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Database: UniProt
Entry: P09323
LinkDB: P09323
Original site: P09323 
ID   PTW3C_ECOLI             Reviewed;         648 AA.
AC   P09323;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-SEP-2014, entry version 137.
DE   RecName: Full=PTS system N-acetylglucosamine-specific EIICBA component;
DE   AltName: Full=EIICBA-Nag;
DE            Short=EII-Nag;
DE   Includes:
DE     RecName: Full=N-acetylglucosamine permease IIC component;
DE     AltName: Full=PTS system N-acetylglucosamine-specific EIIC component;
DE   Includes:
DE     RecName: Full=N-acetylglucosamine-specific phosphotransferase enzyme IIB component;
DE              EC=2.7.1.69;
DE     AltName: Full=PTS system N-acetylglucosamine-specific EIIB component;
DE   Includes:
DE     RecName: Full=N-acetylglucosamine-specific phosphotransferase enzyme IIA component;
DE              EC=2.7.1.-;
DE     AltName: Full=PTS system N-acetylglucosamine-specific EIIA component;
GN   Name=nagE; Synonyms=pstN; OrderedLocusNames=b0679, JW0665;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3284790; DOI=10.1016/0378-1119(88)90558-6;
RA   Rogers M.J., Ohgi T., Plumbridge J., Soell D.;
RT   "Nucleotide sequences of the Escherichia coli nagE and nagB genes: the
RT   structural genes for the N-acetylglucosamine transport protein of the
RT   bacterial phosphoenolpyruvate: sugar phosphotransferase system and for
RT   glucosamine-6-phosphate deaminase.";
RL   Gene 62:197-207(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3056518; DOI=10.1021/bi00416a034;
RA   Peri K.G., Waygood E.B.;
RT   "Sequence of cloned enzyme IIN-acetylglucosamine of the
RT   phosphoenolpyruvate:N-acetylglucosamine phosphotransferase system of
RT   Escherichia coli.";
RL   Biochemistry 27:6054-6061(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar
CC       phosphotransferase system (sugar PTS), a major carbohydrate active
CC       -transport system, catalyzes the phosphorylation of incoming sugar
CC       substrates concomitantly with their translocation across the cell
CC       membrane. This system is involved in N-acetylglucosamine
CC       transport.
CC   -!- CATALYTIC ACTIVITY: Protein EIIA N(pi)-phospho-L-histidine +
CC       protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine.
CC   -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine + sugar = protein EIIB + sugar phosphate.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein.
CC   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel
CC       and contains the specific substrate-binding site.
CC   -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC       cysteinyl or histidyl residue, depending on the transported sugar.
CC       Then, it transfers the phosphoryl group to the sugar substrate
CC       concomitantly with the sugar uptake processed by the EIIC domain.
CC   -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a
CC       histidyl residue. Then, it transfers the phosphoryl group to the
CC       EIIB domain.
CC   -!- SIMILARITY: Contains 1 PTS EIIA type-1 domain.
CC   -!- SIMILARITY: Contains 1 PTS EIIB type-1 domain.
CC   -!- SIMILARITY: Contains 1 PTS EIIC type-1 domain.
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DR   EMBL; M19284; AAA24192.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73773.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35327.1; -; Genomic_DNA.
DR   PIR; B29895; WQEC2N.
DR   RefSeq; NP_415205.1; NC_000913.3.
DR   RefSeq; YP_488959.1; NC_007779.1.
DR   ProteinModelPortal; P09323; -.
DR   SMR; P09323; 392-466, 500-648.
DR   STRING; 511145.b0679; -.
DR   TCDB; 4.A.1.1.2; the pts glucose-glucoside (glc) family.
DR   PaxDb; P09323; -.
DR   PRIDE; P09323; -.
DR   EnsemblBacteria; AAC73773; AAC73773; b0679.
DR   EnsemblBacteria; BAA35327; BAA35327; BAA35327.
DR   GeneID; 12932215; -.
