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YBHR_SHIFL
ID   YBHR_SHIFL              Reviewed;         368 AA.
AC   P0AFQ1; P75774; Q9ZBC6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Probable multidrug ABC transporter permease YbhR {ECO:0000250|UniProtKB:P0AFP9};
GN   Name=ybhR; OrderedLocusNames=SF0742, S0783;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN42377.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16254.1; -; Genomic_DNA.
DR   RefSeq; NP_706670.1; NC_004337.2.
DR   RefSeq; WP_000469031.1; NZ_WPGW01000030.1.
DR   AlphaFoldDB; P0AFQ1; -.
DR   SMR; P0AFQ1; -.
DR   STRING; 198214.SF0742; -.
DR   EnsemblBacteria; AAN42377; AAN42377; SF0742.
DR   EnsemblBacteria; AAP16254; AAP16254; S0783.
DR   GeneID; 1023708; -.
DR   GeneID; 66670936; -.
DR   KEGG; sfl:SF0742; -.
DR   KEGG; sfx:S0783; -.
DR   PATRIC; fig|198214.7.peg.863; -.
DR   HOGENOM; CLU_039483_8_3_6; -.
DR   OMA; WGQELIE; -.
DR   OrthoDB; 1552415at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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_0000183004"
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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