ID   PTW3C_KLEPN             Reviewed;         651 AA.
AC   P45604;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 133.
DE   RecName: Full=PTS system N-acetylglucosamine-specific EIICBA component {ECO:0000250|UniProtKB:P09323};
DE   AltName: Full=EIICBA-Nag {ECO:0000250|UniProtKB:P09323};
DE            Short=EII-Nag {ECO:0000250|UniProtKB:P09323};
DE   Includes:
DE     RecName: Full=N-acetylglucosamine permease IIC component {ECO:0000250|UniProtKB:P09323};
DE     AltName: Full=PTS system N-acetylglucosamine-specific EIIC component {ECO:0000250|UniProtKB:P09323};
DE   Includes:
DE     RecName: Full=N-acetylglucosamine-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P09323};
DE              EC=2.7.1.193 {ECO:0000250|UniProtKB:P09323};
DE     AltName: Full=PTS system N-acetylglucosamine-specific EIIB component {ECO:0000250|UniProtKB:P09323};
DE   Includes:
DE     RecName: Full=N-acetylglucosamine-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P09323};
DE     AltName: Full=PTS system N-acetylglucosamine-specific EIIA component {ECO:0000250|UniProtKB:P09323};
GN   Name=nagE;
OS   Klebsiella pneumoniae.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Klebsiella;
OC   Klebsiella pneumoniae complex.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1033-5P14 / KAY2026;
RX   PubMed=1745234; DOI=10.1007/bf00290677;
RA   Vogler A.P., Lengeler J.W.;
RT   "Comparison of the sequences of the nagE operons from Klebsiella pneumoniae
RT   and Escherichia coli K12: enhanced variability of the enzyme IIN-
RT   acetylglucosamine in regions connecting functional domains.";
RL   Mol. Gen. Genet. 230:270-276(1991).
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. This
CC       system is involved in N-acetylglucosamine transport.
CC       {ECO:0000250|UniProtKB:P09323}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-
CC         glucosamine(out) = N-acetyl-D-glucosamine 6-phosphate(in) + L-
CC         histidyl-[protein]; Xref=Rhea:RHEA:49240, Rhea:RHEA-COMP:9745,
CC         Rhea:RHEA-COMP:9746, ChEBI:CHEBI:29979, ChEBI:CHEBI:57513,
CC         ChEBI:CHEBI:64837, ChEBI:CHEBI:506227; EC=2.7.1.193;
CC         Evidence={ECO:0000250|UniProtKB:P09323};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P69783};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00426}.
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}.
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DR   EMBL; X63289; CAA44923.1; -; Genomic_DNA.
DR   PIR; S18607; S18607.
DR   AlphaFoldDB; P45604; -.
DR   SMR; P45604; -.
DR   BRENDA; 2.7.1.193; 2814.
DR   GO; GO:0019866; C:organelle inner membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022880; F:protein-N(PI)-phosphohistidine-N-acetylglucosamine phosphotransferase system transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IEA:TreeGrafter.
DR   GO; GO:0015764; P:N-acetylglucosamine transport; IEA:TreeGrafter.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   CDD; cd00210; PTS_IIA_glc; 1.
DR   CDD; cd00212; PTS_IIB_glc; 1.
DR   FunFam; 2.70.70.10:FF:000001; PTS system glucose-specific IIA component; 1.
DR   FunFam; 3.30.1360.60:FF:000001; PTS system glucose-specific IIBC component PtsG; 1.
DR   Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR   Gene3D; 3.30.1360.60; Glucose permease domain IIB; 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; IPR050429; PTS_Glucose_EIICBA.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   InterPro; IPR010974; PTS_IIBC_nag.
DR   NCBIfam; TIGR00826; EIIB_glc; 1.
DR   NCBIfam; NF007608; PRK10255.1; 1.
DR   NCBIfam; TIGR00830; PTBA; 1.
DR   NCBIfam; TIGR01998; PTS-II-BC-nag; 1.
DR   PANTHER; PTHR30009; CYTOCHROME C-TYPE SYNTHESIS PROTEIN AND PTS TRANSMEMBRANE COMPONENT; 1.
DR   PANTHER; PTHR30009:SF4; PTS SYSTEM N-ACETYLGLUCOSAMINE-SPECIFIC EIICBA COMPONENT; 1.
DR   Pfam; PF00358; PTS_EIIA_1; 1.
DR   Pfam; PF00367; PTS_EIIB; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR   SUPFAM; SSF55604; Glucose permease domain IIB; 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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Kinase; Membrane; Metal-binding;
KW   Phosphoprotein; Phosphotransferase system; Sugar transport; Transferase;
KW   Transmembrane; Transmembrane helix; Transport; Zinc.
FT   CHAIN           1..651
FT                   /note="PTS system N-acetylglucosamine-specific EIICBA
FT                   component"
FT                   /id="PRO_0000186476"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        40..60
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        165..185
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        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        308..328
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          519..623
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        571
FT                   /note="Tele-phosphohistidine intermediate; for EIIA
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT   BINDING         556
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P69783"
FT   BINDING         571
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P69783"
FT   SITE            556
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         571
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000250|UniProtKB:P69786, ECO:0000305"
SQ   SEQUENCE   651 AA;  68180 MW;  3D8D8ADFF4BD48ED CRC64;
     MNILGFFQRL GRALQLPIAV LPVAALLLRF GQPDLLNVPF IAQAGGAIFD NLALIFAIGV
     ASSWSKDNAG SAALAGAVGY FVMTKAMVTI NPEINMGVLA GIITGLVAGA VYNRWAGIKL
     PDFLSFFGGK RFVPIATGFF CLILAAIFGY VWPPVQHAIH SGGEWIVSAG ALGSGIFGFI
     NRLLIPTGLH QVLNTIAWFQ IGEFTNAAGT VFHGDINRFY AGDGTAGMFM SGFFPIMMFG
     LPGAALAMYL AAPKARRPMV GGMLLSVAIT AFLTGVTEPL EFLFLFLAPL LYLLHAVLTG
     ISLFIATALG IHAGFSFSAG AIDYVLMYSL PAASKNVWML LVMGVVFFFV YFLLFSAVIR
     MFNLKTPGRE DKAADVVTEE ANSNTEEGLT QLATSYIAAV GGTDNLKAID ACITRLRLTV
     GDSAKVNDAA CKRLGASGVV KLNKQTIQVI VGAKAESIGD EMKKVVTRGP VAAAAAAPAG
     NVATAAPAAK PQAVANAKTV ESLVSPITGD VVALEQVPDE AFASKAVGDG IAVKPTDNIV
     VAPAAGTVVK IFNTNHAFCL ETNNGAEIVV HMGIDTVALE GKGFKRLVEE GTDVKAGEPI
     LEMDLDFLNA NARSMISPVV CSNSDDYSAL VILASGKVVA GQTPLYEIKG K
//