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AAXC_CHLTB
ID   AAXC_CHLTB              Reviewed;         483 AA.
AC   B0BC08;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Arginine/agmatine antiporter;
GN   Name=aaxC; Synonyms=arcD; OrderedLocusNames=CTLon_0626;
OS   Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=471473;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCH-1/proctitis;
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; AM884177; CAP07023.1; -; Genomic_DNA.
DR   RefSeq; WP_009873766.1; NC_010280.2.
DR   AlphaFoldDB; B0BC08; -.
DR   SMR; B0BC08; -.
DR   KEGG; ctl:CTLon_0626; -.
DR   HOGENOM; CLU_007946_1_2_0; -.
DR   OMA; FNSDNRV; -.
DR   Proteomes; UP000000794; 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_5000301184"
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
 
 
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