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Protein

Vitamin B12 import ATP-binding protein BtuD

Gene

btuD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Responsible for energy coupling to the transport system.UniRule annotation

Catalytic activityi

ATP + H2O + vitamin B12(Out) = ADP + phosphate + vitamin B12(In).UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi33 – 408ATPUniRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-HAMAP
  • cobalamin-transporting ATPase activity Source: EcoCyc

GO - Biological processi

  • cobalamin transport Source: EcoCyc
  • vitamin transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:BTUD-MONOMER.
ECOL316407:JW1699-MONOMER.
MetaCyc:BTUD-MONOMER.
BRENDAi3.6.3.33. 2026.

Protein family/group databases

TCDBi3.A.1.13.1. the atp-binding cassette (abc) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Vitamin B12 import ATP-binding protein BtuDUniRule annotation (EC:3.6.3.33UniRule annotation)
Alternative name(s):
Vitamin B12-transporting ATPaseUniRule annotation
Gene namesi
Name:btuDUniRule annotation
Ordered Locus Names:b1709, JW1699
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10128. btuD.

Subcellular locationi

GO - Cellular componenti

  • ATP-binding cassette (ABC) transporter complex Source: EcoCyc
  • cytosol Source: EcoCyc
  • extrinsic component of cytoplasmic side of plasma membrane Source: EcoCyc
  • extrinsic component of membrane Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249Vitamin B12 import ATP-binding protein BtuDPRO_0000091950Add
BLAST

Proteomic databases

PaxDbiP06611.

Interactioni

Subunit structurei

The complex is composed of two ATP-binding proteins (BtuD), two transmembrane proteins (BtuC) and a solute-binding protein (BtuF).UniRule annotation1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
btuCP066093EBI-1033420,EBI-1033427

