AAXC_CHLAB
ID AAXC_CHLAB Reviewed; 486 AA.
AC Q5L5E6;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Arginine/agmatine antiporter;
GN Name=aaxC; Synonyms=arcD; OrderedLocusNames=CAB698;
OS Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=218497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27085 / S26/3;
RX PubMed=15837807; DOI=10.1101/gr.3684805;
RA Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT "The Chlamydophila abortus genome sequence reveals an array of variable
RT proteins that contribute to interspecies variation.";
RL Genome Res. 15:629-640(2005).
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; CR848038; CAH64145.1; -; Genomic_DNA.
DR RefSeq; WP_011097273.1; NC_004552.2.
DR AlphaFoldDB; Q5L5E6; -.
DR SMR; Q5L5E6; -.
DR EnsemblBacteria; CAH64145; CAH64145; CAB698.
DR KEGG; cab:CAB698; -.
DR eggNOG; COG0531; Bacteria.
DR HOGENOM; CLU_007946_1_2_0; -.
DR OMA; FNSDNRV; -.
DR OrthoDB; 527053at2; -.
DR Proteomes; UP000001012; 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_0000363173"
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 132..152
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; 52473 MW; F894749325E2D431 CRC64;
MISNGSKSGK NLGAIALAGM VISSMIGGGI FSLPQNMAAS AGVGAIILAW ILTGVGMFFI
ANTFKILSLV RPDLTTGIYM YSREGFGPYI GFTIGWGYWL CQIFGNVGYA VMTMDALNYF
FPPYFQGGNT LPAILGGSIL IWVFNFIVLK GIRQASFINI IGTVGKLVPL IVFIIITAFL
FKLAIFKTDF WGDTVTKTQP LLGSMTSQLK STMLVTLWAF IGIEGAVVMS ARAKSPSAVG
KATILGFTGC LTVYILLSIL PFGSLFQHQL AGIANPSTAG VLDILVGKWG EILMNVGLLI
AVLSSWLSWT MIVAEIPYSA AKNGTFPEIF AIENAHRSPK VSLYVTSALM QIAMLLVYFS
TDAWNTMLSI TGVMVLPAYF ASAAFLVKFS KNKKYPNKGP IKAFTAKITG LLGAVYSIWL
IYAGGLKYLL MAIILLALGI PFYIDAGKKG RNAKTFFAKK EVTEITIIAF LALLAIFLFS
TEKIRL