ID   OPAH_NEIGO              Reviewed;         238 AA.
AC   Q04884;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Opacity protein opA60;
DE   Flags: Precursor; Fragment;
GN   Name=opaH;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MS11 / V18;
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   ERRATUM OF PUBMED:1815562.
RX   PubMed=1584024; DOI=10.1111/j.1365-2958.1992.tb02172.x;
RA   Bhat K.S., Gibbs C.P., Barrera O., Morrison S.G., Jaehnig F., Stern S.,
RA   Kupsch E.-M., Meyer T.F., Swanson J.;
RL   Mol. Microbiol. 6:1073-1076(1992).
CC   -!- FUNCTION: Implicated in a number of adherence functions. OPA proteins
CC       are implicated in pathogenesis and are subject to phase variation.
CC   -!- INTERACTION:
CC       Q04884; P13688: CEACAM1; Xeno; NbExp=3; IntAct=EBI-26495102, EBI-4314481;
CC       Q04884; P40198: CEACAM3; Xeno; NbExp=3; IntAct=EBI-26495102, EBI-12851752;
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane.
CC   -!- SIMILARITY: Belongs to the opacity porin family. {ECO:0000305}.
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DR   EMBL; Z18939; CAA79372.1; -; Genomic_DNA.
DR   EMBL; X60711; CAA43121.1; -; Genomic_DNA.
DR   PIR; S16619; S16619.
DR   PDB; 2MAF; NMR; -; A=1-238.
DR   PDB; 2MLH; NMR; -; A=1-238.
DR   PDBsum; 2MAF; -.
DR   PDBsum; 2MLH; -.
DR   AlphaFoldDB; Q04884; -.
DR   SMR; Q04884; -.
DR   IntAct; Q04884; 2.
DR   MINT; Q04884; -.
DR   PRIDE; Q04884; -.
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; IPR006315; OM_autotransptr_brl.
DR   InterPro; IPR011250; OMP/PagP_b-brl.
DR   InterPro; IPR003394; Porin_opacity.
DR   Pfam; PF02462; Opacity; 1.
DR   SUPFAM; SSF56925; SSF56925; 1.
DR   TIGRFAMs; TIGR01414; autotrans_barl; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell outer membrane; Membrane; Signal; Transmembrane;
KW   Transmembrane beta strand.
FT   SIGNAL          <1..1
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..>238
FT                   /note="Opacity protein opA60"
FT                   /id="PRO_0000021912"
FT   VARIANT         2..4
FT                   /note="SED -> MLKA (in strain: MS11 / V18)"
FT   VARIANT         234
FT                   /note="V -> M (in strain: MS11 / V18)"
FT   NON_TER         1
FT   NON_TER         238
FT   STRAND          7..15
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:2MLH"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   STRAND          55..62
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   STRAND          65..72
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   STRAND          89..92
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:2MLH"
FT   STRAND          115..124
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   STRAND          128..142
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:2MLH"
FT   STRAND          168..170
FT                   /evidence="ECO:0007829|PDB:2MLH"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   TURN            180..182
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   STRAND          184..186
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   STRAND          191..194
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   STRAND          196..203
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   STRAND          206..212
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   STRAND          219..221
FT                   /evidence="ECO:0007829|PDB:2MLH"
FT   STRAND          222..224
FT                   /evidence="ECO:0007829|PDB:2MAF"
FT   STRAND          229..237
FT                   /evidence="ECO:0007829|PDB:2MAF"
SQ   SEQUENCE   238 AA;  27073 MW;  883A3560C2DF1B9F CRC64;
     ASEDGGRGPY VQADLAYAYE HITHDYPEPT APNKNKISTV SDYFRNIRTR SVHPRVSVGY
     DFGGWRIAAD YARYRKWNNN KYSVNIENVR IRKENGIRID RKTENQENGT FHAVSSLGLS
     AIYDFQINDK FKPYIGARVA YGHVRHSIDS TKKTIEVTTV PSNAPNGAVT TYNTDPKTQN
     DYQSNSIRRV GLGVIAGVGF DITPKLTLDA GYRYHNWGRL ENTRFKTHEA SLGVRYRF