OMPC_NEIGO
ID OMPC_NEIGO Reviewed; 270 AA.
AC P09888;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Outer membrane protein P.IIC;
DE Short=Protein IIC;
DE Flags: Precursor;
GN Name=piiC;
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JS3;
RX PubMed=3145386; DOI=10.1111/j.1365-2958.1988.tb00091.x;
RA van der Ley P.;
RT "Three copies of a single protein II-encoding sequence in the genome of
RT Neisseria gonorrhoeae JS3: evidence for gene conversion and gene
RT duplication.";
RL Mol. Microbiol. 2:797-806(1988).
RN [2]
RP PROTEIN SEQUENCE OF 26-45.
RX PubMed=3114142; DOI=10.1128/iai.55.9.2026-2031.1987;
RA Barritt D.S., Schwalbe R.S., Klapper D.G., Cannon J.G.;
RT "Antigenic and structural differences among six proteins II expressed by a
RT single strain of Neisseria gonorrhoeae.";
RL Infect. Immun. 55:2026-2031(1987).
CC -!- FUNCTION: This protein serves as a porin.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the opacity porin family. {ECO:0000305}.
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DR EMBL; X12625; CAA31144.1; -; Genomic_DNA.
DR PIR; S03095; KONH2C.
DR AlphaFoldDB; P09888; -.
DR SMR; P09888; -.
DR PRIDE; P09888; -.
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: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.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR InterPro; IPR016373; Opacity.
DR InterPro; IPR003394; Porin_opacity.
DR Pfam; PF02462; Opacity; 1.
DR PIRSF; PIRSF002984; Opacity; 1.
DR SUPFAM; SSF56925; SSF56925; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Direct protein sequencing; Ion transport; Membrane;
KW Porin; Signal; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:3114142"
FT CHAIN 26..270
FT /note="Outer membrane protein P.IIC"
FT /id="PRO_0000025197"
FT TOPO_DOM 26..35
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..44
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..76
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..85
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..89
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..96
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..142
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..157
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..173
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..221
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..234
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..246
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..261
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..270
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT REGION 194..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 30
FT /note="G -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="L -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="A -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 30269 MW; F6B448373830A50D CRC64;
MQPAKNLLFS SLLFSSLLFS SAARAASEDG GRGPYVQADL AYAAERITHD YPKPTGTGKN
KISTVSDYFR NIRTHSVHPR VSVGYDFGSW RIAADYARYR KWNNNKYSVS IKELLRNDNS
ASGVRGHLNI QTQKTEHQEN GTFHAVSSLG LSTIYDFDTG SRFKPYIGMR VAYGHVRHQV
RSVEQETEII TTYPSNGGGK VSLSSKMPPK SAHHQSNSIR RVGLGVIAGV GFDITPNLTL
DTGYRYHNWG RLENTRFKTH EASLGMRYRF