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BIOP_ECOLI
ID   BIOP_ECOLI              Reviewed;         299 AA.
AC   P0ADP5; P27849; Q2M8D2; Q8X5G7;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Biotin transporter {ECO:0000303|Ref.5};
DE   AltName: Full=Plasmamembrane biotin transport protein {ECO:0000303|Ref.5};
GN   Name=bioP {ECO:0000303|PubMed:1091631}; Synonyms=yigM;
GN   OrderedLocusNames=b3827, JW3803;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=1379743; DOI=10.1126/science.1379743;
RA   Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT   84.5 to 86.5 minutes.";
RL   Science 257:771-778(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   DISRUPTION PHENOTYPE, AND GENE NAME.
RX   PubMed=1091631; DOI=10.1128/jb.122.1.66-72.1975;
RA   Eisenburg M.A., Mee B., Prakash O., Eisenburg M.R.;
RT   "Properties of alpha-dehydrobiotin-resistant mutants of Escherichia coli K-
RT   12.";
RL   J. Bacteriol. 122:66-72(1975).
RN   [5]
RP   FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RA   Ringlstetter S.L.;
RT   "Identification of the biotin transporter in Escherichia coli,
RT   biotinylation of histones in Saccharomyces cerevisiae and analysis of
RT   biotin sensing in Saccharomyces cerevisiae.";
RL   Thesis (2011), University of Regensburg, Germany.
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=24256712; DOI=10.4161/bioe.26887;
RA   Finkenwirth F., Kirsch F., Eitinger T.;
RT   "A versatile Escherichia coli strain for identification of biotin
RT   transporters and for biotin quantification.";
RL   Bioengineered 5:129-132(2014).
CC   -!- FUNCTION: Uptake of biotin. Acts probably by facilitated diffusion.
CC       {ECO:0000269|Ref.5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=biotin(in) = biotin(out); Xref=Rhea:RHEA:28458,
CC         ChEBI:CHEBI:57586; Evidence={ECO:0000305|Ref.5};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28460;
CC         Evidence={ECO:0000305|Ref.5};
CC   -!- ACTIVITY REGULATION: Biotin uptake is weakly inhibited by CCCP and FCCP
CC       protonophores and by the respiratory chain blocker NaN(3).
CC       {ECO:0000269|Ref.5}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=74 nM for biotin {ECO:0000269|Ref.5};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|Ref.5}; Multi-
CC       pass membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is repressed by biotin. {ECO:0000269|Ref.5}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene abolishes biotin uptake
CC       (Ref.5, PubMed:1091631). BioH-bioP double mutant is unable to grow on
CC       trace levels of biotin (PubMed:24256712). {ECO:0000269|PubMed:1091631,
CC       ECO:0000269|PubMed:24256712, ECO:0000269|Ref.5}.
CC   -!- SIMILARITY: Belongs to the drug/metabolite transporter (DMT)
CC       superfamily. 10 TMS drug/metabolite exporter (DME) (TC 2.A.7.3) family.
CC       {ECO:0000305}.
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DR   EMBL; M87049; AAA67623.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76830.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77474.1; -; Genomic_DNA.
DR   PIR; D65187; D65187.
DR   RefSeq; NP_418271.1; NC_000913.3.
DR   RefSeq; WP_001196238.1; NZ_STEB01000021.1.
DR   AlphaFoldDB; P0ADP5; -.
DR   SMR; P0ADP5; -.
DR   BioGRID; 4259475; 5.
DR   STRING; 511145.b3827; -.
DR   TCDB; 2.A.7.3.61; the drug/metabolite transporter (dmt) superfamily.
DR   PaxDb; P0ADP5; -.
DR   PRIDE; P0ADP5; -.
DR   EnsemblBacteria; AAC76830; AAC76830; b3827.
DR   EnsemblBacteria; BAE77474; BAE77474; BAE77474.
DR   GeneID; 66672265; -.
DR   GeneID; 948309; -.
DR   KEGG; ecj:JW3803; -.
DR   KEGG; eco:b3827; -.
DR   PATRIC; fig|511145.12.peg.3943; -.
DR   EchoBASE; EB1439; -.
DR   eggNOG; COG0697; Bacteria.
DR   HOGENOM; CLU_085269_0_0_6; -.
DR   InParanoid; P0ADP5; -.
DR   OMA; RFNPWAL; -.
DR   PhylomeDB; P0ADP5; -.
DR   BioCyc; EcoCyc:EG11471-MON; -.
DR   BioCyc; MetaCyc:EG11471-MON; -.
DR   PRO; PR:P0ADP5; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   InterPro; IPR004779; CO/AA/NH_transpt.
DR   InterPro; IPR000620; EamA_dom.
DR   Pfam; PF00892; EamA; 2.
DR   TIGRFAMs; TIGR00950; 2A78; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..299
FT                   /note="Biotin transporter"
FT                   /id="PRO_0000169663"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          3..128
FT                   /note="EamA 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          139..274
FT                   /note="EamA 2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   299 AA;  33727 MW;  2AF656D013405165 CRC64;
     MALLIITTIL WAFSFSFYGE YLAGHVDSYF AVLVRVGLAA LVFLPFLRTR GNSLKTVGLY
     MLVGAMQLGV MYMLSFRAYL YLTVSELLLF TVLTPLYITL IYDIMSKRRL RWGYAFSALL
     AVIGAGIIRY DQVTDHFWTG LLLVQLSNIT FAIGMVGYKR LMETRPMPQH NAFAWFYLGA
     FLVAVIAWFL LGNAQKMPQT TLQWGILVFL GVVASGIGYF MWNYGATQVD AGTLGIMNNM
     HVPAGLLVNL AIWHQQPHWP TFITGALVIL ASLWVHRKWV APRSSQTADD RRRDCALSE
 
 
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