PTWB_STRCO
ID PTWB_STRCO Reviewed; 77 AA.
AC Q9S2H6;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=PTS system N-acetylglucosamine-specific EIIB component {ECO:0000305};
DE Short=PTS system GlcNAc-specific EIIB component {ECO:0000305};
DE EC=2.7.1.193 {ECO:0000269|PubMed:20487300};
DE AltName: Full=N-acetylglucosamine-specific phosphotransferase enzyme IIB component {ECO:0000305};
DE Short=GlcNAc-specific phosphotransferase enzyme IIB component {ECO:0000305};
GN Name=nagF {ECO:0000303|PubMed:20487300};
GN Synonyms=malX2 {ECO:0000305|PubMed:20487300};
GN OrderedLocusNames=SCO2905 {ECO:0000312|EMBL:CAB50986.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=20487300; DOI=10.1111/j.1365-2958.2009.07020.x;
RA Nothaft H., Rigali S., Boomsma B., Swiatek M., McDowall K.J.,
RA van Wezel G.P., Titgemeyer F.;
RT "The permease gene nagE2 is the key to N-acetylglucosamine sensing and
RT utilization in Streptomyces coelicolor and is subject to multi-level
RT control.";
RL Mol. Microbiol. 75:1133-1144(2010).
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 (GlcNAc) transport.
CC {ECO:0000269|PubMed:20487300}.
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:20487300};
CC -!- INDUCTION: Induced by GlcNAc. {ECO:0000269|PubMed:20487300}.
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 -!- DISRUPTION PHENOTYPE: Mutant is insensitive to GlcNAc.
CC {ECO:0000269|PubMed:20487300}.
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DR EMBL; AL939114; CAB50986.1; -; Genomic_DNA.
DR PIR; T36128; T36128.
DR RefSeq; NP_627131.1; NC_003888.3.
DR RefSeq; WP_003975905.1; NZ_VNID01000010.1.
DR AlphaFoldDB; Q9S2H6; -.
DR SMR; Q9S2H6; -.
DR STRING; 100226.SCO2905; -.
DR TCDB; 4.A.1.1.20; the pts glucose-glucoside (glc) family.
DR GeneID; 1098338; -.
DR KEGG; sco:SCO2905; -.
DR PATRIC; fig|100226.15.peg.2964; -.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_8_4_11; -.
DR OMA; DIEACIT; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0015764; P:N-acetylglucosamine transport; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00212; PTS_IIB_glc; 1.
DR Gene3D; 3.30.1360.60; -; 1.
DR InterPro; IPR036878; Glu_permease_IIB.
DR InterPro; IPR018113; PTrfase_EIIB_Cys.
DR InterPro; IPR001996; PTS_IIB_1.
DR Pfam; PF00367; PTS_EIIB; 1.
DR SUPFAM; SSF55604; SSF55604; 1.
DR TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Kinase; Phosphoprotein; Phosphotransferase system; Reference proteome;
KW Sugar transport; Transferase; Transport.
FT CHAIN 1..77
FT /note="PTS system N-acetylglucosamine-specific EIIB
FT component"
FT /id="PRO_0000447881"
FT DOMAIN 2..77
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 24
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 77 AA; 7904 MW; 73BCE07AE4102D81 CRC64;
MASKAEKIVA GLGGIDNIDE IEGCITRLRT EVNDPALVNE AALKAAGAHG VVKMGTAIQV
VIGTDADPIA AEIEDMM
