AAXC_CHLT2
ID AAXC_CHLT2 Reviewed; 483 AA.
AC B0B7U3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Arginine/agmatine antiporter;
GN Name=aaxC; Synonyms=arcD; OrderedLocusNames=CTL0628;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
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; AM884176; CAP04069.1; -; Genomic_DNA.
DR RefSeq; WP_009873766.1; NC_010287.1.
DR RefSeq; YP_001654702.1; NC_010287.1.
DR AlphaFoldDB; B0B7U3; -.
DR SMR; B0B7U3; -.
DR EnsemblBacteria; CAP04069; CAP04069; CTL0628.
DR KEGG; ctb:CTL0628; -.
DR PATRIC; fig|471472.4.peg.679; -.
DR HOGENOM; CLU_007946_1_2_0; -.
DR OMA; FNSDNRV; -.
DR Proteomes; UP000000795; 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_5000300957"
FT TRANSMEM 11..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..178
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 293..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..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 458..477
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 483 AA; 52662 MW; 96B39D99BE8590A0 CRC64;
MLLKKRSPTS ILGTLALTGI VISYMIGGGI FSLPQNMAAS ASAGAVMLAW MLSGIGIFFI
ANTFKTLSII RPDLKAGIYT YSREGFGPYV GFTIAWGYWL CQIFGNVGYA VITMDALNYF
FPPYFAGGNT IPAILLGSLL IWIFNYIVLR GIRQASFVNI IGVVCTLIPL LLFILITARF
FKFSIFKTDF WGTAPQHTLG SIGSQLKSTM LVTLWAFIGI EGAVVISGRA ANPSSVGKAT
ILGFSGCLLI YVLLSLLPFG SLFQYQLAKI ADPSTAGVLN ILVGKWGEVL MNTGLLIAVL
TSWLSWTILA SEIPYAAAKN GTFPECFAIE NSKHAPSFSL FMTSGLMQIT MLLVYFSSNA
WNTMLEITGV MVLPAYLTSS LFLVKFSLSK KYPKQAAIKA RIAMITGLLG SLYSLWLIYA
GGLQHLFMVA ILLALGIPFY VDSGIRHKQE KTFLNRKEIL KMTIMALAAL LAIFLFSANK
IHL