(data stored in SCRATCH9089 zone)

SWISSPROT: OMPH_PASMU

ID   OMPH_PASMU              Reviewed;         348 AA.
AC   Q9CNN9; O54347; O54349;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 110.
DE   RecName: Full=Major outer membrane protein;
DE            Short=MOMP;
DE   AltName: Full=Outer membrane protein H;
DE   Flags: Precursor;
GN   Name=ompH; OrderedLocusNames=PM0388;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-348.
RC   STRAIN=Serotype 10, and Serotype 12;
RX   PubMed=10067687; DOI=10.1016/s0264-410x(98)00266-7;
RA   Luo Y., Zeng Q., Glisson J.R., Jackwood M.W., Cheng I.H., Wang C.;
RT   "Sequence analysis of Pasteurella multocida major outer membrane protein
RT   (OmpH) and application of synthetic peptides in vaccination of chickens
RT   against homologous strain challenge.";
RL   Vaccine 17:821-831(1999).
CC   -!- FUNCTION: Structural rigidity of the outer membrane of elementary
CC       bodies and porin forming, permitting diffusion of solutes through the
CC       intracellular reticulate body membrane. {ECO:0000250}.
CC   -!- SUBUNIT: Disulfide bond interactions within and between MOMP molecules
CC       and other components form high molecular-weight oligomers.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
DR   EMBL; AE004439; AAK02472.1; -; Genomic_DNA.
DR   EMBL; U52207; AAC02251.1; -; Genomic_DNA.
DR   EMBL; U52209; AAC02253.1; -; Genomic_DNA.
DR   RefSeq; WP_010906619.1; NC_002663.1.
DR   TCDB; 1.B.1.1.14; the general bacterial porin (gbp) family.
DR   EnsemblBacteria; AAK02472; AAK02472; PM0388.
DR   KEGG; pmu:PM0388; -.
DR   PATRIC; fig|272843.6.peg.401; -.
DR   eggNOG; COG3203; LUCA.
DR   HOGENOM; HOG000249557; -.
DR   OMA; YAGFAYE; -.
DR   BioCyc; PMUL272843:G1FZ8-407-MONOMER; -.
DR   Proteomes; UP000000809; 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:0006811; P:ion transport; IEA:UniProtKB-KW.
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; IPR002299; Porin_Neis.
DR   Pfam; PF13609; Porin_4; 1.
DR   PRINTS; PR00184; NEISSPPORIN.
PE   3: Inferred from homology;
DR   PRODOM; Q9CNN9.
DR   SWISS-2DPAGE; Q9CNN9.
KW   Cell outer membrane; Disulfide bond; Ion transport; Membrane; Porin;
KW   Reference proteome; Signal; Transmembrane; Transmembrane beta strand;
KW   Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..348
FT                   /note="Major outer membrane protein"
FT                   /id="PRO_0000025269"
FT   VARIANT         167
FT                   /note="A -> T (in strain: Serotype 10)"
FT   VARIANT         221..223
FT                   /note="PPP -> APS (in strain: Serotype 10 and Serotype 12)"
SQ   SEQUENCE   348 AA;  37450 MW;  E5074B736F937ABE CRC64;
     MKKTIVALAV AAVAATSANA ATVYNQDGTK VDVNGSVRLL LKKEKDKRGD LMDNGSRVSF
     KASHDLGEGL SALAYAELRF SKDVKNKDGE VIKQPIGNNV HAKRLYAGFA YEGVGTLTFG
     NQLTIGDDVG VSDYTYFLGG INNLLSSGEK AINFKSAEFN GLTFGGAYVF SDDFDKNGLR
     DGRGFVVAGL YNRKIGDVGF AFEAGYSQKY VKQEVASVLP PPPGSVTVYK DEKEKAFMVG
     AELSYAGLAL GVDYAQSKVT NVDGKKRALE VGLNYDINDK AKVYTDFIWA KEGPKGATTR
     DRSIILGAGY KLHKQVETFV EGGWGREKDA NGVTTKDNVV GVGLRVHF
//

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