AAXC_CHLFF
ID AAXC_CHLFF Reviewed; 486 AA.
AC Q255I1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Arginine/agmatine antiporter;
GN Name=aaxC; Synonyms=arcD; OrderedLocusNames=CF0285;
OS Chlamydia felis (strain Fe/C-56) (Chlamydophila felis).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=264202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fe/C-56;
RX PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H.,
RA Hattori M., Kuhara S., Shirai M.;
RT "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL DNA Res. 13:15-23(2006).
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; AP006861; BAE81057.1; -; Genomic_DNA.
DR RefSeq; WP_011457838.1; NC_007899.1.
DR AlphaFoldDB; Q255I1; -.
DR SMR; Q255I1; -.
DR STRING; 264202.CF0285; -.
DR KEGG; cfe:CF0285; -.
DR eggNOG; COG0531; Bacteria.
DR HOGENOM; CLU_007946_1_2_0; -.
DR OMA; FNSDNRV; -.
DR OrthoDB; 527053at2; -.
DR Proteomes; UP000001260; 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_0000363175"
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 161..181
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; 52702 MW; EC06E8FEBC88F888 CRC64;
MISNGSKTRK NLGAIALAGM VISSMIGGGI FSLPQNMAAS AGAGAIILAW ILTGIGMFFI
ANTFKILSLV RPDLTTGIYM YSREGFGPYV GFTIGWGYWL CQIFGNVGYA VMTMDALNYF
FPPYFKGGNT IPAIIGGSIL IWVFNFIVLK GIRQASFINV IGTICKLIPL LIFIIITAFF
FKLAIFKTDF WGHTATKTQP LLGSVTSQLK STMLVTLWAF IGIEGAVVMS ARAKSPNAVG
KATILGFSGC LIVYVLLSLL PFGSLFQHQL AGIANPSTAG VLDILVGRWG EILMNIGLLI
AILSSWLSWT VIVAEIPYSA AKNGTFPEIF TIENAAHSPK VSLYITSALM QVAMLLVYFS
TNAWSTMLSI TGVMVLPAYL ASAAFLVKFS KDKKYPNKGP IKSFTAKYTG ILAVIYSIWL
IYAGGIKYLF MAIVLLALGI PFYIEAGKKG KNAKTFFAKK EVTKITIIAF LALLAIFLFS
TERIRL