PTWC_STRCO
ID PTWC_STRCO Reviewed; 416 AA.
AC Q9S2H4;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=PTS system N-acetylglucosamine-specific EIIC component {ECO:0000305};
DE Short=PTS system GlcNAc-specific EIIC component {ECO:0000305};
DE AltName: Full=GlcNAc-specific transporter {ECO:0000303|PubMed:16925557};
DE AltName: Full=N-acetylglucosamine permease IIC component {ECO:0000305};
DE Short=GlcNAc permease IIC component {ECO:0000305};
GN Name=nagE2 {ECO:0000303|PubMed:16925557};
GN OrderedLocusNames=SCO2907 {ECO:0000312|EMBL:CAB50988.1};
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, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=16925557; DOI=10.1111/j.1365-2958.2006.05319.x;
RA Rigali S., Nothaft H., Noens E.E.E., Schlicht M., Colson S., Mueller M.,
RA Joris B., Koerten H.K., Hopwood D.A., Titgemeyer F., van Wezel G.P.;
RT "The sugar phosphotransferase system of Streptomyces coelicolor is
RT regulated by the GntR-family regulator DasR and links N-acetylglucosamine
RT metabolism to the control of development.";
RL Mol. Microbiol. 61:1237-1251(2006).
RN [3]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, 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 (PubMed:16925557, PubMed:20487300). High-affinity permease, which
CC exhibits a narrow specificity for GlcNAc (PubMed:20487300). Essential
CC for C-signaling between vegetative growth and development
CC (PubMed:20487300). {ECO:0000269|PubMed:16925557,
CC ECO:0000269|PubMed:20487300}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 uM for GlcNAc {ECO:0000269|PubMed:20487300};
CC Vmax=0.55 nmol/min/mg enzyme {ECO:0000269|PubMed:20487300};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
CC -!- INDUCTION: Induced by GlcNAc (PubMed:20487300). Transcriptionally
CC activated by AtrA (PubMed:20487300). Expression is repressed by DasR in
CC the absence of glucosamine 6-P (GlcN6P) (PubMed:16925557).
CC {ECO:0000269|PubMed:16925557, ECO:0000269|PubMed:20487300}.
CC -!- DOMAIN: The EIIC domain type-1 forms the PTS system translocation
CC channel and contains the specific substrate-binding site.
CC {ECO:0000255|PROSITE-ProRule:PRU00426}.
CC -!- DISRUPTION PHENOTYPE: Mutant is unable to grow on GlcNAc, while growth
CC on glucose, fructose, xylose, mannose, sucrose or galactose is not
CC impaired (PubMed:20487300). Mutant is insensitive to GlcNAc
CC (PubMed:16925557, PubMed:20487300). {ECO:0000269|PubMed:16925557,
CC ECO:0000269|PubMed:20487300}.
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DR EMBL; AL939114; CAB50988.1; -; Genomic_DNA.
DR PIR; T36130; T36130.
DR RefSeq; NP_627133.1; NC_003888.3.
DR RefSeq; WP_011028657.1; NZ_VNID01000010.1.
DR AlphaFoldDB; Q9S2H4; -.
DR SMR; Q9S2H4; -.
DR STRING; 100226.SCO2907; -.
DR TCDB; 4.A.1.1.20; the pts glucose-glucoside (glc) family.
DR GeneID; 1098340; -.
DR KEGG; sco:SCO2907; -.
DR PATRIC; fig|100226.15.peg.2966; -.
DR eggNOG; COG1263; Bacteria.
DR HOGENOM; CLU_012312_1_0_11; -.
DR InParanoid; Q9S2H4; -.
DR OMA; ETDATIM; -.
DR PhylomeDB; Q9S2H4; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphotransferase system; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..416
FT /note="PTS system N-acetylglucosamine-specific EIIC
FT component"
FT /id="PRO_0000447882"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00426"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00426"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00426"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00426"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00426"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00426"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00426"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00426"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00426"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00426"
FT DOMAIN 16..406
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
SQ SEQUENCE 416 AA; 44168 MW; 5A9240CDDDBD1572 CRC64;
MSTATDTAAP AKKRGSGLFQ GLQKVGRSLQ LPIAVLPAAG IMVRLGQDDI FGKDGLGWDK
VAAVFNNAGG ALTGSLPILF CIGVAIGFAK KADGSTALAA VVGFLVYSKV LEAFPVTEAV
VQDGADVAAT YNDPGVLGGI IMGLLAAVLW QRYHRKKLVD WLGFFNGRRL VPIIMAFVGI
VVGVFFGLVW EPIGDGISNF GEWMTGLGSG GAALFGGVNR ALIPVGMHQF VNTVAWFQLG
DFTNSAGDVV HGDITRFLAG DPSAGIFQAG FFPIMMFGLP AAALAMAHTA RPERRKAVLG
MMISLAATSF VTGVTEPIEF SFMFIAPVLY VLHAVLTAIS MAITWGLGVH AGFNFSAGFI
DYALNWHLAT KPWLIIPIGL VFAAIYYVTF RFAIVKFNLK TPGREPEEEV EDLTKA
