ADIC_YERPE
ID ADIC_YERPE Reviewed; 444 AA.
AC Q8ZGS9; Q0WHK2;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Arginine/agmatine antiporter;
GN Name=adiC; OrderedLocusNames=YPO1200, y2988, YP_0937;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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; AL590842; CAL19863.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM86539.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS61192.1; -; Genomic_DNA.
DR PIR; AE0147; AE0147.
DR RefSeq; WP_002210804.1; NZ_WUCM01000017.1.
DR RefSeq; YP_002346236.1; NC_003143.1.
DR AlphaFoldDB; Q8ZGS9; -.
DR SMR; Q8ZGS9; -.
DR STRING; 214092.YPO1200; -.
DR PaxDb; Q8ZGS9; -.
DR DNASU; 1147935; -.
DR EnsemblBacteria; AAM86539; AAM86539; y2988.
DR EnsemblBacteria; AAS61192; AAS61192; YP_0937.
DR GeneID; 57977340; -.
DR KEGG; ype:YPO1200; -.
DR KEGG; ypk:y2988; -.
DR KEGG; ypm:YP_0937; -.
DR PATRIC; fig|214092.21.peg.1502; -.
DR eggNOG; COG0531; Bacteria.
DR HOGENOM; CLU_007946_1_0_6; -.
DR OMA; YDGWILI; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..444
FT /note="Arginine/agmatine antiporter"
FT /id="PRO_0000054236"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 21
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 21
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 24
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 94
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 94
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 95
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 99
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 200
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 203
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 203
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 291
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT BINDING 355
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT SITE 91
FT /note="Cytoplasmic (distal) gate"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT SITE 200
FT /note="Periplasmic (proximal) gate"
FT /evidence="ECO:0000250|UniProtKB:P60063"
FT SITE 206
FT /note="Cytoplasmic (distal) gate"
FT /evidence="ECO:0000250|UniProtKB:P60061"
FT SITE 291
FT /note="Middle gate"
FT /evidence="ECO:0000250|UniProtKB:P60063"
FT SITE 363
FT /note="Cytoplasmic (distal) gate"
FT /evidence="ECO:0000250|UniProtKB:P60061"
SQ SEQUENCE 444 AA; 46639 MW; 359438CC2039BADB CRC64;
MSTDDQKVGL IPVTLMVAGN IMGSGVFLLP ANLASTGGIA IWGWLVTIIG ALALSMVYAK
ISSLDDSPGG SYAYARRAFG PFLGYQTNVL YWLACWIGNI AMVVIGVGYL SYFFPILKEP
MVLTITCVVF LWIFVGLNII GPKMITRVQA VATSLALIPI VGIALFGWFW FKGETYMAAW
NVSGLGTFGA IQSTLNVTLW SFIGVETASV AAGVVKNPKR NVPIATVGGV LIAAVCYVLS
SSAIMGMIPN AELRLSASPF GDAARLALGD TAGAVVSLCA AAGCLGSLGG WTLVAGQTAK
AAADDGLFPP IFGKVNKAGT PVAGLLILGV LMTIFQISSI SPNAAKEFGL VSSVSVIFTL
VPYLYTCSAL LLVGHGHLGN QVKTYVGITL IAFVYCIWAV VGSGAEEVMW SFVTLMVITA
LYTFNYNRTH KNPFPLDAPV KNGQ
