ID   OMPD_SALT1              Reviewed;         362 AA.
AC   D0ZXQ1;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Outer membrane porin protein OmpD;
DE   Flags: Precursor;
GN   Name=ompD; Synonyms=nmpC; OrderedLocusNames=STM14_1898;
OS   Salmonella typhimurium (strain 14028s / SGSC 2262).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=588858;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=14028s / SGSC 2262;
RX   PubMed=19897643; DOI=10.1128/jb.01233-09;
RA   Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT   "Short-term signatures of evolutionary change in the Salmonella enterica
RT   serovar typhimurium 14028 genome.";
RL   J. Bacteriol. 192:560-567(2010).
RN   [2]
RP   FUNCTION IN METHYL VIOLOGEN RESISTANCE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=14028s / SGSC 2262;
RX   PubMed=12410826; DOI=10.1046/j.1365-2958.2002.03204.x;
RA   Santiviago C.A., Fuentes J.A., Bueno S.M., Trombert A.N., Hildago A.A.,
RA   Socias L.T., Youderian P., Mora G.C.;
RT   "The Salmonella enterica sv. Typhimurium smvA, yddG and ompD (porin) genes
RT   are required for the efficient efflux of methyl viologen.";
RL   Mol. Microbiol. 46:687-698(2002).
CC   -!- FUNCTION: Forms pores that allow passive diffusion of small molecules
CC       across the outer membrane (By similarity). Required for resistance to
CC       methyl viologen. {ECO:0000250, ECO:0000269|PubMed:12410826}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mutants show increased sensitivity to methyl
CC       viologen. {ECO:0000269|PubMed:12410826}.
CC   -!- SIMILARITY: Belongs to the Gram-negative porin family. {ECO:0000305}.
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DR   EMBL; CP001363; ACY88369.1; -; Genomic_DNA.
DR   RefSeq; WP_000769035.1; NZ_CP043402.1.
DR   AlphaFoldDB; D0ZXQ1; -.
DR   SMR; D0ZXQ1; -.
DR   PRIDE; D0ZXQ1; -.
DR   EnsemblBacteria; ACY88369; ACY88369; STM14_1898.
DR   KEGG; seo:STM14_1898; -.
DR   PATRIC; fig|588858.6.peg.1809; -.
DR   HOGENOM; CLU_058202_0_0_6; -.
DR   OMA; AVYQHAM; -.
DR   BioCyc; SENT588858:STM14_RS08735-MON; -.
DR   Proteomes; UP000002695; 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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..362
FT                   /note="Outer membrane porin protein OmpD"
FT                   /id="PRO_0000415646"
SQ   SEQUENCE   362 AA;  39680 MW;  9F68A9A7B948174C CRC64;
     MKLKLVAVAV TSLLAAGVVN AAEVYNKDGN KLDLYGKVHA QHYFSDDNGS DGDKTYARLG
     FKGETQINDQ LTGFGQWEYE FKGNRTESQG ADKDKTRLAF AGLKFADYGS FDYGRNYGVA
     YDIGAWTDVL PEFGGDTWTQ TDVFMTGRTT GVATYRNTDF FGLVEGLNFA AQYQGKNDRD
     GAYESNGDGF GLSATYEYEG FGVGAAYAKS DRTNNQVKAA SNLNAAGKNA EVWAAGLKYD
     ANNIYLATTY SETLNMTTFG EDAAGDAFIA NKTQNFEAVA QYQFDFGLRP SIAYLKSKGK
     NLGTYGDQDL VEYIDVGATY YFNKNMSTFV DYKINLLDDS DFTKAAKVST DNIVAVGLNY
     QF