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AAXA_CHLT2
ID   AAXA_CHLT2              Reviewed;         461 AA.
AC   B0B7U1;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Porin AaxA;
DE   AltName: Full=Outer membrane protein AaxA;
DE   Flags: Precursor;
GN   Name=aaxA; OrderedLocusNames=CTL0626;
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: Facilitates L-arginine uptake, as part of the AaxABC system.
CC       The arginine uptake by the bacterium in the macrophage may be a
CC       virulence factor against the host innate immune response (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the OprB family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAP04067.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM884176; CAP04067.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_001654701.1; NC_010287.1.
DR   AlphaFoldDB; B0B7U1; -.
DR   EnsemblBacteria; CAP04067; CAP04067; CTL0626.
DR   KEGG; ctb:CTL0626; -.
DR   PATRIC; fig|471472.4.peg.675; -.
DR   HOGENOM; CLU_619231_0_0_0; -.
DR   Proteomes; UP000000795; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR   GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:InterPro.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.160.180; -; 1.
DR   InterPro; IPR007049; Carb-sel_porin_OprB.
DR   InterPro; IPR038673; OprB_sf.
DR   Pfam; PF04966; OprB; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Cell outer membrane; Ion transport; Membrane; Porin;
KW   Signal; Transmembrane; Transmembrane beta strand; Transport; Virulence.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..461
FT                   /note="Porin AaxA"
FT                   /id="PRO_0000363186"
SQ   SEQUENCE   461 AA;  51517 MW;  9CAF5F90F41780E6 CRC64;
     MSFRSVLLTA LLSLSFTTTM QAAHHHYHRY TDKLHRQNHK KDLISPKPTE QEACNTPSLS
     KELIPLSEQR GLLSPIYDFI SERLCLHGVS VRNLKQALKN SAGTQIALDW SILPQWFNPR
     VSHAPKLSIR DFGYSAHQTV TEATPPCWQN CFNPSAAVTI YDSSYGKGVF QISYTLVHYW
     RENAATAGDA MMLAGSINDY PSRQNIFSQF TFSQNFPNER VSLTIGQYSL YAIDGTLYNN
     DQQLGFISYA LSQNPTATYS SGSLGAYLQV APTASTSLQI GFQDAYNISG SSIKWSNLTK
     NRYNFHGFAS WAPRCCLGSG QYSVLLYVTR QVPEQMEQTM GWSVNASQYI SSKLYVFGRY
     SGVTGHVFPI NRTYSCGMVS ANLFNRNPQD LFGIACAFNN VHLSASPNAK RKYETVIEGF
     ATIGCGPYLS FAPDFQLYLY PALRPNKQSA RVYSVRANLA I
 
 
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