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BTUD_ECOLI
ID   BTUD_ECOLI              Reviewed;         249 AA.
AC   P06611;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 185.
DE   RecName: Full=Vitamin B12 import ATP-binding protein BtuD {ECO:0000255|HAMAP-Rule:MF_01005};
DE            EC=7.6.2.8 {ECO:0000255|HAMAP-Rule:MF_01005};
DE   AltName: Full=Vitamin B12-transporting ATPase {ECO:0000255|HAMAP-Rule:MF_01005};
GN   Name=btuD {ECO:0000255|HAMAP-Rule:MF_01005};
GN   OrderedLocusNames=b1709, JW1699;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3528129; DOI=10.1128/jb.167.3.928-934.1986;
RA   Friedrich M.J., Deveaux L.C., Kadner R.J.;
RT   "Nucleotide sequence of the btuCED genes involved in vitamin B12 transport
RT   in Escherichia coli and homology with components of periplasmic-binding-
RT   protein-dependent transport systems.";
RL   J. Bacteriol. 167:928-934(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [3]
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   [4]
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   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH BTUC.
RX   PubMed=12004122; DOI=10.1126/science.1071142;
RA   Locher K.P., Lee A.T., Rees D.C.;
RT   "The E. coli BtuCD structure: a framework for ABC transporter architecture
RT   and mechanism.";
RL   Science 296:1091-1098(2002).
CC   -!- FUNCTION: Part of the ABC transporter complex BtuCDF involved in
CC       vitamin B12 import. Responsible for energy coupling to the transport
CC       system. {ECO:0000255|HAMAP-Rule:MF_01005}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an R-cob(III)alamin(out) + ATP + H2O = ADP + an R-
CC         cob(III)alamin(in) + H(+) + phosphate; Xref=Rhea:RHEA:17873,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:140785, ChEBI:CHEBI:456216;
CC         EC=7.6.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01005};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (BtuD),
CC       two transmembrane proteins (BtuC) and a solute-binding protein (BtuF).
CC       {ECO:0000255|HAMAP-Rule:MF_01005, ECO:0000269|PubMed:12004122}.
CC   -!- INTERACTION:
CC       P06611; P06609: btuC; NbExp=13; IntAct=EBI-1033420, EBI-1033427;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Vitamin B12
CC       importer (TC 3.A.1.13.1) family. {ECO:0000255|HAMAP-Rule:MF_01005}.
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DR   EMBL; M14031; AAA23528.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74779.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15477.1; -; Genomic_DNA.
DR   PIR; C24498; QRECBD.
DR   RefSeq; NP_416224.1; NC_000913.3.
DR   RefSeq; WP_000029474.1; NZ_LN832404.1.
DR   PDB; 1L7V; X-ray; 3.20 A; C/D=1-249.
DR   PDB; 2QI9; X-ray; 2.60 A; C/D=1-249.
DR   PDB; 4DBL; X-ray; 3.49 A; C/D/H/I=1-249.
DR   PDB; 4FI3; X-ray; 3.47 A; C/D=1-249.
DR   PDB; 4R9U; X-ray; 2.78 A; C/D=1-249.
DR   PDBsum; 1L7V; -.
DR   PDBsum; 2QI9; -.
DR   PDBsum; 4DBL; -.
DR   PDBsum; 4FI3; -.
DR   PDBsum; 4R9U; -.
DR   AlphaFoldDB; P06611; -.
DR   SMR; P06611; -.
DR   BioGRID; 4260301; 185.
DR   ComplexPortal; CPX-2105; Cobalamin ABC transporter complex.
DR   ComplexPortal; CPX-2106; BtuCD complex.
DR   DIP; DIP-9234N; -.
DR   IntAct; P06611; 9.
DR   MINT; P06611; -.
DR   STRING; 511145.b1709; -.
DR   TCDB; 3.A.1.13.1; the atp-binding cassette (abc) superfamily.
DR   jPOST; P06611; -.
DR   PaxDb; P06611; -.
DR   PRIDE; P06611; -.
DR   EnsemblBacteria; AAC74779; AAC74779; b1709.
DR   EnsemblBacteria; BAA15477; BAA15477; BAA15477.
DR   GeneID; 945751; -.
DR   KEGG; ecj:JW1699; -.
DR   KEGG; eco:b1709; -.
DR   PATRIC; fig|1411691.4.peg.548; -.
DR   EchoBASE; EB0126; -.
DR   eggNOG; COG4138; Bacteria.
DR   HOGENOM; CLU_000604_1_11_6; -.
DR   InParanoid; P06611; -.
DR   OMA; HHADRVW; -.
DR   PhylomeDB; P06611; -.
DR   BioCyc; EcoCyc:BTUD-MON; -.
DR   BioCyc; MetaCyc:BTUD-MON; -.
DR   BRENDA; 7.6.2.8; 2026.
DR   EvolutionaryTrace; P06611; -.
DR   PRO; PR:P06611; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:EcoCyc.
DR   GO; GO:1990191; C:cobalamin transport complex; IPI:ComplexPortal.
DR   GO; GO:0019898; C:extrinsic component of membrane; IDA:EcoliWiki.
DR   GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR   GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015889; P:cobalamin transport; IDA:EcoCyc.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01005; BtuD; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR023693; ABC_transptr_BtuD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..249
FT                   /note="Vitamin B12 import ATP-binding protein BtuD"
FT                   /id="PRO_0000091950"
FT   DOMAIN          1..233
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01005"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01005"
FT   STRAND          3..12
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   TURN            13..15
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   STRAND          16..24
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   STRAND          28..32
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   HELIX           39..46
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   STRAND          53..58
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   HELIX           63..65
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   HELIX           68..74
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   STRAND          75..78
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   HELIX           90..95
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   HELIX           104..113
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   HELIX           117..119
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   STRAND          120..123
FT                   /evidence="ECO:0007829|PDB:4DBL"
FT   HELIX           124..126
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   HELIX           129..144
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   TURN            146..148
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   STRAND          154..159
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   TURN            160..163
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   HELIX           166..181
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   STRAND          185..189
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   HELIX           193..199
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   STRAND          201..207
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   STRAND          210..216
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   HELIX           217..220
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   HELIX           223..230
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   STRAND          234..239
FT                   /evidence="ECO:0007829|PDB:2QI9"
FT   STRAND          242..247
FT                   /evidence="ECO:0007829|PDB:2QI9"
SQ   SEQUENCE   249 AA;  27081 MW;  760004A5C0134245 CRC64;
     MSIVMQLQDV AESTRLGPLS GEVRAGEILH LVGPNGAGKS TLLARMAGMT SGKGSIQFAG
     QPLEAWSATK LALHRAYLSQ QQTPPFATPV WHYLTLHQHD KTRTELLNDV AGALALDDKL
     GRSTNQLSGG EWQRVRLAAV VLQITPQANP AGQLLLLDEP MNSLDVAQQS ALDKILSALC
     QQGLAIVMSS HDLNHTLRHA HRAWLLKGGK MLASGRREEV LTPPNLAQAY GMNFRRLDIE
     GHRMLISTI
 
 
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