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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   25-OCT-2017, entry version 160.
DE   RecName: Full=PTS system N-acetylglucosamine-specific EIICBA component {ECO:0000303|PubMed:3056518};
DE   AltName: Full=EIICBA-Nag {ECO:0000303|PubMed:3056518};
DE            Short=EII-Nag {ECO:0000303|PubMed:3056518};
DE   Includes:
DE     RecName: Full=N-acetylglucosamine permease IIC component {ECO:0000303|PubMed:3056518};
DE     AltName: Full=PTS system N-acetylglucosamine-specific EIIC component {ECO:0000303|PubMed:3056518};
DE   Includes:
DE     RecName: Full=N-acetylglucosamine-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:3056518};
DE              EC=2.7.1.193 {ECO:0000269|PubMed:4919472};
DE     AltName: Full=PTS system N-acetylglucosamine-specific EIIB component {ECO:0000303|PubMed:3056518};
DE   Includes:
DE     RecName: Full=N-acetylglucosamine-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:3056518};
DE              EC=2.7.1.193 {ECO:0000269|PubMed:4919472};
DE     AltName: Full=PTS system N-acetylglucosamine-specific EIIA component {ECO:0000303|PubMed:3056518};
GN   Name=nagE {ECO:0000303|PubMed:3056518}; Synonyms=pstN;
GN   OrderedLocusNames=b0679, JW0665;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND ACTIVE SITE.
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   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=4919472; DOI=10.1042/bj1180089;
RA   White R.J.;
RT   "The role of the phosphoenolpyruvate phosphotransferase system in the
RT   transport of N-acetyl-D-glucosamine by Escherichia coli.";
RL   Biochem. J. 118:89-92(1970).
RN   [7]
RP   FUNCTION, AND ENZYME REGULATION.
RX   PubMed=161156; DOI=10.1128/AAC.16.6.801;
RA   Ammer J., Brennenstuhl M., Schindler P., Hoeltje J.V., Zaehner H.;
RT   "Phosphorylation of streptozotocin during uptake via the
RT   phosphoenolpyruvate: sugar phosphotransferase system in Escherichia
RT   coli.";
RL   Antimicrob. Agents Chemother. 16:801-807(1979).
RN   [8]
RP   INDUCTION.
RX   PubMed=1766379; DOI=10.1111/j.1365-2958.1991.tb00828.x;
RA   Plumbridge J.A.;
RT   "Repression and induction of the nag regulon of Escherichia coli K-12:
RT   the roles of nagC and nagA in maintenance of the uninduced state.";
RL   Mol. Microbiol. 5:2053-2062(1991).
RN   [9]
RP   INDUCTION.
RX   PubMed=7791215; DOI=10.1006/jmbi.1995.0346;
RA   Plumbridge J., Kolb A.;
RT   "Nag repressor-operator interactions: protein-DNA contacts cover more
RT   than two turns of the DNA helix.";
RL   J. Mol. Biol. 249:890-902(1995).
RN   [10]
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).
RN   [11]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19617367; DOI=10.1128/JB.00448-09;
RA   Plumbridge J.;
RT   "An alternative route for recycling of N-acetylglucosamine from
RT   peptidoglycan involves the N-acetylglucosamine phosphotransferase
RT   system in Escherichia coli.";
RL   J. Bacteriol. 191:5641-5647(2009).
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 (PubMed:4919472). This system is involved in N-
CC       acetylglucosamine transport (PubMed:4919472). It can also
CC       transport and phosphorylate the antibiotic streptozotocin
CC       (PubMed:161156). Could play a significant role in the recycling of
CC       peptidoglycan (PubMed:19617367). {ECO:0000269|PubMed:161156,
CC       ECO:0000269|PubMed:19617367, ECO:0000269|PubMed:4919472,
CC       ECO:0000305|PubMed:3056518}.
CC   -!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + N-
CC       acetyl-D-glucosamine(Side 1) = [protein]-L-histidine + N-acetyl-D-
CC       glucosamine 6-phosphate(Side 2). {ECO:0000269|PubMed:4919472}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P69783};
CC   -!- ENZYME REGULATION: P-chloromercuribenzoate inhibits the
CC       accumulation of both N-acetyl-D-glucosamine and antibiotic
CC       streptozotocin (2-deoxy-2-(3-methyl-3-nitrosoureido)-D-
CC       glucopyranose). N-acetyl-D-glucosamine is a competitive inhibitor
CC       for the uptake of streptozotocin. {ECO:0000269|PubMed:161156}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00426, ECO:0000269|PubMed:15919996}; Multi-pass
CC       membrane protein {ECO:0000255|PROSITE-ProRule:PRU00426,
CC       ECO:0000269|PubMed:15919996}.
