PTW3C_ECOLI
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-AUG-2022, entry version 185.
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 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., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT 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., Mau B.,
RA 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 MG1655
RT 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 ACTIVITY 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 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: the
RT 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 than
RT 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 system in
RT Escherichia coli.";
RL J. Bacteriol. 191:5641-5647(2009).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane
CC (PubMed:4919472). This system is involved in N-acetylglucosamine
CC transport (PubMed:4919472). It can also transport and phosphorylate the
CC antibiotic streptozotocin (PubMed:161156). Could play a significant
CC role in the recycling of peptidoglycan (PubMed:19617367).
CC {ECO:0000269|PubMed:161156, ECO:0000269|PubMed:19617367,
CC ECO:0000269|PubMed:4919472, ECO:0000305|PubMed:3056518}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-
CC glucosamine(out) = L-histidyl-[protein] + N-acetyl-D-glucosamine 6-
CC phosphate(in); Xref=Rhea:RHEA:49240, Rhea:RHEA-COMP:9745, Rhea:RHEA-
CC COMP:9746, ChEBI:CHEBI:29979, ChEBI:CHEBI:57513, ChEBI:CHEBI:64837,
CC ChEBI:CHEBI:506227; EC=2.7.1.193;
CC Evidence={ECO:0000269|PubMed:4919472};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P69783};
CC -!- ACTIVITY REGULATION: P-chloromercuribenzoate inhibits the accumulation
CC of both N-acetyl-D-glucosamine and antibiotic streptozotocin (2-deoxy-
CC 2-(3-methyl-3-nitrosoureido)-D-glucopyranose). N-acetyl-D-glucosamine
CC is a competitive inhibitor for the uptake of streptozotocin.
CC {ECO:0000269|PubMed:161156}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00426,
CC ECO:0000269|PubMed:15919996}.
CC -!- INDUCTION: Induced by N-acetylglucosamine-6-phosphate and repressed by
CC NagC. {ECO:0000269|PubMed:1766379, ECO:0000269|PubMed:7791215}.
CC -!- DOMAIN: The PTS EIIC type-1 domain forms the PTS system translocation
CC channel and contains the specific substrate-binding site.
CC {ECO:0000255|PROSITE-ProRule:PRU00426}.
CC -!- DOMAIN: The PTS EIIB type-1 domain is phosphorylated by phospho-EIIA on
CC a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-1 domain. {ECO:0000255|PROSITE-ProRule:PRU00421}.
CC -!- DOMAIN: The PTS EIIA type-1 domain is phosphorylated by phospho-HPr on
CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC EIIB type-1 domain. {ECO:0000255|PROSITE-ProRule:PRU00416}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking nagE and nagA reduce by 50% the
CC amount of GlcNAc6P. Together with the mutations of the genes of the
CC peptidoglycan recycling pathway (ampG, anmK, murQ, nagK and nagZ), the
CC accumulation of GlcNAc6P is eliminated. {ECO:0000269|PubMed:19617367}.
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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; WP_001023093.1; NZ_LN832404.1.
DR AlphaFoldDB; P09323; -.
DR SMR; P09323; -.
DR BioGRID; 4261209; 24.
DR STRING; 511145.b0679; -.
DR TCDB; 4.A.1.1.2; the pts glucose-glucoside (glc) family.
DR jPOST; P09323; -.
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 eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR eggNOG; COG2190; Bacteria.
DR HOGENOM; CLU_012312_1_3_6; -.
DR InParanoid; P09323; -.
DR OMA; IVHCARP; -.
DR PhylomeDB; P09323; -.
DR BioCyc; EcoCyc:NAGE-MON; -.
DR BioCyc; MetaCyc:NAGE-MON; -.
DR BRENDA; 2.7.1.193; 2026.
DR PRO; PR:P09323; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0019866; C:organelle inner membrane; IEA:InterPro.
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:0090587; F:protein-phosphocysteine-glucosamine phosphotransferase system transporter activity; IBA:GO_Central.
DR GO; GO:0090586; F:protein-phosphocysteine-N-acetylglucosamine phosphotransferase system transporter activity; IDA:EcoCyc.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00212; PTS_IIB_glc; 1.
DR Gene3D; 2.70.70.10; -; 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; Kinase; Membrane; Metal-binding;
KW Phosphoprotein; Phosphotransferase system; Reference proteome;
KW Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW Transport; Zinc.
FT CHAIN 1..648
FT /note="PTS system N-acetylglucosamine-specific EIICBA
FT component"
FT /id="PRO_0000186475"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..371
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 390..472
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 517..621
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT ACT_SITE 412
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 569
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416,
FT ECO:0000305|PubMed:3056518"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P69783"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P69783"
FT SITE 554
FT /note="Important for phospho-donor activity"
FT /evidence="ECO:0000250|UniProtKB:P69783"
FT MOD_RES 412
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P69786, ECO:0000305"
FT MOD_RES 569
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P69783, 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
