PTW3C_KLEPN
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 03-AUG-2022, entry version 121.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
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) = 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: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 PRIDE; P45604; -.
DR BRENDA; 2.7.1.193; 2814.
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:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
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 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