DR   GeneID; 945292; -.
DR   KEGG; ecj:Y75_p0658; -.
DR   KEGG; eco:b0679; -.
DR   PATRIC; 32116545; VBIEscCol129921_0705.
DR   EchoBASE; EB0629; -.
DR   EcoGene; EG10635; nagE.
DR   eggNOG; COG1263; -.
DR   HOGENOM; HOG000250993; -.
DR   KO; K02802; -.
DR   KO; K02803; -.
DR   KO; K02804; -.
DR   OMA; GMWIANS; -.
DR   OrthoDB; EOG6FFS9V; -.
DR   PhylomeDB; P09323; -.
DR   BioCyc; EcoCyc:NAGE-MONOMER; -.
DR   BioCyc; ECOL316407:JW0665-MONOMER; -.
DR   BioCyc; MetaCyc:NAGE-MONOMER; -.
DR   PRO; PR:P09323; -.
DR   Genevestigator; P09323; -.
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-SubCell.
DR   GO; GO:0042895; F:antibiotic transporter activity; IGI:EcoCyc.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0022880; F:protein-N(PI)-phosphohistidine-N-acetylglucosamine phosphotransferase system transporter activity; IDA:EcoCyc.
DR   GO; GO:0042891; P:antibiotic transport; IGI:EcoCyc.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR   GO; GO:0015764; P:N-acetylglucosamine transport; IDA:EcoCyc.
DR   GO; GO:0009254; P:peptidoglycan turnover; IGI:EcoCyc.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:EcoCyc.
DR   GO; GO:0015771; P:trehalose transport; IDA:GOC.
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;
KW   Cell inner membrane; Cell membrane; Complete proteome; Kinase;
KW   Membrane; Phosphotransferase system; Reference proteome;
KW   Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    648       PTS system N-acetylglucosamine-specific
FT                                EIICBA component.
FT                                /FTId=PRO_0000186475.
FT   TRANSMEM     16     36       Helical; (Potential).
FT   TRANSMEM     38     58       Helical; (Potential).
FT   TRANSMEM     70     90       Helical; (Potential).
FT   TRANSMEM     92    112       Helical; (Potential).
FT   TRANSMEM    132    152       Helical; (Potential).
FT   TRANSMEM    159    179       Helical; (Potential).
FT   TRANSMEM    192    212       Helical; (Potential).
FT   TRANSMEM    232    252       Helical; (Potential).
FT   TRANSMEM    260    280       Helical; (Potential).
FT   TRANSMEM    282    302       Helical; (Potential).
FT   TRANSMEM    303    323       Helical; (Potential).
FT   TRANSMEM    339    359       Helical; (Potential).
FT   DOMAIN        1    371       PTS EIIC type-1.
FT   DOMAIN      390    472       PTS EIIB type-1.
FT   DOMAIN      517    621       PTS EIIA type-1.
FT   ACT_SITE    412    412       Phosphocysteine intermediate; for EIIB
FT                                activity (By similarity).
FT   ACT_SITE    569    569       Tele-phosphohistidine intermediate; for
FT                                EIIA activity (By similarity).
SQ   SEQUENCE   648 AA;  68347 MW;  1E24C97CFCBBAA59 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 LVMGVIFFAI YFVVFSLVIR
     MFNLKTPGRE DKEDEIVTEE ANSNTEEGLT QLATNYIAAV GGTDNLKAID ACITRLRLTV
     ADSARVNDTM CKRLGASGVV KLNKQTIQVI VGAKAESIGD AMKKVVARGP VAAASAEATP
     ATAAPVAKPQ AVPNAVSIAE LVSPITGDVV ALDQVPDEAF ASKAVGDGVA VKPTDKIVVS
     PAAGTIVKIF NTNHAFCLET EKGAEIVVHM GIDTVALEGK GFKRLVEEGA QVSAGQPILE
     MDLDYLNANA RSMISPVVCS NIDDFSGLII KAQGHIVAGQ TPLYEIKK
//
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