ID   OMP1_ACTSU              Reviewed;          21 AA.
AC   P80442;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Major outer membrane protein;
DE            Short=MOMP;
DE   Flags: Fragment;
OS   Actinobacillus suis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=716 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   STRAIN=S 76 H2 {ECO:0000269|PubMed:8837386};
RX   PubMed=8837386; DOI=10.1016/s0934-8840(96)80101-0;
RA   Hartmann L., Schroeder W., Luebke-Becker A.;
RT   "Serological and biochemical properties of the major outer membrane protein
RT   within strains of the genus Actinobacillus.";
RL   Zentralbl. Bakteriol. 284:255-262(1996).
CC   -!- FUNCTION: Structural rigidity of the outer membrane of elementary
CC       bodies and porin forming, permitting diffusion of solutes through the
CC       intracellular reticulate body membrane. {ECO:0000250|UniProtKB:P80368}.
CC   -!- SUBUNIT: Disulfide bond interactions within and between MOMP molecules
CC       and other components form high molecular-weight oligomers.
CC       {ECO:0000250|UniProtKB:P80368}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:8837386};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:8837386}.
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DR   AlphaFoldDB; P80442; -.
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.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Direct protein sequencing; Disulfide bond;
KW   Ion transport; Membrane; Porin; Transmembrane; Transmembrane beta strand;
KW   Transport.
FT   CHAIN           1..>21
FT                   /note="Major outer membrane protein"
FT                   /id="PRO_0000198025"
FT   NON_TER         21
FT                   /evidence="ECO:0000303|PubMed:8837386"
SQ   SEQUENCE   21 AA;  2279 MW;  EB6D14CEA916563B CRC64;
     VTVYDAEGTK VQVDGSLRLV E