CC   -!- INDUCTION: Induced by N-acetylglucosamine-6-phosphate and
CC       repressed by NagC. {ECO:0000269|PubMed:1766379,
CC       ECO:0000269|PubMed:7791215}.
CC   -!- DOMAIN: The PTS EIIC type-1 domain forms the PTS system
CC       translocation channel and contains the specific substrate-binding
CC       site. {ECO:0000255|PROSITE-ProRule:PRU00426}.
CC   -!- DOMAIN: The PTS EIIB type-1 domain is phosphorylated by phospho-
CC       EIIA on a cysteinyl residue. Then, it transfers the phosphoryl
CC       group to the sugar substrate concomitantly with the sugar uptake
CC       processed by the PTS EIIC type-1 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00421}.
CC   -!- DOMAIN: The PTS EIIA type-1 domain is phosphorylated by phospho-
CC       HPr on a histidyl residue. Then, it transfers the phosphoryl group
CC       to the PTS EIIB type-1 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00416}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking nagE and nagA reduce by 50%
CC       the amount of GlcNAc6P. Together with the mutations of the genes
CC       of the peptidoglycan recycling pathway (ampG, anmK, murQ, nagK and
CC       nagZ), the accumulation of GlcNAc6P is eliminated.
CC       {ECO:0000269|PubMed:19617367}.
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; WP_001023093.1; NZ_LN832404.1.
DR   ProteinModelPortal; P09323; -.
DR   SMR; P09323; -.
DR   BioGrid; 4261209; 4.
DR   STRING; 316385.ECDH10B_0744; -.
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; 945292; -.
DR   KEGG; ecj:JW0665; -.
DR   KEGG; eco:b0679; -.
DR   PATRIC; fig|1411691.4.peg.1598; -.
DR   EchoBASE; EB0629; -.
DR   EcoGene; EG10635; nagE.
DR   eggNOG; ENOG4105CI1; Bacteria.
DR   eggNOG; COG1263; LUCA.
DR   eggNOG; COG1264; LUCA.
DR   eggNOG; COG2190; LUCA.
DR   HOGENOM; HOG000250993; -.
DR   InParanoid; P09323; -.
DR   KO; K02802; -.
DR   KO; K02803; -.
DR   KO; K02804; -.
DR   PhylomeDB; P09323; -.
DR   BioCyc; EcoCyc:NAGE-MONOMER; -.
DR   BioCyc; MetaCyc:NAGE-MONOMER; -.
DR   PRO; PR:P09323; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; 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-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; 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:0090586; F:protein-phosphocysteine-N-acetylglucosamine phosphotransferase system transporter activity; IDA: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:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:EcoCyc.
DR   CDD; cd00212; PTS_IIB_glc; 1.
DR   Gene3D; 3.30.1360.60; -; 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR036878; Glu_permease_IIB.
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   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Complete proteome; Kinase;
KW   Membrane; Metal-binding; Phosphoprotein; Phosphotransferase system;
KW   Reference proteome; Sugar transport; Transferase; Transmembrane;
KW   Transmembrane helix; Transport; Zinc.
FT   CHAIN         1    648       PTS system N-acetylglucosamine-specific
FT                                EIICBA component.
FT                                /FTId=PRO_0000186475.
FT   TRANSMEM     16     36       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM     38     58       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM     70     90       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM     92    112       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    132    152       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    159    179       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    192    212       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    232    252       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    260    280       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    282    302       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    303    323       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    339    359       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   DOMAIN        1    371       PTS EIIC type-1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   DOMAIN      390    472       PTS EIIB type-1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00421}.
FT   DOMAIN      517    621       PTS EIIA type-1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00416}.
FT   ACT_SITE    412    412       Phosphocysteine intermediate; for EIIB
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00421}.
FT   ACT_SITE    569    569       Tele-phosphohistidine intermediate; for
FT                                EIIA activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00416,
FT                                ECO:0000305|PubMed:3056518}.
FT   METAL       554    554       Zinc. {ECO:0000250|UniProtKB:P69783}.
FT   METAL       569    569       Zinc. {ECO:0000250|UniProtKB:P69783}.
FT   SITE        554    554       Important for phospho-donor activity.
FT                                {ECO:0000250|UniProtKB:P69783}.
FT   MOD_RES     412    412       Phosphocysteine; by EIIA.
FT                                {ECO:0000250|UniProtKB:P69786,
FT                                ECO:0000305}.
FT   MOD_RES     569    569       Phosphohistidine; by HPr.
FT                                {ECO:0000250|UniProtKB:P69783,
FT                                ECO:0000305}.
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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