ID   OMPF_SHIFM              Reviewed;         362 AA.
AC   A0A4P7TN82;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-JUL-2019, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Outer membrane porin F {ECO:0000303|PubMed:8359885};
DE   AltName: Full=Outer membrane protein F;
DE   AltName: Full=Porin OmpF;
DE   Flags: Precursor;
GN   Name=ompF; ORFNames=EKN05_011710;
OS   Shigella flexneri serotype 5a (strain M90T).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=1086030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M90T / Serotype 5a;
RA   Cervantes-Rivera R., Puhar A.;
RT   "Complete genome sequence and annotation of the laboratory reference strain
RT   Shigella flexneri 5a M90T and genome-wide transcription start site
RT   determination.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=M90T / Serotype 5a;
RX   PubMed=8359885; DOI=10.1128/iai.61.9.3625-3635.1993;
RA   Bernardini M.L., Sanna M.G., Fontaine A., Sansonetti P.J.;
RT   "OmpC is involved in invasion of epithelial cells by Shigella flexneri.";
RL   Infect. Immun. 61:3625-3635(1993).
CC   -!- FUNCTION: Forms pores that allow passive diffusion of small molecules
CC       across the outer membrane. {ECO:0000305}.
CC   -!- SUBUNIT: Homotrimer. Forms mixed heterotrimers with OmpC and with PhoE;
CC       other mixed heterotrimers are also probable.
CC       {ECO:0000250|UniProtKB:P02931}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:8359885};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P02931}.
CC   -!- INDUCTION: Expressed at low osmolarity, not expressed at high
CC       osmolarity (at protein level). Expression is under the control of OmpR-
CC       EnvZ two-component system; not expressed in the absence of ompR-envZ
CC       (at protein elevel). {ECO:0000269|PubMed:8359885}.
CC   -!- DISRUPTION PHENOTYPE: No visible effect on infection of HeLa cells.
CC       {ECO:0000269|PubMed:8359885}.
CC   -!- SIMILARITY: Belongs to the Gram-negative porin family. {ECO:0000305}.
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DR   EMBL; CP037923; QCC32183.1; -; Genomic_DNA.
DR   RefSeq; WP_000977920.1; NZ_CM001474.1.
DR   AlphaFoldDB; A0A4P7TN82; -.
DR   SMR; A0A4P7TN82; -.
DR   EnsemblBacteria; QCC32183; QCC32183; EKN05_011710.
DR   GeneID; 66670795; -.
DR   Proteomes; UP000296678; 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; IPR001897; Porin_gammaproteobac.
DR   InterPro; IPR001702; Porin_Gram-ve.
DR   InterPro; IPR013793; Porin_Gram-ve_CS.
DR   Pfam; PF00267; Porin_1; 1.
DR   PRINTS; PR00183; ECOLIPORIN.
DR   PRINTS; PR00182; ECOLNEIPORIN.
DR   PROSITE; PS00576; GRAM_NEG_PORIN; 1.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Ion transport; Membrane; Porin; Signal; Transmembrane;
KW   Transmembrane beta strand; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..362
FT                   /note="Outer membrane porin F"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5020675545"
SQ   SEQUENCE   362 AA;  39333 MW;  3F0974D96DB65464 CRC64;
     MMKRNILAVI VPALLVAGTA NAAEIYNKDG NKVDLYGKAV GLHYFSKGNG ENSYGGNGDM
     TYARLGFKGE TQINSDLTGY GQWEYNFQGN NSEGADAQTG NKTRLAFAGL KYADVGSFDY
     GRNYGVVYDA LGYTDMLPEF GGDTAYSDDF FVGRVGGVAT YRNSNFFGLV DGLNFAVQYL
     GKNERDTARR SNGDGVGGSI SYEYEGFGIV GAYGAADRTN LQEAQPLGNG KKAEQWATGL
     KYDANNIYLA ANYGETRNAT PITNKFTNTS GFANKTQDVL LVAQYQFDFG LRPSIAYTKS
     KAKDVEGIGD VDLVNYFEVG ATYYFNKNMS TYVDYIINQI DSDNKLGVGS DDTVAVGIVY
     QF