ID   NGCE_STRCO              Reviewed;         469 AA.
AC   O50499;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Diacetylchitobiose binding protein NgcE {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ngcE {ECO:0000303|PubMed:30089751};
GN   OrderedLocusNames=SCO6005 {ECO:0000312|EMBL:CAA15782.1};
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, SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=30089751; DOI=10.1264/jsme2.me17172;
RA   Iinuma C., Saito A., Ohnuma T., Tenconi E., Rosu A., Colson S.,
RA   Mizutani Y., Liu F., Swiatek-Polatynska M., van Wezel G.P., Rigali S.,
RA   Fujii T., Miyashita K.;
RT   "NgcESco acts as a lower-affinity binding protein of an ABC transporter for
RT   the uptake of N,N'-diacetylchitobiose in Streptomyces coelicolor A3(2).";
RL   Microbes Environ. 33:272-281(2018).
CC   -!- FUNCTION: Part of the ABC transporter complex NgcEFG-MsiK involved in
CC       N,N'-diacetylchitobiose ((GlcNAc)2) uptake. Binds (GlcNAc)2. Can also
CC       bind GlcNAc. {ECO:0000269|PubMed:30089751}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MsiK),
CC       two transmembrane proteins (NgcF and NgcG) and a solute-binding protein
CC       (NgcE). {ECO:0000305|PubMed:30089751}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}.
CC   -!- INDUCTION: Constitutively expressed. Slightly induced by GlcNAc,
CC       (GlcNAc)2 and chitin. Repressed by DasR. {ECO:0000269|PubMed:30089751}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC       {ECO:0000255|PROSITE-ProRule:PRU00648}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene delays (GlcNAc)2
CC       consumption, but does not affect GlcNAc consumption ability. Deletion
CC       reduces the level of chitinase activity induced in the presence of
CC       (GlcNAc)2. {ECO:0000269|PubMed:30089751}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AL939126; CAA15782.1; -; Genomic_DNA.
DR   PIR; T35670; T35670.
DR   RefSeq; NP_630119.1; NC_003888.3.
DR   RefSeq; WP_011030591.1; NZ_VNID01000007.1.
DR   AlphaFoldDB; O50499; -.
DR   SMR; O50499; -.
DR   STRING; 100226.SCO6005; -.
DR   GeneID; 1101447; -.
DR   KEGG; sco:SCO6005; -.
DR   PATRIC; fig|100226.15.peg.6103; -.
DR   eggNOG; COG1653; Bacteria.
DR   HOGENOM; CLU_047233_0_0_11; -.
DR   OMA; VYGVWYS; -.
DR   PhylomeDB; O50499; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   InterPro; IPR022386; Chitin_NgcE.
DR   InterPro; IPR006059; SBP.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF01547; SBP_bac_1; 1.
DR   TIGRFAMs; TIGR03851; chitin_NgcE; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome; Signal; Sugar transport;
KW   Transport.
FT   SIGNAL          1..37
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           38..469
FT                   /note="Diacetylchitobiose binding protein NgcE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT                   /id="PRO_5004159544"
FT   REGION          30..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   469 AA;  50611 MW;  E1C4B383BA8C8B52 CRC64;
     MTIRAGSLDR RTLLRGAIAT AAMGSFAVAC SSPSSEDKES DSGPKGEKSA NNPFGAAANS
     TVEAAIFDGG YGTDYVDYAN QVLGSQVKGL KVQVKPVVDI APQLQPRFVG GNPPDLIDNS
     GEDQIGFLGI LDQLEELDDL FEASTYEGKK IADIVYPGVK DPGTFKDKFV ALNYVMTVYG
     VWYSKTLFEE NGWTPPKTWD EALDLGQEAK KKGKYLFVHG KEAATYYRTL LIDSAIKEGG
     DEVRLALENL EKGCWSHPAV QGVIKVMETM VKQKMFVPGG SGTQFQKAQA IWSNDQKALL
     YPSGGWIENE MKKATKADFQ MTGIPSMTLT DKPALPYEAL RAAAGEPFIV PKQGKNPAGG
     KEVLRAMLSE KAAANFSKTK LAPTIVKGTV PADGYGSTAL VSQTKMLEAA GTNIFNYMFV
     ETYGLNTDQL VPWNSFLAGD LDGKGLTSAL QKISDKVRED DSVDKVKVS