AAXC_CHLTR
ID AAXC_CHLTR Reviewed; 483 AA.
AC O84379;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Arginine/agmatine antiporter;
GN Name=aaxC; Synonyms=arcD; OrderedLocusNames=CT_374;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC67970.1; -; Genomic_DNA.
DR PIR; G71523; G71523.
DR RefSeq; NP_219883.1; NC_000117.1.
DR RefSeq; WP_009873122.1; NC_000117.1.
DR AlphaFoldDB; O84379; -.
DR SMR; O84379; -.
DR STRING; 813.O172_02045; -.
DR EnsemblBacteria; AAC67970; AAC67970; CT_374.
DR GeneID; 884744; -.
DR KEGG; ctr:CT_374; -.
DR PATRIC; fig|272561.5.peg.403; -.
DR HOGENOM; CLU_007946_1_2_0; -.
DR InParanoid; O84379; -.
DR OMA; FNSDNRV; -.
DR Proteomes; UP000000431; 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; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Virulence.
FT CHAIN 1..483
FT /note="Arginine/agmatine antiporter"
FT /id="PRO_0000363178"
FT TRANSMEM 9..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..107
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; 52658 MW; DAC657500A1A8A69 CRC64;
MLLKKRSPTS ILGTLALTGI VISSMIGGGI FSLPQNMVAS ASAGAVMLAW MLSGIGIFFI
ANTFKTLSII RPDLKAGIYT YSREGFGPYV GFTIAWGYWL CQIFGNVDYA VITMDALNYF
FPPYFAGGNT IPAILLGSLL IWIFNYIVLR GIRQASFVNI IGAVCTLIPL LLFILITARF
FKFSIFKTDF WGTAPQHTLG SIGSQLKSTM LVTLWAFIGI EGAVVISGRA ANLSSVGKAT
ILGFSGCLLI YVLLSLLPFG SLFQYQLAKI ADPSTAGVLN ILVGKWGEVL MNTGLLIAVL
TSWLSWTILA SEIPYAAAKN GTFPECFAIE NSKHAPSFSL FMTSGLMQIT MLLVYFSSNA
WNTMLEITGV MVLPAYLTSS LFLVKFSLSK KYPKQAAIKA RIAMITSLLG SLYSLWLIYA
GGLQHLFMVA ILLALGIPFY VDSGIRHKQE KTFLNRKEIL KMTIVALAAL LAIFLFSANK
IHL