ID   AAXA_CHLAB              Reviewed;         448 AA.
AC   Q5L5E8;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Porin AaxA;
DE   AltName: Full=Outer membrane protein AaxA;
DE   Flags: Precursor;
GN   Name=aaxA; OrderedLocusNames=CAB696;
OS   Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=218497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27085 / S26/3;
RX   PubMed=15837807; DOI=10.1101/gr.3684805;
RA   Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA   Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA   Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA   Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT   "The Chlamydophila abortus genome sequence reveals an array of variable
RT   proteins that contribute to interspecies variation.";
RL   Genome Res. 15:629-640(2005).
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}.
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DR   EMBL; CR848038; CAH64143.1; -; Genomic_DNA.
DR   RefSeq; WP_011097271.1; NC_004552.2.
DR   AlphaFoldDB; Q5L5E8; -.
DR   PRIDE; Q5L5E8; -.
DR   EnsemblBacteria; CAH64143; CAH64143; CAB696.
DR   KEGG; cab:CAB696; -.
DR   eggNOG; COG3659; Bacteria.
DR   HOGENOM; CLU_619231_0_0_0; -.
DR   OMA; SQTFPGD; -.
DR   OrthoDB; 338964at2; -.
DR   Proteomes; UP000001012; 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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..448
FT                   /note="Porin AaxA"
FT                   /id="PRO_0000363181"
SQ   SEQUENCE   448 AA;  50045 MW;  481FDFA99F3A94CD CRC64;
     MASFRSSLLS ALCAYGMMVM PAYAIDPNHP KLHHHKYSER LKKRHTEDSY LSSSSTLESS
     KTFAQEPRRH VLTPIRNVLA DRPCEEGLSI SKLFNSIEKE TNSQISVDFT ILPQWFYPKK
     GLLKAVDEKQ PTWQFYVSPN VSWQLYNSPT AGVGSIDFSY TLVRYWRNNA QNANNAIGIA
     GGINDYSTRT NTLSQLTFSQ TFPENILTIS FGQYSLYSID GTLYDNDQQS GFLSYALSQN
     ASATYSSGSV GAYLQFTPTP SINIQAGFQD AYNVSGSSFD LYNLTRNRYN FYGYVSWAPQ
     SSLGSGQYSA LVYSTRKVPE QPVQTTGWSL NFGQHLGEKL YVFGRWNGAT GTVTNLNRSY
     VLGLASANPI NRNPQDLLGA ACSMSKVNPK VITEKKIRKY ETVIETFATI GFGPHISLTP
     DLQIYIHPAR RPDKRAAKVY GVRANFST