Protein-protein interaction databases

BioGridi4260301. 184 interactions.
DIPiDIP-9234N.
IntActiP06611. 9 interactions.
MINTiMINT-6803741.
STRINGi511145.b1709.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1210Combined sources
Turni13 – 153Combined sources
Beta strandi16 – 249Combined sources
Beta strandi28 – 325Combined sources
Helixi39 – 468Combined sources
Beta strandi53 – 586Combined sources
Helixi63 – 653Combined sources
Helixi68 – 747Combined sources
Beta strandi75 – 784Combined sources
Helixi90 – 956Combined sources
Helixi104 – 11310Combined sources
Helixi117 – 1193Combined sources
Beta strandi120 – 1234Combined sources
Helixi124 – 1263Combined sources
Helixi129 – 14416Combined sources
Turni146 – 1483Combined sources
Beta strandi154 – 1596Combined sources
Turni160 – 1634Combined sources
Helixi166 – 18116Combined sources
Beta strandi185 – 1895Combined sources
Helixi193 – 1997Combined sources
Beta strandi201 – 2077Combined sources
Beta strandi210 – 2167Combined sources
Helixi217 – 2204Combined sources
Helixi223 – 2308Combined sources
Beta strandi234 – 2396Combined sources
Beta strandi242 – 2476Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L7VX-ray3.20C/D1-249[»]
2QI9X-ray2.60C/D1-249[»]
4DBLX-ray3.49C/D/H/I1-249[»]
4FI3X-ray3.47C/D1-249[»]
4R9UX-ray2.78C/D1-249[»]
ProteinModelPortaliP06611.
SMRiP06611. Positions 2-232.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06611.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 233233ABC transporterUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ABC transporter superfamily. Vitamin B12 importer (TC 3.A.1.13.1) family. [View classification]UniRule annotation
Contains 1 ABC transporter domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG41080WI. Bacteria.
COG4138. LUCA.
InParanoidiP06611.
KOiK06074.
OMAiHLAYYAR.
OrthoDBiEOG6VXF80.
PhylomeDBiP06611.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_01005. BtuD.
InterProiIPR003593. AAA+_ATPase.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR023693. ABC_transptr_BtuD.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00005. ABC_tran. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P06611-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIVMQLQDV AESTRLGPLS GEVRAGEILH LVGPNGAGKS TLLARMAGMT
60 70 80 90 100
SGKGSIQFAG QPLEAWSATK LALHRAYLSQ QQTPPFATPV WHYLTLHQHD
110 120 130 140 150
KTRTELLNDV AGALALDDKL GRSTNQLSGG EWQRVRLAAV VLQITPQANP
160 170 180 190 200
AGQLLLLDEP MNSLDVAQQS ALDKILSALC QQGLAIVMSS HDLNHTLRHA
210 220 230 240
HRAWLLKGGK MLASGRREEV LTPPNLAQAY GMNFRRLDIE GHRMLISTI
Length:249
Mass (Da):27,081
Last modified:January 1, 1988 - v1
Checksum:i760004A5C0134245
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14031 Genomic DNA. Translation: AAA23528.1.
U00096 Genomic DNA. Translation: AAC74779.1.
AP009048 Genomic DNA. Translation: BAA15477.1.
PIRiC24498. QRECBD.
RefSeqiNP_416224.1. NC_000913.3.
WP_000029474.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74779; AAC74779; b1709.
BAA15477; BAA15477; BAA15477.
GeneIDi945751.
KEGGiecj:JW1699.
eco:b1709.
PATRICi32118724. VBIEscCol129921_1780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14031 Genomic DNA. Translation: AAA23528.1.
U00096 Genomic DNA. Translation: AAC74779.1.
AP009048 Genomic DNA. Translation: BAA15477.1.
PIRiC24498. QRECBD.
RefSeqiNP_416224.1. NC_000913.3.
WP_000029474.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L7VX-ray3.20C/D1-249[»]
2QI9X-ray2.60C/D1-249[»]
4DBLX-ray3.49C/D/H/I1-249[»]
4FI3X-ray3.47C/D1-249[»]
4R9UX-ray2.78C/D1-249[»]
ProteinModelPortaliP06611.
SMRiP06611. Positions 2-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260301. 184 interactions.
DIPiDIP-9234N.
IntActiP06611. 9 interactions.
MINTiMINT-6803741.
STRINGi511145.b1709.

Protein family/group databases

TCDBi3.A.1.13.1. the atp-binding cassette (abc) superfamily.

Proteomic databases

PaxDbiP06611.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74779; AAC74779; b1709.
BAA15477; BAA15477; BAA15477.
GeneIDi945751.
KEGGiecj:JW1699.
eco:b1709.
PATRICi32118724. VBIEscCol129921_1780.

Organism-specific databases

EchoBASEiEB0126.
EcoGeneiEG10128. btuD.

Phylogenomic databases

eggNOGiENOG41080WI. Bacteria.
COG4138. LUCA.
InParanoidiP06611.
KOiK06074.
OMAiHLAYYAR.
OrthoDBiEOG6VXF80.
PhylomeDBiP06611.

Enzyme and pathway databases

BioCyciEcoCyc:BTUD-MONOMER.
ECOL316407:JW1699-MONOMER.
MetaCyc:BTUD-MONOMER.
BRENDAi3.6.3.33. 2026.

Miscellaneous databases

EvolutionaryTraceiP06611.
PROiP06611.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_01005. BtuD.
InterProiIPR003593. AAA+_ATPase.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR023693. ABC_transptr_BtuD.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00005. ABC_tran. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the btuCED genes involved in vitamin B12 transport in Escherichia coli and homology with components of periplasmic-binding-protein-dependent transport systems."
    Friedrich M.J., Deveaux L.C., Kadner R.J.
    J. Bacteriol. 167:928-934(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism."
    Locher K.P., Lee A.T., Rees D.C.
    Science 296:1091-1098(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH BTUC.

Entry informationi

Entry nameiBTUD_ECOLI
AccessioniPrimary (citable) accession number: P06611
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: January 20, 2016
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.