ID   AAXC_CHLMU              Reviewed;         483 AA.
AC   Q9PK20;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Arginine/agmatine antiporter;
GN   Name=aaxC; Synonyms=arcD; OrderedLocusNames=TC_0653;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF73583.1; -; Genomic_DNA.
DR   RefSeq; WP_010231123.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PK20; -.
DR   SMR; Q9PK20; -.
DR   STRING; 243161.TC_0653; -.
DR   EnsemblBacteria; AAF73583; AAF73583; TC_0653.
DR   GeneID; 1246014; -.
DR   KEGG; cmu:TC_0653; -.
DR   eggNOG; COG0531; Bacteria.
DR   HOGENOM; CLU_007946_1_2_0; -.
DR   OMA; FNSDNRV; -.
DR   OrthoDB; 527053at2; -.
DR   Proteomes; UP000000800; 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..483
FT                   /note="Arginine/agmatine antiporter"
FT                   /id="PRO_0000363176"
FT   TRANSMEM        9..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        295..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        367..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        462..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   483 AA;  52591 MW;  EE1688604AB6275B CRC64;
     MFLKKRSSSG ILGTLSLTGV VISSMVGGGI FSLPQNMAAS ASAGAIIIAW LLSGIGIFFI
     ANTFKTLSLV RPDLKAGIYT YSREGFGPYV GFTIAWGYWL CQIFGNVGYA VITMDALNYF
     FPPYFEGGNT LPAILLGSIL IWVFNSIVLR GIRQAAFMNV IGVIFTLIPL LIFILITALF
     FKFSIFKTDF WGTAPQHHLG SIGSQLKSTM LVTLWAFIGI EGAVVMSGRA SNPSSVGKAT
     ILGFSGCLLI YVLLSLLPFG SLSQYQLAKI ADPSTAGVLK FLVGKWGEVL MNTGLLIAVL
     TSWLSWTILT AEIPYAAAKN GTFPECFAIE NAKHSPAFSL FITSGLMQIT MLLVYFSSNA
     WHTMLEITSV MVLPAYLTSS LFLVKLSLSK KYPKQAPIKA RVAIFTGILG TLYSLWLIYA
     GGLQHLFMVA VLLALGIPFY IDSGIRHDQE KTFLNRKEVM KMTTLALIAL LAVFLFSANK
     IHL