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EXBD_ECOLI
ID   EXBD_ECOLI              Reviewed;         141 AA.
AC   P0ABV2; P18784; Q2M9J3;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Biopolymer transport protein ExbD;
GN   Name=exbD; OrderedLocusNames=b3005, JW2973;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2670903; DOI=10.1128/jb.171.9.5117-5126.1989;
RA   Eick-Helmerich K., Braun V.;
RT   "Import of biopolymers into Escherichia coli: nucleotide sequences of the
RT   exbB and exbD genes are homologous to those of the tolQ and tolR genes,
RT   respectively.";
RL   J. Bacteriol. 171:5117-5126(1989).
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   TOPOLOGY.
RX   PubMed=1644779; DOI=10.1128/jb.174.16.5485-5487.1992;
RA   Kampfenkel K., Braun V.;
RT   "Membrane topology of the Escherichia coli ExbD protein.";
RL   J. Bacteriol. 174:5485-5487(1992).
RN   [5]
RP   INDUCTION BY HYDROXYUREA.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA   Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA   Walker G.C.;
RT   "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT   coli.";
RL   Mol. Cell 36:845-860(2009).
CC   -!- FUNCTION: Involved in the TonB-dependent energy-dependent transport of
CC       various receptor-bound substrates.
CC   -!- SUBUNIT: The accessory proteins ExbB and ExbD seem to form a complex
CC       with TonB.
CC   -!- INTERACTION:
CC       P0ABV2; P0ABU7: exbB; NbExp=7; IntAct=EBI-6417016, EBI-6399986;
CC       P0ABV2; P0ABV2: exbD; NbExp=3; IntAct=EBI-6417016, EBI-6417016;
CC       P0ABV2; P02929: tonB; NbExp=3; IntAct=EBI-6417016, EBI-6399993;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane
CC       protein.
CC   -!- INDUCTION: Induced 2.1-fold by hydroxyurea.
CC       {ECO:0000269|PubMed:20005847}.
CC   -!- SIMILARITY: Belongs to the ExbD/TolR family. {ECO:0000305}.
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DR   EMBL; M28819; AAA23733.1; -; Genomic_DNA.
DR   EMBL; U28377; AAA69172.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76041.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77063.1; -; Genomic_DNA.
DR   PIR; JV0030; BVECED.
DR   RefSeq; NP_417478.1; NC_000913.3.
DR   RefSeq; WP_001240712.1; NZ_STEB01000001.1.
DR   PDB; 2PFU; NMR; -; A=44-141.
DR   PDB; 5SV1; X-ray; 3.50 A; Y/Z=1-49.
DR   PDB; 5ZFU; EM; 6.70 A; G/H/I=19-40.
DR   PDB; 5ZFV; EM; 7.10 A; F=19-40.
DR   PDB; 6TYI; EM; 3.30 A; Y/Z=1-141.
DR   PDBsum; 2PFU; -.
DR   PDBsum; 5SV1; -.
DR   PDBsum; 5ZFU; -.
DR   PDBsum; 5ZFV; -.
DR   PDBsum; 6TYI; -.
DR   AlphaFoldDB; P0ABV2; -.
DR   BMRB; P0ABV2; -.
DR   SMR; P0ABV2; -.
DR   BioGRID; 4261413; 269.
DR   BioGRID; 850702; 2.
DR   ComplexPortal; CPX-1083; Cobalamin outer membrane transporter complex.
DR   ComplexPortal; CPX-2843; Ferrichrome outer membrane transporter complex.
DR   ComplexPortal; CPX-3576; Ferric-citrate outer membrane transporter complex.
DR   ComplexPortal; CPX-3577; Ferric-catecholate outer membrane transporter complex.
DR   ComplexPortal; CPX-3578; Ferric-enterobactin outer membrane transporter complex.
DR   ComplexPortal; CPX-3579; Ferric-coprogen outer membrane transporter complex.
DR   ComplexPortal; CPX-3580; fiu outer membrane transporter complex.
