ID   OMPA1_NEIMC             Reviewed;         393 AA.
AC   P13415;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Major outer membrane protein P.IA;
DE            Short=PIA;
DE            Short=Protein IA;
DE   AltName: Full=Class 1 protein;
DE   Flags: Precursor;
GN   Name=porA;
OS   Neisseria meningitidis serogroup C.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=135720;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MC50 / Serogroup C / Type NT / Subtype 16;
RX   PubMed=2503673; DOI=10.1111/j.1365-2958.1989.tb01802.x;
RA   Barlow A.K., Heckels J.E., Clarke I.N.;
RT   "The class 1 outer membrane protein of Neisseria meningitidis: gene
RT   sequence and structural and immunological similarities to gonococcal
RT   porins.";
RL   Mol. Microbiol. 3:131-139(1989).
CC   -!- FUNCTION: Serves as a slightly cation selective porin. Major antigen on
CC       the gonococcal cell surface and it may have pathogenic properties in
CC       addition to its porin activity.
CC   -!- SUBUNIT: Homotrimer.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the Gram-negative porin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X12899; CAA31385.1; -; Genomic_DNA.
DR   PIR; S04161; S04161.
DR   PDB; 5NQP; X-ray; 2.86 A; A/B/C=195-208.
DR   PDB; 5NQX; X-ray; 3.66 A; A/B/C/D/E=195-207.
DR   PDB; 5NQY; X-ray; 2.60 A; A=195-208.
DR   PDB; 5NQZ; X-ray; 1.63 A; A/B=195-206.
DR   PDBsum; 5NQP; -.
DR   PDBsum; 5NQX; -.
DR   PDBsum; 5NQY; -.
DR   PDBsum; 5NQZ; -.
DR   AlphaFoldDB; P13415; -.
DR   SMR; P13415; -.
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:0034220; P:ion transmembrane transport; IEA:InterPro.
DR   CDD; cd00342; gram_neg_porins; 1.
DR   Gene3D; 2.40.160.10; -; 1.
DR   InterPro; IPR033900; Gram_neg_porin_domain.
DR   InterPro; IPR023614; Porin_dom_sf.
DR   InterPro; IPR001702; Porin_Gram-ve.
DR   InterPro; IPR013793; Porin_Gram-ve_CS.
DR   InterPro; IPR002299; Porin_Neis.
DR   Pfam; PF00267; Porin_1; 1.
DR   PRINTS; PR00182; ECOLNEIPORIN.
DR   PRINTS; PR00184; NEISSPPORIN.
DR   PROSITE; PS00576; GRAM_NEG_PORIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell outer membrane; Ion transport; Membrane; Porin; Signal;
KW   Transmembrane; Transmembrane beta strand; Transport.
FT   SIGNAL          1..19
FT   CHAIN           20..393
FT                   /note="Major outer membrane protein P.IA"
FT                   /id="PRO_0000025275"
FT   STRAND          195..198
FT                   /evidence="ECO:0007829|PDB:5NQY"
FT   STRAND          200..202
FT                   /evidence="ECO:0007829|PDB:5NQP"
FT   STRAND          204..208
FT                   /evidence="ECO:0007829|PDB:5NQY"
SQ   SEQUENCE   393 AA;  42262 MW;  955C364812F9E30F CRC64;
     MRKKLTALVL SALPLAAVAD VSLYGEIKAG VEGRNIQAQL TEQPQVTNGV QGNQVKVTKA
     KSRIRTKISD FGSFIGFKGS EDLGEGLKAV WQLEQDVSVA GGGASQWGNR ESFIGLAGEF
     GTLRAGRVAN QFDDASQAIN PWDSNNDVAS QLGIFKRHDD MPVSVRYDSP EFSGFSGSVQ
     FVPAQNSKSA YKPAYYTKDT NNNLTLVPAV VGKPGSDVYY AGLNYKNGGF AGNYAFKYAR
     HANVGRNAFE LFLIGSATSD EAKGTDPLKN HQVHRLTGGY EEGGLNLALA AQLDLSENGD
     KAKTKNSTTE IAATASYRFG NAVPRISYAH GFDLIERGKK GENTSYDQII AGVDYDFSKR
     TSAIVSGAWL KRNTGIGNYT QINAASVGLR HKF