ADIC_ECOL6
ID ADIC_ECOL6 Reviewed; 445 AA.
AC P60062; P39268; P39269;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Arginine/agmatine antiporter;
GN Name=adiC; OrderedLocusNames=c5120;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Major component of the acid-resistance (AR) system allowing
CC enteric pathogens to survive the acidic environment in the stomach.
CC Exchanges extracellular arginine for its intracellular decarboxylation
CC product agmatine (Agm) thereby expelling intracellular protons.
CC Probably undergoes several conformational states in order to
CC translocate the substrate across the membrane; keeps the substrate
CC accessible to only 1 side of the membrane at a time by opening and
CC closing 3 membrane-internal gates. {ECO:0000250|UniProtKB:P60063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=agmatine(in) + L-arginine(out) = agmatine(out) + L-
CC arginine(in); Xref=Rhea:RHEA:29651, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:58145; Evidence={ECO:0000250|UniProtKB:P60061};
CC -!- SUBUNIT: Homodimer; each subunit has its own individual transport
CC capacity. {ECO:0000250|UniProtKB:P60061}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P60061}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: Each subunit has 12 transmembrane (TM) helices; TM1 and TM6 are
CC interrupted by short non-helical Gly-rich loops in the middle of their
CC transmembrane spans. Each subunit has a central cavity which binds
CC substrate. {ECO:0000250|UniProtKB:P60061}.
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; AE014075; AAN83544.1; -; Genomic_DNA.
DR RefSeq; WP_000093154.1; NC_004431.1.
DR AlphaFoldDB; P60062; -.
DR SMR; P60062; -.
DR STRING; 199310.c5120; -.
DR EnsemblBacteria; AAN83544; AAN83544; c5120.
DR GeneID; 66671974; -.
DR KEGG; ecc:c5120; -.
DR eggNOG; COG0531; Bacteria.
DR HOGENOM; CLU_007946_1_0_6; -.
DR OMA; YDGWILI; -.
DR BioCyc; ECOL199310:C5120-MON; -.
DR Proteomes; UP000001410; 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 Pfam; PF13520; AA_permease_2; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Antiport; Cell inner membrane; Cell membrane;
KW Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..445
FT /note="Arginine/agmatine antiporter"
FT /id="PRO_0000054231"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..38
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..122
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..196
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..275
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..355
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..408
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 23
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 23
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 26
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 96
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 96
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 97
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 101
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 202
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 205
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 205
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 293
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 357
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT SITE 93
FT /note="Cytoplasmic (distal) gate"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT SITE 202
FT /note="Periplasmic (proximal) gate"
FT /evidence="ECO:0000250|UniProtKB:P60063"
FT SITE 208
FT /note="Cytoplasmic (distal) gate"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT SITE 293
FT /note="Middle gate"
FT /evidence="ECO:0000250|UniProtKB:P60063"
FT SITE 365
FT /note="Cytoplasmic (distal) gate"
FT /evidence="ECO:0000250|UniProtKB:P60061"
SQ SEQUENCE 445 AA; 46843 MW; 359F70C489A20663 CRC64;
MSSDADAHKV GLIPVTLMVS GNIMGSGVFL LPANLASTGG IAIYGWLVTI IGALGLSMVY
AKMSFLDPSP GGSYAYARRC FGPFLGYQTN VLYWLACWIG NIAMVVIGVG YLSYFFPILK
DPLVLTITCV VVLWIFVLLN IVGPKMITRV QAVATVLALI PIVGIAVFGW FWFRGETYMA
AWNVSGLGTF GAIQSTLNVT LWSFIGVESA SVAAGVVKNP KRNVPIATIG GVLIAAVCYV
LSTTAIMGMI PNAALRVSAS PFGDAARMAL GDTAGAIVSF CAAAGCLGSL GGWTLLAGQT
AKAAADDGLF PPIFARVNKA GTPVAGLIIV GILMTIFQLS SISPNATKEF GLVSSVSVIF
TLVPYLYTCA ALLLLGHGHF GKARPAYLAV TTIAFLYCIW AVVGSGAKEV MWSFVTLMVI
TAMYALNYNR LHKNPYPLDA PISKD
