OMP2B_BRUA2
ID OMP2B_BRUA2 Reviewed; 362 AA.
AC Q2YMY7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Porin Omp2b;
DE Flags: Precursor;
GN Name=omp2b; OrderedLocusNames=BAB1_0660;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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 {ECO:0000250}; Multi-pass
CC membrane protein {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=CAJ10616.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM040264; CAJ10616.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002971512.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YMY7; -.
DR SMR; Q2YMY7; -.
DR STRING; 359391.BAB1_0660; -.
DR EnsemblBacteria; CAJ10616; CAJ10616; BAB1_0660.
DR GeneID; 3788833; -.
DR KEGG; bmf:BAB1_0660; -.
DR PATRIC; fig|359391.11.peg.2974; -.
DR HOGENOM; CLU_044836_0_0_5; -.
DR PhylomeDB; Q2YMY7; -.
DR Proteomes; UP000002719; 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; Reference proteome;
KW Signal; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..362
FT /note="Porin Omp2b"
FT /id="PRO_0000354008"
SQ SEQUENCE 362 AA; 38723 MW; E4738BF34DB8615C CRC64;
MNIKSLLLGS AAALVAASGA QAADAIVAPE PEAVEYVRVC DAYGAGYFYI PGTETCLRVH
GYVRYDVKGG DDVYSGTDRN 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