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RBSC_ECO57
ID   RBSC_ECO57              Reviewed;         321 AA.
AC   P0AGI3; P04984;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Ribose import permease protein RbsC {ECO:0000250|UniProtKB:P0AGI1};
GN   Name=rbsC; OrderedLocusNames=Z5251, ECs4692;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose
CC       import. Probably responsible for the translocation of the substrate
CC       across the membrane. {ECO:0000250|UniProtKB:P0AGI1}.
CC   -!- SUBUNIT: The complex is composed of an ATP-binding protein (RbsA), two
CC       transmembrane proteins (RbsC) and a solute-binding protein (RbsB).
CC       {ECO:0000250|UniProtKB:P0AGI1}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P0AGI1}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P0AGI1}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. AraH/RbsC subfamily. {ECO:0000305}.
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DR   EMBL; AE005174; AAG58953.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38115.1; -; Genomic_DNA.
DR   PIR; D91215; D91215.
DR   RefSeq; NP_312719.1; NC_002695.1.
DR   RefSeq; WP_000211858.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AGI3; -.
DR   STRING; 155864.EDL933_5080; -.
DR   PRIDE; P0AGI3; -.
DR   EnsemblBacteria; AAG58953; AAG58953; Z5251.
DR   EnsemblBacteria; BAB38115; BAB38115; ECs_4692.
DR   GeneID; 67417737; -.
DR   GeneID; 915328; -.
DR   KEGG; ece:Z5251; -.
DR   KEGG; ecs:ECs_4692; -.
DR   PATRIC; fig|386585.9.peg.4898; -.
DR   eggNOG; COG1172; Bacteria.
DR   HOGENOM; CLU_028880_2_2_6; -.
DR   OMA; FDVWNKR; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001851; ABC_transp_permease.
DR   Pfam; PF02653; BPD_transp_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..321
FT                   /note="Ribose import permease protein RbsC"
FT                   /id="PRO_0000060224"
FT   TOPO_DOM        1..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGI1"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGI1"
FT   TOPO_DOM        44..56
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGI1"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGI1"
FT   TOPO_DOM        78..125
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGI1"
FT   TRANSMEM        126..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGI1"
FT   TOPO_DOM        146..168
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGI1"
FT   TRANSMEM        169..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGI1"
FT   TOPO_DOM        191..220
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGI1"
FT   TRANSMEM        221..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGI1"
FT   TOPO_DOM        241..294
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGI1"
FT   TRANSMEM        295..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGI1"
FT   TOPO_DOM        317..321
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGI1"
SQ   SEQUENCE   321 AA;  33452 MW;  C7292EE5F0C78781 CRC64;
     MTTQTVSGRR YFTKAWLMEQ KSLIALLVLI AIVSTLSPNF FTINNLFNIL QQTSVNAIMA
     VGMTLVILTS GIDLSVGSLL ALTGAVAASI VGIEVNALVA VAAALALGAA IGAVTGVIVA
     KGRVQAFIAT LVMMLLLRGV TMVYTNGSPV NTGFTENADL FGWFGIGRPL GVPTPVWIMG
     IVFLAAWYML HHTRLGRYIY ALGGNEAATR LSGINVNKIK IIVYSLCGLL ASLAGIIEVA
     RLSSAQPTAG TGYELDAIAA VVLGGTSLAG GKGRIVGTLI GALILGFLNN GLNLLGVSSY
     YQMIVKAVVI LLAVLVDNKK Q
 
 
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