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 01-MAY-2013, entry version 124.
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 277:1453-1474(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_000913.2.
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; 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; QANLEMI; -.
DR ProtClustDB; PRK10255; -.
DR BioCyc; EcoCyc:NAGE-MONOMER; -.
DR BioCyc; ECOL316407:JW0665-MONOMER; -.
DR Genevestigator; P09323; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0019866; C:organelle inner membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:EC.
DR GO; GO:0005351; F:sugar:hydrogen symporter activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; NAS:UniProtKB.
DR GO; GO:0005215; F:transporter activity; NAS:UniProtKB.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:response to DNA damage stimulus; IEP:EcoliWiki.
DR Gene3D; 3.30.1360.60; -; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR018113; PTrfase_EIIB/Cys_phosph_CS.
DR InterPro; IPR001127; PTS_EIIA_1_perm.
DR InterPro; IPR001996; PTS_EIIB_1.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR011535; PTS_Glc-like_IIB_component.
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; Dup_hybrid_motif; 1.
DR SUPFAM; SSF55604; PTS_EIIB; 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
//
