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CSCB_ECOLX
ID   CSCB_ECOLX              Reviewed;         415 AA.
AC   P30000;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Sucrose permease {ECO:0000303|PubMed:7535526};
DE   AltName: Full=Sucrose transport protein {ECO:0000305};
GN   Name=cscB {ECO:0000303|PubMed:1435727};
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EC3132;
RX   PubMed=1435727; DOI=10.1007/bf00286177;
RA   Bockmann J., Heuel H., Lengeler J.W.;
RT   "Characterization of a chromosomally encoded, non-PTS metabolic pathway for
RT   sucrose utilization in Escherichia coli EC3132.";
RL   Mol. Gen. Genet. 235:22-32(1992).
RN   [2]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX   PubMed=7535526; DOI=10.1006/bbrc.1995.1449;
RA   Sahin-Toth M., Frillingos S., Lengeler J.W., Kaback H.R.;
RT   "Active transport by the CscB permease in Escherichia coli K-12.";
RL   Biochem. Biophys. Res. Commun. 208:1116-1123(1995).
RN   [3]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19294451; DOI=10.1007/s00232-009-9161-9;
RA   Peng Y., Kumar S., Hernandez R.L., Jones S.E., Cadle K.M., Smith K.P.,
RA   Varela M.F.;
RT   "Evidence for the transport of maltose by the sucrose permease, CscB, of
RT   Escherichia coli.";
RL   J. Membr. Biol. 228:79-88(2009).
RN   [4]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=22106930; DOI=10.1021/bi201592y;
RA   Sugihara J., Smirnova I., Kasho V., Kaback H.R.;
RT   "Sugar recognition by CscB and LacY.";
RL   Biochemistry 50:11009-11014(2011).
CC   -!- FUNCTION: Responsible for transport of sucrose into the cell, with the
CC       concomitant import of a proton (symport system) (PubMed:7535526,
CC       PubMed:22106930). Can also transport maltose, fructose or lactulose,
CC       but not glucose, lactose or melibiose (PubMed:19294451, PubMed:7535526,
CC       PubMed:22106930). The substrate specificity is directed toward the
CC       fructofuranosyl moiety of the substrate (PubMed:22106930).
CC       {ECO:0000269|PubMed:19294451, ECO:0000269|PubMed:22106930,
CC       ECO:0000269|PubMed:7535526}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1 mM for sucrose {ECO:0000269|PubMed:7535526};
CC         KM=0.37 mM for sucrose {ECO:0000269|PubMed:19294451};
CC         KM=0.59 mM for maltose {ECO:0000269|PubMed:19294451};
CC         KM=6.7 mM for sucrose {ECO:0000269|PubMed:22106930};
CC         KM=36 mM for fructose {ECO:0000269|PubMed:22106930};
CC         Vmax=23 nmol/min/mg enzyme with sucrose as substrate
CC         {ECO:0000269|PubMed:7535526};
CC         Vmax=83 nmol/min/mg enzyme with sucrose as substrate
CC         {ECO:0000269|PubMed:19294451};
CC         Vmax=111 nmol/min/mg enzyme with maltose as substrate
CC         {ECO:0000269|PubMed:19294451};
CC         Vmax=130 nmol/min/mg enzyme with sucrose as substrate
CC         {ECO:0000269|PubMed:22106930};
CC         Vmax=60 nmol/min/mg enzyme with fructose as substrate
CC         {ECO:0000269|PubMed:22106930};
CC   -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:7535526};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       Oligosaccharide:H(+) symporter (OHS) (TC 2.A.1.5) family.
CC       {ECO:0000305}.
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DR   EMBL; X63740; CAA45274.1; -; Genomic_DNA.
DR   EMBL; X81461; CAA57217.1; -; Genomic_DNA.
DR   PIR; S30107; GRECST.
DR   RefSeq; WP_001197021.1; NZ_WVUW01000001.1.
DR   AlphaFoldDB; P30000; -.
DR   SMR; P30000; -.
DR   STRING; 585034.ECIAI1_2426; -.
DR   TCDB; 2.A.1.5.3; the major facilitator superfamily (mfs).
DR   OrthoDB; 791272at2; -.
DR   UniPathway; UPA00238; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR   GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.1250.20; -; 2.
DR   InterPro; IPR000576; LacY/RafB_perm_fam.
DR   InterPro; IPR018457; LacY/RafB_perm_fam_CS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF01306; LacY_symp; 1.
DR   PRINTS; PR00174; LACYSMPORT.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00882; 2A0105; 1.
DR   PROSITE; PS00896; LACY_1; 1.
DR   PROSITE; PS00897; LACY_2; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Sugar transport; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..415
FT                   /note="Sucrose permease"
FT                   /id="PRO_0000196188"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..48
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        70..77
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        99..107
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..147
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        148..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        168..170
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        171..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        191..220
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        242..260
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        282..287
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        309..311
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..342
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        364..377
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        399..415
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   415 AA;  46924 MW;  D05BBD305B61AC22 CRC64;
     MALNIPFRNA YYRFASSYSF LFFISWSLWW SLYAIWLKGH LGLTGTELGT LYSVNQFTSI
     LFMMFYGIVQ DKLGLKKPLI WCMSFILVLT GPFMIYVYEP LLQSNFSVGL ILGALFFGLG
     YLAGCGLLDS FTEKMARNFH FEYGTARAWG SFGYAIGAFF AGIFFSISPH INFWLVSLFG
     AVFMMINMRF KDKDHQCIAA DAGGVKKEDF IAVFKDRNFW VFVIFIVGTW SFYNIFDQQL
     FPVFYAGLFE SHDVGTRLYG YLNSFQVVLE ALCMAIIPFF VNRVGPKNAL LIGVVIMALR
     ILSCALFVNP WIISLVKLLH AIEVPLCVIS VFKYSVANFD KRLSSTIFLI GFQIASSLGI
     VLLSTPTGIL FDHAGYQTVF FAISGIVCLM LLFGIFFLSK KREQIVMETP VPSAI
 
 
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