ID   OMP2A_BRUC2             Reviewed;         367 AA.
AC   A9MA14;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Porin Omp2a;
DE   Flags: Precursor;
GN   Name=omp2a; OrderedLocusNames=BCAN_A0651;
OS   Brucella canis (strain ATCC 23365 / NCTC 10854).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=483179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23365 / NCTC 10854;
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA   Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA   Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA   Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA   Bruce D., Detter C., Munk C., Brettin T.S.;
RT   "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms passive diffusion pores that allow small molecular
CC       weight hydrophilic materials across the outer membrane.
CC       {ECO:0000250|UniProtKB:B2SAB9}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:B2SAB9}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000250|UniProtKB:B2SAB9}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:B2SAB9}.
CC   -!- DOMAIN: Consists of 16-stranded beta-barrel sheets, with large surface-
CC       exposed loops, that form a transmembrane pore at the center of each
CC       barrel. The pore is partially ocluded by a peptide loop that folds into
CC       the pore lumen. {ECO:0000250|UniProtKB:B2SAB9}.
CC   -!- MISCELLANEOUS: The pore formed by Omp2a is larger than the one formed
CC       by Omp2b. Omp2b pores have optimal permeability to allow growth and
CC       protection against harmful compounds. The larger pore formed by Omp2a
CC       may be advantageous for intracellular growth, when the bacterium is
CC       competing with the host cell for nutrients whose concentration is
CC       particularly low within the phagosome. {ECO:0000250|UniProtKB:B2SAB9}.
CC   -!- SIMILARITY: Belongs to the alphaproteobacteria porin family.
CC       {ECO:0000305}.
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DR   EMBL; CP000872; ABX61726.1; -; Genomic_DNA.
DR   RefSeq; WP_006132438.1; NC_010103.1.
DR   AlphaFoldDB; A9MA14; -.
DR   SMR; A9MA14; -.
DR   EnsemblBacteria; ABX61726; ABX61726; BCAN_A0651.
DR   GeneID; 55590366; -.
DR   KEGG; bcs:BCAN_A0651; -.
DR   HOGENOM; CLU_044836_0_0_5; -.
DR   OMA; NMRFTLR; -.
DR   PhylomeDB; A9MA14; -.
DR   Proteomes; UP000001385; Chromosome I.
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:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003684; Porin_alphabac.
DR   Pfam; PF02530; Porin_2; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Ion transport; Membrane; Porin; Signal; Transmembrane;
KW   Transmembrane beta strand; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..367
FT                   /note="Porin Omp2a"
FT                   /id="PRO_0000354009"
SQ   SEQUENCE   367 AA;  39478 MW;  4D6F4E119553157F CRC64;
     MNIKSLLLGS AAALVAASGA QAADAIVAPE PEAVEYVRVC DAYGAGYFYI PGTETCLRVH
     GYVRYDVKGG DDVYTGSDRK GWDKGARFAL MFNTNSETEL GTLGTYTQLR FNYTSNNSRH
     DGQYGDFSDD RDVADGGVST GTDLQFAYIT LGGFKVGIDE SEFHTFTGYL GDVINDDVVA
     AGSYRTGKIA YTFTGGNGFS AVIALEQGGE DVDNDYTIDG YMPHVVGGLK YAGGWGSIAG
     AVAYDPVIEE WATKVRGDVN ITDRFSVWLQ GAYSSAATPN QNYGQWGGDW AVWGGAKFIA
     TEKATFNLQA AHDDWGKTAV TANVAYQLVP GFTITPEVSY TKFGGEWKDT VAEDNAWGGI
     VRFQRSF