AAXA_CHLCV
ID AAXA_CHLCV Reviewed; 451 AA.
AC Q822F4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Porin AaxA;
DE AltName: Full=Outer membrane protein AaxA;
DE Flags: Precursor;
GN Name=aaxA; OrderedLocusNames=CCA_00729;
OS Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS (Chlamydophila caviae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=227941;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX PubMed=12682364; DOI=10.1093/nar/gkg321;
RA Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA Fraser C.M.;
RT "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT examining the role of niche-specific genes in the evolution of the
RT Chlamydiaceae.";
RL Nucleic Acids Res. 31:2134-2147(2003).
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; AE015925; AAP05470.1; -; Genomic_DNA.
DR RefSeq; WP_011006684.1; NC_003361.3.
DR AlphaFoldDB; Q822F4; -.
DR STRING; 227941.CCA_00729; -.
DR EnsemblBacteria; AAP05470; AAP05470; CCA_00729.
DR KEGG; cca:CCA_00729; -.
DR eggNOG; COG3659; Bacteria.
DR HOGENOM; CLU_619231_0_0_0; -.
DR OMA; SQTFPGD; -.
DR OrthoDB; 338964at2; -.
DR Proteomes; UP000002193; 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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..451
FT /note="Porin AaxA"
FT /id="PRO_0000363182"
SQ SEQUENCE 451 AA; 50305 MW; 0A86B8C863EE2D14 CRC64;
MASFHSSLLT ALCTLCTYGI LTMPAYGLDP NHPKHHYHKY SERLKRSNAE DSAFYLSSAS
ESSEDLRQEP RRHILTPVRN VLKDDPCDEG LSISKLLHSI EKETNSQISV DFTILPQWFY
PKKSALATSE EKQPTWQFYV SPNISWQLYN SPTAGVGSID FSYTLIRYWN NSAQNANNAI
GIAGEINDYS SRTNTLSLLT FSQTFPGEML TVSFGQYSLY SIDGTLYDND QQCGFLSYAL
SQNASATYSS GSVGAYVQFT PIPSINIQAG FQDAYSIVGS SFDVYNLTKN RYNFYGYFSW
APQSCLGAGQ YSALIYSTRN VPQQPVQTTG WSLNFGQYLG EKLYVFGRWN GSTGTAVNLN
RSHVLGLASA NPINRNPKDL LGAACSMSKV NPKVVTDKKI RKYETVIETF ATVGFGPHLS
LSPDLQVYIH PARRPDRRSA TVYSIRANFF V