(data stored in SCRATCH zone)

SWISSPROT: C8U1X2_ECO10

ID   C8U1X2_ECO10            Unreviewed;       351 AA.
AC   C8U1X2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 55.
DE   SubName: Full=Outer membrane phosphoporin PhoE {ECO:0000313|EMBL:BAI29130.1};
GN   Name=phoE {ECO:0000313|EMBL:BAI29130.1};
GN   OrderedLocusNames=ECO103_0256 {ECO:0000313|EMBL:BAI29130.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29130.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29130.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|RuleBase:RU000469}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000256|RuleBase:RU000469}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU000469}.
CC   -!- SIMILARITY: Belongs to the Gram-negative porin family.
CC       {ECO:0000256|RuleBase:RU000469}.
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DR   EMBL; AP010958; BAI29130.1; -; Genomic_DNA.
DR   RefSeq; WP_000749881.1; NC_013353.1.
DR   EnsemblBacteria; BAI29130; BAI29130; ECO103_0256.
DR   KEGG; eoh:ECO103_0256; -.
DR   HOGENOM; HOG000272406; -.
DR   KO; K11929; -.
DR   OMA; KAMHYIS; -.
DR   BioCyc; ECOL585395:ECO103_RS01345-MONOMER; -.
DR   Proteomes; UP000000959; 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; 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   3: Inferred from homology;
DR   PRODOM; C8U1X2.
DR   SWISS-2DPAGE; C8U1X2.
KW   Cell outer membrane {ECO:0000256|RuleBase:RU000469};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Ion transport {ECO:0000256|RuleBase:RU000469,
KW   ECO:0000256|SAAS:SAAS00985375};
KW   Membrane {ECO:0000256|RuleBase:RU000469,
KW   ECO:0000256|SAAS:SAAS00726758};
KW   Porin {ECO:0000256|RuleBase:RU000469, ECO:0000256|SAAS:SAAS00985411};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|RuleBase:RU000469,
KW   ECO:0000256|SAAS:SAAS00985441};
KW   Transmembrane beta strand {ECO:0000256|SAAS:SAAS00985390};
KW   Transport {ECO:0000256|RuleBase:RU000469,
KW   ECO:0000256|SAAS:SAAS00985485}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    351       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002992406.
SQ   SEQUENCE   351 AA;  38966 MW;  3E58F4F284B5D42E CRC64;
     MKKSTLALVV MGIVASASVQ AAEIYNKDGN KLDVYGKVKA MHYMSDNDSK DGDQSYIRFG
     FKGETQINDQ LTGYGRWEAE FAGNKAESDT AQQKTRLAFA GLKYKDLGSF DYGRNLGALY
     DVEAWTDMFP EFGGDSSAQT DNFMTKRASG LATYRNTDFF GVIDGLNLTL QYQGKNENRD
     VKKQNGDGFG TSLTYDFGGS DFAISGAYTN SDRTNEQNLQ SRGTGKRAEA WATGLKYDAN
     NIYLATFYSE TRKMTPITGG FANKTQNFEA VAQYQFDFGL RPSLGYVLSK GKDIEGIGDE
     DLVNYIDVGA TYYFNKNMSA FVDYKINQLD SDNKLNINND DIVAVGMTYQ F
//

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