OMP2A_BRUA1
ID OMP2A_BRUA1 Reviewed; 321 AA.
AC B2SAB9; Q44667; Q57EA4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Porin Omp2a;
DE Flags: Precursor;
GN Name=omp2a; OrderedLocusNames=BAbS19_I06180;
OS Brucella abortus (strain S19).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=430066;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND EXPRESSION.
RX PubMed=2509359; DOI=10.1128/iai.57.11.3281-3291.1989;
RA Ficht T.A., Bearden S.W., Sowa B.A., Adams L.G.;
RT "DNA sequence and expression of the 36-kilodalton outer membrane protein
RT gene of Brucella abortus.";
RL Infect. Immun. 57:3281-3291(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S19;
RX PubMed=18478107; DOI=10.1371/journal.pone.0002193;
RA Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S.,
RA Bricker B., Yu G., Du L., Sobral B.W.;
RT "Genome sequence of Brucella abortus vaccine strain S19 compared to
RT virulent strains yields candidate virulence genes.";
RL PLoS ONE 3:E2193-E2193(2008).
RN [3]
RP FUNCTION AS PORIN, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=7689540; DOI=10.1128/iai.61.9.3785-3790.1993;
RA Marquis H., Ficht T.A.;
RT "The omp2 gene locus of Brucella abortus encodes two homologous outer
RT membrane proteins with properties characteristic of bacterial porins.";
RL Infect. Immun. 61:3785-3790(1993).
RN [4]
RP DOMAIN, AND TOPOLOGY MODEL.
RX PubMed=9345760; DOI=10.1111/j.1574-6968.1997.tb12681.x;
RA Mobasheri H., Ficht T.A., Marquis H., Lea E.J.A., Lakey J.H.;
RT "Brucella Omp2a and Omp2b porins: single channel measurements and topology
RT prediction.";
RL FEMS Microbiol. Lett. 155:23-30(1997).
RN [5]
RP DOMAIN, AND TOPOLOGY MODEL.
RX PubMed=10698111; DOI=10.1080/07391102.2000.10506564;
RA Paquet J.-Y., Vinals C., Wouters J., Letesson J.-J., Depiereux E.;
RT "Topology prediction of Brucella abortus Omp2b and Omp2a porins after
RT critical assessment of transmembrane beta strands prediction by several
RT secondary structure prediction methods.";
RL J. Biomol. Struct. Dyn. 17:747-757(2000).
CC -!- FUNCTION: Forms passive diffusion pores that allow small molecular
CC weight hydrophilic materials across the outer membrane.
CC {ECO:0000269|PubMed:7689540}.
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:7689540}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:7689540};
CC Multi-pass membrane protein {ECO:0000269|PubMed:7689540}.
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:0000269|PubMed:10698111,
CC ECO:0000269|PubMed:9345760}.
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:0000305|PubMed:9345760}.
CC -!- SIMILARITY: Belongs to the alphaproteobacteria porin family.
CC {ECO:0000305}.
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DR EMBL; M26034; AAA83993.1; -; Genomic_DNA.
DR EMBL; CP000887; ACD72149.1; -; Genomic_DNA.
DR RefSeq; WP_002969883.1; NC_010742.1.
DR AlphaFoldDB; B2SAB9; -.
DR EnsemblBacteria; ACD72149; ACD72149; BAbS19_I06180.
DR GeneID; 3787381; -.
DR KEGG; bmc:BAbS19_I06180; -.
DR HOGENOM; CLU_044836_0_0_5; -.
DR OMA; NMRFTLR; -.
DR Proteomes; UP000002565; Chromosome 1.
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 1: Evidence at protein level;
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..321
FT /note="Porin Omp2a"
FT /id="PRO_0000354005"
SQ SEQUENCE 321 AA; 34535 MW; 255D624AB464A4A7 CRC64;
MNIKSLLLGS AAALVAASGA QAADAIVAPE PEAVEYVRVC DAYGAGYFYI PGTETCLRVH
GYVRYDVKGG DDVYSGTDRN GWDKGARFAL MFNTNSETEL GTLGTYTQLR FNYTSNNSRH
DGQYGDFSDD RDVADGGVST GKIAYTFTGG NGFSAVIALE QGGEDVDNDY TIDGYMPHVV
GGLKYAGGWG SIAGVVAYDS VIEEWATKVR GDVNITDRFS VWLQGAYSSA ATPNQNYGQW
GGDWAVWGGA KFIAPEKATF NLQAAHDDWG KTAVTANVAY QLVPGFTITP EVSYTKFGGE
WKDTVAEDNA WGGIVRFQRS F