ID   OPAC_NEIGO              Reviewed;         236 AA.
AC   P11296;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Opacity protein opA50;
DE   AltName: Full=V0;
DE   AltName: Full=opA30;
DE   Flags: Precursor; Fragment;
GN   Name=opaC;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=MS11 / V0;
RX   PubMed=3093085; DOI=10.1016/0092-8674(86)90366-1;
RA   Stern A., Brown M., Nickel P., Meyer T.F.;
RT   "Opacity genes in Neisseria gonorrhoeae: control of phase and antigenic
RT   variation.";
RL   Cell 47:61-71(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1815562; DOI=10.1111/j.1365-2958.1991.tb00813.x;
RA   Bhat K.S., Gibbs C.P., Barrera O., Morrison S.G., Jaehnig F., Stern A.,
RA   Kupsch E.-M., Meyer T.F., Swanson J.;
RT   "The opacity proteins of Neisseria gonorrhoeae strain MS11 are encoded by a
RT   family of 11 complete genes.";
RL   Mol. Microbiol. 5:1889-1901(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MS11 / F3;
RX   PubMed=8440254; DOI=10.1002/j.1460-2075.1993.tb05697.x;
RA   Kupsch E.-M., Knepper B., Kuroki T., Heuer I., Meyer T.F.;
RT   "Variable opacity (Opa) outer membrane proteins account for the cell
RT   tropisms displayed by Neisseria gonorrhoeae for human leukocytes and
RT   epithelial cells.";
RL   EMBO J. 12:641-650(1993).
CC   -!- FUNCTION: Implicated in a number of adherence functions. OPA proteins
CC       are implicated in pathogenesis and are subject to phase variation.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane.
CC   -!- MISCELLANEOUS: Expression of opacity proteins is regulated by the
CC       number of translated repeat elements CTCTT, which code for part of the
CC       signal sequence; the protein can only be synthesized when the number of
CC       repeats place the start codon in frame with the rest of the protein.
CC   -!- SIMILARITY: Belongs to the opacity porin family. {ECO:0000305}.
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DR   EMBL; M14746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X52370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z18927; CAA79360.1; -; Genomic_DNA.
DR   PIR; S16618; KONH0.
DR   AlphaFoldDB; P11296; -.
DR   SMR; P11296; -.
DR   PRIDE; P11296; -.
DR   Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR   GO; GO:0009279; C:cell outer membrane; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015288; F:porin activity; IEA:InterPro.
DR   InterPro; IPR011250; OMP/PagP_b-brl.
DR   InterPro; IPR003394; Porin_opacity.
DR   Pfam; PF02462; Opacity; 1.
DR   SUPFAM; SSF56925; SSF56925; 1.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Direct protein sequencing; Membrane; Signal;
KW   Transmembrane; Transmembrane beta strand.
FT   SIGNAL          <1..1
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..>236
FT                   /note="Opacity protein opA50"
FT                   /id="PRO_0000021907"
FT   NON_TER         1
FT   NON_TER         236
SQ   SEQUENCE   236 AA;  26685 MW;  68DC237692183398 CRC64;
     ASEDGGRGPY VQADLAYAYE HITHDYPKPT DPSKGKISTV SDYFRNIRTH SIHPRVSVGY
     DFGGWRIAAD YARYRKWSDN KYSVSIKNMR VHKHNSNRKN LKTENQENGS FHAVSSLGLS
     AIYDFQINDK FKPYIGARVA YGHVRHSIDS TKKITGLLTT STPGIMSGVY KVLRTPGAHR
     ESDSIRRVGL GVIAGVGFDI TPKLTLDAGY RYHNWGRLEN TRFKTHEASL GVRYRF