2158926}; OrderedLocusNames=PA5170;
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 [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=2158926; DOI=10.1016/0378-1119(90)90493-b;
RA Luethi E., Baur H., Gamper M., Brunner F., Villeval D., Mercenier A.,
RA Haas D.;
RT "The arc operon for anaerobic arginine catabolism in Pseudomonas aeruginosa
RT contains an additional gene, arcD, encoding a membrane protein.";
RL Gene 87:37-43(1990).
RN [2]
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=1311296; DOI=10.1128/jb.174.5.1568-1573.1992;
RA Verhoogt H.J., Smit H., Abee T., Gamper M., Driessen A.J., Haas D.,
RA Konings W.N.;
RT "arcD, the first gene of the arc operon for anaerobic arginine catabolism
RT in Pseudomonas aeruginosa, encodes an arginine-ornithine exchanger.";
RL J. Bacteriol. 174:1568-1573(1992).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8449902; DOI=10.1016/s0021-9258(18)53337-8;
RA Bourdineaud J.P., Heierli D., Gamper M., Verhoogt H.J., Driessen A.J.,
RA Konings W.N., Lazdunski C., Haas D.;
RT "Characterization of the arcD arginine:ornithine exchanger of Pseudomonas
RT aeruginosa. Localization in the cytoplasmic membrane and a topological
RT model.";
RL J. Biol. Chem. 268:5417-5424(1993).
CC -!- FUNCTION: Catalyzes electroneutral exchange between arginine and
CC ornithine to allow high-efficiency energy conversion in the arginine
CC deiminase pathway (PubMed:1311296, PubMed:8449902). Also mediates the
CC proton motive force-driven uptake of arginine and ornithine, but the
CC exchange is several orders of magnitude faster than the proton motive
CC force-driven transport (PubMed:1311296). {ECO:0000269|PubMed:1311296,
CC ECO:0000269|PubMed:8449902}.
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:1311296,
CC ECO:0000269|PubMed:8449902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34992;
CC Evidence={ECO:0000305|PubMed:1311296, ECO:0000305|PubMed:8449902};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:1311296,
CC ECO:0000269|PubMed:8449902}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:8449902}.
CC -!- DISRUPTION PHENOTYPE: Mutant is unable to utilize extracellular
CC arginine as an energy source under oxygen-limiting or anaerobic
CC conditions. {ECO:0000269|PubMed:2158926}.
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; M33223; AAA25719.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08555.1; -; Genomic_DNA.
DR PIR; JH0110; JH0110.
DR RefSeq; NP_253857.1; NC_002516.2.
DR RefSeq; WP_003123669.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; P18275; -.
DR SMR; P18275; -.
DR STRING; 287.DR97_2538; -.
DR TCDB; 2.A.3.2.3; the amino acid-polyamine-organocation (apc) family.
DR PaxDb; P18275; -.
DR PRIDE; P18275; -.
DR EnsemblBacteria; AAG08555; AAG08555; PA5170.
DR GeneID; 881800; -.
DR KEGG; pae:PA5170; -.
DR PATRIC; fig|208964.12.peg.5418; -.
DR PseudoCAP; PA5170; -.
DR HOGENOM; CLU_007946_1_2_6; -.
DR InParanoid; P18275; -.
DR OMA; THDFWGE; -.
DR PhylomeDB; P18275; -.
DR BioCyc; PAER208964:G1FZ6-5287-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0043858; F:arginine:ornithine antiporter activity; IMP:PseudoCAP.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0019546; P:arginine deiminase pathway; IMP:PseudoCAP.
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 1: Evidence at protein level;
KW Amino-acid transport; Antiport; Cell inner membrane; Cell membrane;
KW Membrane; Reference proteome; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..482
FT /note="Arginine/ornithine antiporter"
FT /id="PRO_0000054239"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8449902"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..40
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8449902"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8449902"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..124
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8449902"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8449902"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..202
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8449902"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8449902"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..283
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8449902"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8449902"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..365
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8449902"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8449902"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8449902"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8449902"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..482
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8449902"
SQ SEQUENCE 482 AA; 52027 MW; C7FC1A7323FB0607 CRC64;
MSQESSQKLR LGALTALVVG SMIGGGIFSL PQNMAASADV GAVLIGWAIT AVGMLTLAFV
FQTLANRKPE LDGGVYAYAK AGFGDYMGFS SAWGYWISAW LGNVGYFVLL FSTLGYFFPI
FGKGDTVAAI VCASVLLWAL HFLVLRGIKE AAFINTVTTV AKVVPLFLFI LICLFAFKLD
IFTADIWGKS NPDLGSVMNQ VRNMMLVTVW VFIGIEGASI FSSRAEKRSD VGKATVIGFI
TVLLLLVLVN VLSMGVMTQP ELAKLQNPSM ALVLEHVVGH WGAVLISVGL LISLLGALLS
WVLLCAEIMF AAAKDHTMPE FLRRENANQV PANALWLTNI CVQVFLVVVF FTSGDPDGMD
PYTKMLLLAT SMILIPYFWS AAYGLLLTLK GETYENDARE RSKDLVIAGI AVAYAVWLLY
AGGLKYLLLS ALLYAPGAIL FAKAKHEVGQ PIFTGIEKLI FAAVVIGALV AAYGLYDGFL
TL