DR   ComplexPortal; CPX-3585; Uncharacterized yncD-DHBS outer membrane transporter complex.
DR   DIP; DIP-47973N; -.
DR   IntAct; P0ABV2; 4.
DR   STRING; 511145.b3005; -.
DR   TCDB; 1.A.30.2.1; the h(+)- or na(+)-translocating bacterial flagellar motor/exbbd outer membrane transport energizer (mot/exb) superfamily.
DR   jPOST; P0ABV2; -.
DR   PaxDb; P0ABV2; -.
DR   PRIDE; P0ABV2; -.
DR   EnsemblBacteria; AAC76041; AAC76041; b3005.
DR   EnsemblBacteria; BAE77063; BAE77063; BAE77063.
DR   GeneID; 67415049; -.
DR   GeneID; 946345; -.
DR   KEGG; ecj:JW2973; -.
DR   KEGG; eco:b3005; -.
DR   PATRIC; fig|1411691.4.peg.3724; -.
DR   EchoBASE; EB0268; -.
DR   eggNOG; COG0848; Bacteria.
DR   HOGENOM; CLU_085305_1_3_6; -.
DR   InParanoid; P0ABV2; -.
DR   OMA; TQGKKDT; -.
DR   PhylomeDB; P0ABV2; -.
DR   BioCyc; EcoCyc:EG10272-MON; -.
DR   BioCyc; MetaCyc:EG10272-MON; -.
DR   EvolutionaryTrace; P0ABV2; -.
DR   PRO; PR:P0ABV2; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IC:ComplexPortal.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR   GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0098797; C:plasma membrane protein complex; IDA:EcoCyc.
DR   GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
DR   GO; GO:0031992; F:energy transducer activity; IMP:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0043213; P:bacteriocin transport; IEA:UniProtKB-KW.
DR   GO; GO:0015889; P:cobalamin transport; IC:ComplexPortal.
DR   GO; GO:0055072; P:iron ion homeostasis; IC:ComplexPortal.
DR   GO; GO:0055065; P:metal ion homeostasis; IC:ComplexPortal.
DR   GO; GO:0050821; P:protein stabilization; IMP:EcoCyc.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003400; ExbD.
DR   InterPro; IPR014170; TonB_ExbD_1.
DR   PANTHER; PTHR30558; PTHR30558; 1.
DR   Pfam; PF02472; ExbD; 1.
DR   TIGRFAMs; TIGR02803; ExbD_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Bacteriocin transport; Cell inner membrane; Cell membrane;
KW   Membrane; Protein transport; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..141
FT                   /note="Biopolymer transport protein ExbD"
FT                   /id="PRO_0000129117"
FT   TOPO_DOM        1..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:1644779"
FT   TRANSMEM        23..43
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        44..141
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:1644779"
FT   HELIX           21..36
FT                   /evidence="ECO:0007829|PDB:6TYI"
FT   HELIX           39..41
FT                   /evidence="ECO:0007829|PDB:6TYI"
FT   STRAND          65..69
FT                   /evidence="ECO:0007829|PDB:2PFU"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:2PFU"
FT   STRAND          73..76
FT                   /evidence="ECO:0007829|PDB:2PFU"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:2PFU"
FT   HELIX           86..93
FT                   /evidence="ECO:0007829|PDB:2PFU"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:2PFU"
FT   STRAND          102..106
FT                   /evidence="ECO:0007829|PDB:2PFU"
FT   HELIX           112..124
FT                   /evidence="ECO:0007829|PDB:2PFU"
SQ   SEQUENCE   141 AA;  15527 MW;  25A539A2FAEB9F6C CRC64;
     MAMHLNENLD DNGEMHDINV TPFIDVMLVL LIIFMVAAPL ATVDVKVNLP ASTSTPQPRP
     EKPVYLSVKA DNSMFIGNDP VTDETMITAL NALTEGKKDT TIFFRADKTV DYETLMKVMD
     TLHQAGYLKI GLVGEETAKA K
 
 
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