AAXC_CHLCV
ID AAXC_CHLCV Reviewed; 486 AA.
AC Q822F2;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Arginine/agmatine antiporter;
GN Name=aaxC; Synonyms=arcD; OrderedLocusNames=CCA_00731;
OS Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS (Chlamydophila caviae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=227941;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX PubMed=12682364; DOI=10.1093/nar/gkg321;
RA Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA Fraser C.M.;
RT "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT examining the role of niche-specific genes in the evolution of the
RT Chlamydiaceae.";
RL Nucleic Acids Res. 31:2134-2147(2003).
CC -!- FUNCTION: Catalyzes the exchange of L-arginine for agmatine. The
CC arginine uptake by the bacterium in the macrophage may be a virulence
CC factor against the host innate immune response (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
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; AE015925; AAP05472.1; -; Genomic_DNA.
DR RefSeq; WP_011006686.1; NC_003361.3.
DR AlphaFoldDB; Q822F2; -.
DR SMR; Q822F2; -.
DR STRING; 227941.CCA_00731; -.
DR EnsemblBacteria; AAP05472; AAP05472; CCA_00731.
DR KEGG; cca:CCA_00731; -.
DR eggNOG; COG0531; Bacteria.
DR HOGENOM; CLU_007946_1_2_0; -.
DR OMA; FNSDNRV; -.
DR OrthoDB; 527053at2; -.
DR Proteomes; UP000002193; 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 InterPro; IPR004754; Amino_acid_antiprt.
DR Pfam; PF13520; AA_permease_2; 1.
DR TIGRFAMs; TIGR00905; 2A0302; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Antiport; Cell inner membrane; Cell membrane;
KW Membrane; Transmembrane; Transmembrane helix; Transport; Virulence.
FT CHAIN 1..486
FT /note="Arginine/agmatine antiporter"
FT /id="PRO_0000363174"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 486 AA; 52914 MW; EAFEAC796A789A1F CRC64;
MFLNRGKSKK NLGAIALAGM VISSMIGGGI FSLPQNMAAS AGAGAIILAW LLTGIGMFFI
ANTFKILSLV RPDLTTGIYM YSREGFGPYV GFTIGWGYWL CQIFGNVGYA VMTMDALNYF
FPPYFKGGNT IPAIIGGSIL IWVFNFIVLK GIRQASFINI IGTVCKLVPL IVFIIITAFA
FKLAIFKTDF WGDAVTKTQP ALGSVTSQLK STMLVTLWAF IGIEGAVVMS ARAKSPSAVG
KATLLGFVGC LTVYILLSIL PFGSLFQYQL AGIPNPSTAG VLGMLVGRWG EILMNVGLLI
AILSSWLSWT IIVAEIPYTA ATNGTFPEIF AIENAQHSPK LSLYITSALM QITMLFVYFS
TNAWNTMLSI TGVMVLPAYL ASAAFLFQFS KNKKYPNKGP VKSYIAKYTG FFAVIYSLWL
IYAGGLNYLL MSVILLALGI PFYIDAGKKS KREKTFFAKK EVTKIIIIAL LALLAIFLFS
TEKIRL