ID   OMP2B_BRUC2             Reviewed;         362 AA.
AC   A9MA15;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Porin Omp2b;
DE   Flags: Precursor;
GN   Name=omp2b; OrderedLocusNames=BCAN_A0653;
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:Q44665}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q44665}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000250|UniProtKB:Q44665}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q44665}.
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:Q44665}.
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:Q44665}.
CC   -!- SIMILARITY: Belongs to the alphaproteobacteria porin family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABX61727.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000872; ABX61727.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_006132439.1; NC_010103.1.
DR   AlphaFoldDB; A9MA15; -.
DR   EnsemblBacteria; ABX61727; ABX61727; BCAN_A0653.
DR   GeneID; 55590368; -.
DR   KEGG; bcs:BCAN_A0653; -.
DR   HOGENOM; CLU_044836_0_0_5; -.
DR   PhylomeDB; A9MA15; -.
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..362
FT                   /note="Porin Omp2b"
FT                   /id="PRO_0000354010"
SQ   SEQUENCE   362 AA;  38737 MW;  3155787BD566DEA6 CRC64;
     MNIKSLLLGS AAALVAASGA QAADAIVAPE PEAVEYVRVC DAYGAGYFYI PGTETCLRVH
     GYVRYDVKGG DDVYTGSDRK GWDKSARFAL RVSTGSETEL GTLKTFTELR FNYAANNSGV
     DGKYGNETSS GTVMEFAYIQ LGGLRVGIDE SEFHTFTGYL GDVINDDVIS AGSYRTGKIS
     YTFTGGNGFS AVIALEQGGD NDGGYTGTTN YHIDGYMPDV VGGLKYAGGW GSIAGVVAYD
     SVIEEWAAKV RGDVNITDQF SVWLQGAYSS AATPDQNYGQ WGGDWAVWGG LKYQATQKAA
     FNLQAAHDDW GKTAVTANVA YELVPGFTVT PEVSYTKFGG EWKNTVAEDN AWGGIVRFQR
     SF