ADIC_SALTY
ID ADIC_SALTY Reviewed; 445 AA.
AC P60066; Q8XFJ0;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Arginine/agmatine antiporter;
GN Name=adiC; Synonyms=aniC; OrderedLocusNames=STM4294;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP INDUCTION.
RC STRAIN=UK-1;
RX PubMed=9882690; DOI=10.1128/jb.181.2.689-694.1999;
RA Park K.R., Giard J.-C., Eom J.H., Bearson S., Foster J.W.;
RT "Cyclic AMP receptor protein and TyrR are required for acid pH and
RT anaerobic induction of hyaB and aniC in Salmonella typhimurium.";
RL J. Bacteriol. 181:689-694(1999).
RN [3] {ECO:0007744|PDB:3NCY}
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN OUTWARD-OPEN CONFORMATION,
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=19578361; DOI=10.1038/nature08201;
RA Fang Y., Jayaram H., Shane T., Kolmakova-Partensky L., Wu F., Williams C.,
RA Xiong Y., Miller C.;
RT "Structure of a prokaryotic virtual proton pump at 3.2 A resolution.";
RL Nature 460:1040-1043(2009).
CC -!- FUNCTION: Major component of the acid-resistance (AR) system allowing
CC enteric pathogens to survive the acidic environment in the stomach
CC (Probable). Exchanges extracellular arginine for its intracellular
CC decarboxylation product agmatine (Agm) thereby expelling intracellular
CC protons (PubMed:19578361). Probably undergoes several conformational
CC states in order to translocate the substrate across the membrane; keeps
CC the substrate accessible to only 1 side of the membrane at a time by
CC opening and closing 3 membrane-internal gates (By similarity).
CC {ECO:0000250|UniProtKB:P60063, ECO:0000269|PubMed:19578361,
CC ECO:0000305|PubMed:19578361}.
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:0000305|PubMed:19578361};
CC -!- SUBUNIT: Homodimer; each subunit has its own individual transport
CC capacity. {ECO:0000269|PubMed:19578361}.
CC -!- INTERACTION:
CC P60066; P60066: adiC; NbExp=2; IntAct=EBI-15792734, EBI-15792734;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:19578361}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19578361}.
CC -!- INDUCTION: Maximum induction requires anaerobiosis, acidic conditions
CC and tyrosine. {ECO:0000269|PubMed:9882690}.
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. TM11 and TM12 provide most of the homodimerization
CC interface. Each subunit has a central cavity which probably binds
CC substrate. {ECO:0000269|PubMed:19578361}.
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; AE006468; AAL23118.1; -; Genomic_DNA.
DR RefSeq; NP_463159.1; NC_003197.2.
DR RefSeq; WP_000093130.1; NC_003197.2.
DR PDB; 3NCY; X-ray; 3.20 A; A/B/C/D=1-445.
DR PDBsum; 3NCY; -.
DR AlphaFoldDB; P60066; -.
DR SMR; P60066; -.
DR DIP; DIP-59280N; -.
DR STRING; 99287.STM4294; -.
DR PaxDb; P60066; -.
DR ABCD; P60066; 1 sequenced antibody.
DR EnsemblBacteria; AAL23118; AAL23118; STM4294.
DR GeneID; 1255820; -.
DR GeneID; 66758511; -.
DR KEGG; stm:STM4294; -.
DR PATRIC; fig|99287.12.peg.4516; -.
DR HOGENOM; CLU_007946_1_0_6; -.
DR OMA; YDGWILI; -.
DR PhylomeDB; P60066; -.
DR BioCyc; SENT99287:STM4294-MON; -.
DR EvolutionaryTrace; P60066; -.
DR Proteomes; UP000001014; 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:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Antiport; Cell inner membrane;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..445
FT /note="Arginine/agmatine antiporter"
FT /id="PRO_0000054235"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TRANSMEM 12..24
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TOPO_DOM 25..41
FT /note="Periplasmic"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TRANSMEM 42..61
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TOPO_DOM 62..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TRANSMEM 84..109
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TOPO_DOM 110..124
FT /note="Periplasmic"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TRANSMEM 125..142
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TOPO_DOM 143..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TRANSMEM 145..167
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TOPO_DOM 168..192
FT /note="Periplasmic"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TRANSMEM 193..204
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TOPO_DOM 205..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TRANSMEM 224..243
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TOPO_DOM 244..276
FT /note="Periplasmic"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TRANSMEM 277..301
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TOPO_DOM 302..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TRANSMEM 326..342
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TOPO_DOM 343..349
FT /note="Periplasmic"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TRANSMEM 350..373
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TOPO_DOM 374..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TRANSMEM 385..404
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TOPO_DOM 405..408
FT /note="Periplasmic"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TRANSMEM 409..427
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:3NCY"
FT TOPO_DOM 428..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0007744|PDB:3NCY"
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:P60063"
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:P60063"
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:P60063"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:3NCY"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:3NCY"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 43..66
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 84..98
FT /evidence="ECO:0007829|PDB:3NCY"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:3NCY"
FT TURN 110..114
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 122..140
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 144..164
FT /evidence="ECO:0007829|PDB:3NCY"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 189..200
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:3NCY"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:3NCY"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:3NCY"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 223..240
FT /evidence="ECO:0007829|PDB:3NCY"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:3NCY"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:3NCY"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 284..305
FT /evidence="ECO:0007829|PDB:3NCY"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:3NCY"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 327..342
FT /evidence="ECO:0007829|PDB:3NCY"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 348..360
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 362..374
FT /evidence="ECO:0007829|PDB:3NCY"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:3NCY"
FT TURN 379..382
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 384..403
FT /evidence="ECO:0007829|PDB:3NCY"
FT HELIX 407..425
FT /evidence="ECO:0007829|PDB:3NCY"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:3NCY"
SQ SEQUENCE 445 AA; 46933 MW; A187BA326CB6FA97 CRC64;
MSSDADAHKV GLIPVTLMVS GNIMGSGVFL LPANLAATGG IAIYGWLVTI IGALALSMVY
AKMSSLDPSP GGSYAYARRC FGPFLGYQTN VLYWLACWIG NIAMVVIGVG YLSYFFPILK
DPLVLTLTCV AVLWIFVLLN IVGPKMITRV QAVATVLALV PIVGIAVFGW FWFKGETYMA
AWNVSGMNTF GAIQSTLNVT LWSFIGVESA SVAAGVVKNP KRNVPIATIG GVLIAAVCYV
LSTTAIMGMI PNAALRVSAS PFGDAARMAL GDTAGAIVSF CAAAGCLGSL GGWTLLAGQT
AKAAADDGLF PPIFARVNKA GTPVAGLLIV GVLMTIFQFS SMSPNAAKEF GLVSSVSVIF
TLVPYLYTCA ALLLLGHGHF GKARPLYLLI TFVAFVYCIW AVIGSGAKEV MWSFVTLMVI
TALYALNYNR IHKNPYPLDA PVKQD
