OMPA_NEIMA
ID OMPA_NEIMA Reviewed; 395 AA.
AC P57041; A1ISL8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
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; OrderedLocusNames=NMA1642;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(2000).
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}.
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DR EMBL; AL157959; CAM08777.1; -; Genomic_DNA.
DR PIR; F81858; F81858.
DR RefSeq; WP_002247001.1; NC_003116.1.
DR PDB; 1QKZ; X-ray; 1.95 A; P=46-55.
DR PDBsum; 1QKZ; -.
DR AlphaFoldDB; P57041; -.
DR SMR; P57041; -.
DR ABCD; P57041; 1 sequenced antibody.
DR EnsemblBacteria; CAM08777; CAM08777; NMA1642.
DR KEGG; nma:NMA1642; -.
DR HOGENOM; CLU_038238_4_0_4; -.
DR OMA; GDKTKNS; -.
DR BioCyc; NMEN122587:NMA_RS08205-MON; -.
DR EvolutionaryTrace; P57041; -.
DR Proteomes; UP000000626; Chromosome.
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 /evidence="ECO:0000250"
FT CHAIN 20..395
FT /note="Major outer membrane protein P.IA"
FT /id="PRO_0000025273"
SQ SEQUENCE 395 AA; 42270 MW; F7D9CE6480586577 CRC64;
MRKKLTALVL SALPLAAVAD VSLYGEIKAG VEGRNYQLQL TEAQAANGGA SGQVKVTKVT
KAKSRIRTKI SDFGSFIGFK GSEDLGEGLK AVWQLEQDVS VAGGGATQWG NRESFIGLAG
EFGTLRAGRV ANQFDDASQA IDPWDSNNDV ASQLGIFKRH DDMPVSVRYD SPEFSGFSGS
VQFVPAQNSK SAYKPAYWTT VNTGSATTTT FVPAVVGKPG SDVYYAGLNY KNGGFAGNYA
FKYARHANVG RDAFELFLLG SGSDQAKGTD PLKNHQVHRL TGGYEEGGLN LALAAQLDLS
ENGDKTKNST TEIAATASYR FGNAVPRISY AHGFDFIERG KKGENTSYDQ IIAGVDYDFS
KRTSAIVSGA WLKRNTGIGN YTQINAASVG LRHKF