(data stored in ACNUC7421 zone)

SWISSPROT: A0A0H3JE22_ECO57

ID   A0A0H3JE22_ECO57        Unreviewed;       648 AA.
AC   A0A0H3JE22;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   30-AUG-2017, entry version 21.
DE   SubName: Full=PTS system, N-acetylglucosamine-specific enzyme IIABC {ECO:0000313|EMBL:BAB34132.1};
GN   OrderedLocusNames=ECs0709 {ECO:0000313|EMBL:BAB34132.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB34132.1, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB34132.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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DR   EMBL; BA000007; BAB34132.1; -; Genomic_DNA.
DR   RefSeq; NP_308736.1; NC_002695.1.
DR   RefSeq; WP_001023104.1; NZ_MWVM01000011.1.
DR   ProteinModelPortal; A0A0H3JE22; -.
DR   STRING; 155864.Z0826; -.
DR   EnsemblBacteria; BAB34132; BAB34132; BAB34132.
DR   GeneID; 917078; -.
DR   KEGG; ecs:ECs0709; -.
DR   PATRIC; fig|386585.9.peg.822; -.
DR   KO; K02802; -.
DR   KO; K02803; -.
DR   KO; K02804; -.
DR   Proteomes; UP000000558; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019866; C:organelle inner membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015572; F:N-acetylglucosamine transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   CDD; cd00212; PTS_IIB_glc; 1.
DR   Gene3D; 3.30.1360.60; -; 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR018113; PTrfase_EIIB_Cys.
DR   InterPro; IPR001127; PTS_EIIA_1_perm.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013013; PTS_EIIC_1.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   InterPro; IPR010974; PTS_IIBC_nag.
DR   Pfam; PF00358; PTS_EIIA_1; 1.
DR   Pfam; PF00367; PTS_EIIB; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   SUPFAM; SSF51261; SSF51261; 1.
DR   SUPFAM; SSF55604; SSF55604; 1.
DR   TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR   TIGRFAMs; TIGR00830; PTBA; 1.
DR   TIGRFAMs; TIGR01998; PTS-II-BC-nag; 1.
DR   PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR   PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 1.
DR   PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR   PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR   PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE   4: Predicted;
DR   PRODOM; A0A0H3JE22.
DR   SWISS-2DPAGE; A0A0H3JE22.
KW   Cell membrane {ECO:0000256|SAAS:SAAS00102901};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558};
KW   Kinase {ECO:0000256|SAAS:SAAS00737055};
KW   Membrane {ECO:0000256|SAAS:SAAS00103123, ECO:0000256|SAM:Phobius};
KW   Phosphotransferase system {ECO:0000256|SAAS:SAAS00102775};
KW   Sugar transport {ECO:0000256|SAAS:SAAS00468169};
KW   Transferase {ECO:0000256|SAAS:SAAS00515976};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00103383,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00102926,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00102828}.
FT   TRANSMEM     38     61       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     68     88       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     94    112       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    132    153       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    165    185       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    192    212       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    232    252       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    259    276       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    282    306       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    337    359       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    371       PTS EIIC type-1. {ECO:0000259|PROSITE:
FT                                PS51103}.
FT   DOMAIN      390    472       PTS EIIB type-1. {ECO:0000259|PROSITE:
FT                                PS51098}.
FT   DOMAIN      517    621       PTS EIIA type-1. {ECO:0000259|PROSITE:
FT                                PS51093}.
FT   ACT_SITE    412    412       Phosphocysteine intermediate; for EIIB
FT                                activity. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00421}.
SQ   SEQUENCE   648 AA;  68332 MW;  F39796C2E9A66A7C CRC64;
     MNILGFFQRL GRALQLPIAV LPVAALLLRF GQPDLLNVAF IAQAGGAIFD NLALIFAIGV
     ASSWSKDSAG AAALAGAVGY FVLTKAMVTI NPEINMGVLA GIITGLVGGA AYNRWSDIKL
     PDFLSFFGGK RFVPIATGFF CLVLAAIFGY VWPPVQHAIH AGGEWIVSAG ALGSGIFGFI
     NRLLIPTGLH QVLNTIAWFQ IGEFTNAAGT VFHGDINRFY AGDGTAGMFM SGFFPIMMFG
     LPGAALAMYF AAPKERRPMV GGMLLSVAVT AFLTGVTEPL EFLFMFLAPL LYLLHALLTG
     ISLFVATLLG IHAGFSFSAG AIDYALMYNL PAASQNVWML LVMGVVFFAI YFVVFSLVIR
     MFNLKTPGRE DKEDEIVTEE ANSNTEEGLN QLATNYIAAV GGTDNLKAID ACITRLRLTV
     ADSARVNDTM CKRLGASGVV KLNKQTIQVI VGAKAESIGD AMKKVVARGP VAAASAEATP
     ATAAPVAKPQ AVPNAVSIAE LVSPITGDVV ALDQVPDEAF ASKAVGDGVA VKPTDKIVVS
     PAAGTIVKIF NTNHAFCLET EKGAEIVVHM GIDTVALEGK GFKRLVEEGA QVSAGQPILE
     MDLDYLNANA RSMISPVVCS NIDDFSGLII KAQGHVVAGQ TPLYEIKK
//

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