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YBHR_ECO57
ID   YBHR_ECO57              Reviewed;         368 AA.
AC   P0AFQ0; P75774; Q9ZBC6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Probable multidrug ABC transporter permease YbhR {ECO:0000250|UniProtKB:P0AFP9};
GN   Name=ybhR; OrderedLocusNames=Z1012, ECs0870;
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 YbhFSR that could be
CC       involved in efflux of cefoperazone. Probably involved in the
CC       translocation of the substrate across the membrane.
CC       {ECO:0000250|UniProtKB:P0AFP9}.
CC   -!- SUBUNIT: The complex is probably composed of two ATP-binding proteins
CC       (YbhF) and two transmembrane proteins (YbhR and YbhS).
CC       {ECO:0000250|UniProtKB:P0AFP9}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P0AFP9}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ABC-2 integral membrane protein family.
CC       {ECO:0000305}.
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DR   EMBL; AE005174; AAG55163.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34293.1; -; Genomic_DNA.
DR   PIR; F90737; F90737.
DR   RefSeq; NP_308897.1; NC_002695.1.
DR   RefSeq; WP_000469031.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AFQ0; -.
DR   SMR; P0AFQ0; -.
DR   STRING; 155864.EDL933_0913; -.
DR   EnsemblBacteria; AAG55163; AAG55163; Z1012.
DR   EnsemblBacteria; BAB34293; BAB34293; ECs_0870.
DR   GeneID; 66670936; -.
DR   GeneID; 917635; -.
DR   KEGG; ece:Z1012; -.
DR   KEGG; ecs:ECs_0870; -.
DR   PATRIC; fig|386585.9.peg.984; -.
DR   eggNOG; COG0842; Bacteria.
DR   HOGENOM; CLU_039483_8_3_6; -.
DR   OMA; WGQELIE; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR000412; ABC_2_transport.
DR   PRINTS; PR00164; ABC2TRNSPORT.
DR   PROSITE; PS51012; ABC_TM2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..368
FT                   /note="Probable multidrug ABC transporter permease YbhR"
FT                   /id="PRO_0000183003"
FT   TOPO_DOM        1..24
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..173
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        195..222
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..253
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        275..284
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        306..339
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        361..368
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP9"
FT   DOMAIN          129..366
FT                   /note="ABC transmembrane type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00442"
SQ   SEQUENCE   368 AA;  41566 MW;  CD9380B094EB86F2 CRC64;
     MFHRLWTLIR KELQSLLREP QTRAILILPV LIQVILFPFA ATLEVTNATI AIYDEDNGEH
     SVELTQRFAR ASAFTHVLLL KSPQEIRPTI DTQKALLLVR FPADFSRKLD TFQTAPLQLI
     LDGRNSNSAQ IAANYLQQIV KNYQQELLEG KPKPNNSELV VRNWYNPNLD YKWFVVPSLI
     AMITTIGVMI VTSLSVARER EQGTLDQLLV SPLTTWQIFI GKAVPALIVA TFQATIVLAI
     GIWAYQIPFA GSLALFYFTM VIYGLSLVGF GLLISSLCST QQQAFIGVFV FMMPAILLSG
     YVSPVENMPV WLQNLTWINP IRHFTDITKQ IYLKDASLDI VWNSLWPLLV ITATTGSAAY
     AMFRRKVM
 
 
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