OMP2A_BRUSS
ID OMP2A_BRUSS Reviewed; 367 AA.
AC P0DI94; Q45429; Q7CEH9; Q9EY45;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Porin Omp2a;
DE Flags: Precursor;
GN Name=omp2a;
OS Brucella suis.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=29461;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=83-210;
RX PubMed=11466287; DOI=10.1128/jb.183.16.4839-4847.2001;
RA Paquet J.-Y., Diaz M.A., Genevrois S., Grayon M., Verger J.-M.,
RA de Bolle X., Lakey J.H., Letesson J.-J., Cloeckaert A.;
RT "Molecular, antigenic, and functional analyses of Omp2b porin size variants
RT of Brucella spp.";
RL J. Bacteriol. 183:4839-4847(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=8035;
RA Scholz H.C., Hubalek Z., Sedlacek I., Vergnaud G., Tomaso H., Al Dahouk S.,
RA Melzer F., Kampfer P., Neubauer H., Cloeckaert A., Maquart M.,
RA Zygmunt M.S., Whatmore A.M., Falsen E., Bahn P., Gollner C., Pfeffer M.,
RA Huber B., Busse H.J., Nockler K.;
RT "Brucella microti sp. nov., isolated from the common vole Microtus
RT arvalis.";
RL Int. J. Syst. Evol. Microbiol. 58:375-382(2008).
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; AY008721; AAG38245.1; -; Genomic_DNA.
DR EMBL; AM712079; CAM98689.1; -; Genomic_DNA.
DR RefSeq; WP_006190002.1; NZ_UFTY01000001.1.
DR AlphaFoldDB; P0DI94; -.
DR GeneID; 45051723; -.
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_0000412628"
FT VARIANT 59..60
FT /note="VH -> IS (in strain: 83-210)"
FT VARIANT 130..131
FT /note="DR -> SV (in strain: 83-210)"
FT VARIANT 139
FT /note="S -> N (in strain: 83-210)"
FT VARIANT 241
FT /note="A -> V (in strain: 83-210)"
FT VARIANT 246
FT /note="P -> S (in strain: 83-210)"
FT VARIANT 304
FT /note="V -> A (in strain: 83-210)"
SQ SEQUENCE 367 AA; 39506 MW; 527F511E85531568 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
TEKVTFNLQA AHDDWGKTAV TANVAYQLVP GFTITPEVSY TKFGGEWKDT VAEDNAWGGI
VRFQRSF