ID   OMP1_ACTPL              Reviewed;          21 AA.
AC   P80368;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=40 kDa major outer membrane protein;
DE            Short=MOMP;
DE   Flags: Fragment;
OS   Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=715;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=598;
RX   PubMed=7483902; DOI=10.1111/j.1439-0450.1995.tb00682.x;
RA   Hartmann L., Schroeder W., Luebke-Becker A.;
RT   "Isolation of the major outer-membrane protein of Actinobacillus
RT   pleuropneumoniae and Haemophilus parasuis.";
RL   J. Vet. Med. B 42:59-63(1995).
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.
CC   -!- SUBUNIT: Disulfide bond interactions within and between MOMP molecules
CC       and other components form high molecular-weight oligomers.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
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DR   AlphaFoldDB; P80368; -.
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="40 kDa major outer membrane protein"
FT                   /id="PRO_0000198026"
FT   NON_TER         21
SQ   SEQUENCE   21 AA;  2293 MW;  FFE7D12EA916563B CRC64;
     VTVYDAEGTK VQIDGSLRVE L