ID   AAXA_CHLMU              Reviewed;         461 AA.
AC   Q9PK22;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Porin AaxA;
DE   AltName: Full=Outer membrane protein AaxA;
DE   Flags: Precursor;
GN   Name=aaxA; OrderedLocusNames=TC_0651;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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=AAF39477.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE002160; AAF39477.1; ALT_INIT; Genomic_DNA.
DR   PIR; A81680; A81680.
DR   AlphaFoldDB; Q9PK22; -.
DR   SMR; Q9PK22; -.
DR   STRING; 243161.TC_0651; -.
DR   EnsemblBacteria; AAF39477; AAF39477; TC_0651.
DR   KEGG; cmu:TC_0651; -.
DR   eggNOG; COG3659; Bacteria.
DR   HOGENOM; CLU_619231_0_0_0; -.
DR   Proteomes; UP000000800; 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_0000363183"
SQ   SEQUENCE   461 AA;  51520 MW;  073119CEFE039AAD CRC64;
     MSFRSILLTA LLSLSFTNTM QAAHHHYHRY DDKLRRQYHK KDLPTQENVR KEFCNPYSHS
     SDPIPLSQQR GVLSPICDLV SECSFLNGIS VRSLKQTLKN SAGTQVALDW SILPQWFNPR
     SSWAPKLSIR DLGYGKPQSL IEADSPCCQT CFNPSAAITI YDSSCGKGVV QVSYTLVRYW
     RETAALAGQT MMLAGSINDY PARQNIFSQL TFSQTFPNER VNLTVGQYSL YSIDGTLYNN
     DQQLGFISYA LSQNPTATYS SGSLGAYLQV APTESTCLQV GFQDAYNISG SSIKWNNLTK
     NKYNFHGYAS WAPHCCLGPG QYSVLLYVTR KVPEQMMQTM GWSVNASQYI SSKLYVFGRY
     SGVTGQLSPI NRTYSFGLVS PNLLNRNPQD LFGVACAFNN IHASAFQNAQ RKYETVIEGF
     ATIGCGPYIS FAPDFQLYLY PALRPNKQSA RVYSVRANLA I