Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Vitamin B12-binding protein

Gene

btuF

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. Binds vitamin B12 and delivers it to the periplasmic surface of BtuC.UniRule annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501CobalaminUniRule annotation1 Publication
Sitei72 – 721Important for BtuC bindingUniRule annotation1 Publication
Sitei202 – 2021Important for BtuC bindingUniRule annotation1 Publication

GO - Molecular functioni

  • cobalamin binding Source: EcoliWiki

GO - Biological processi

  • cobalamin transport Source: EcoliWiki
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

BioCyciEcoCyc:EG12334-MONOMER.
ECOL316407:JW0154-MONOMER.
MetaCyc:EG12334-MONOMER.
BRENDAi3.6.3.33. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Vitamin B12-binding proteinUniRule annotation
Gene namesi
Name:btuF
Synonyms:yadT
Ordered Locus Names:b0158, JW0154
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12334. btuF.

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
  • periplasmic space Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 266244Vitamin B12-binding proteinPRO_0000003497Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi183 ↔ 259

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP37028.
PRIDEiP37028.

Interactioni

Subunit structurei

The complex is composed of two ATP-binding proteins (BtuD), two transmembrane proteins (BtuC) and a solute-binding protein (BtuF).UniRule annotation2 Publications

Protein-protein interaction databases

BioGridi4261861. 275 interactions.
DIPiDIP-11194N.
IntActiP37028. 5 interactions.
MINTiMINT-6803779.
STRINGi511145.b0158.

Structurei

Secondary structure

1
266
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 283Combined sources
Helixi31 – 399Combined sources
Beta strandi45 – 484Combined sources
Helixi55 – 595Combined sources
Beta strandi62 – 654Combined sources
Helixi71 – 766Combined sources
Beta strandi80 – 845Combined sources
Turni86 – 883Combined sources
Helixi91 – 999Combined sources
Beta strandi104 – 1063Combined sources
Helixi112 – 12211Combined sources
Helixi123 – 1253Combined sources
Beta strandi126 – 1283Combined sources
Helixi129 – 15022Combined sources
Beta strandi156 – 1605Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi172 – 1743Combined sources
Helixi175 – 1828Combined sources
Beta strandi185 – 1873Combined sources
Turni188 – 1914Combined sources
Beta strandi193 – 1964Combined sources
Helixi201 – 2055Combined sources
Beta strandi210 – 2167Combined sources
Helixi218 – 2203Combined sources
Helixi221 – 2288Combined sources
Helixi229 – 2313Combined sources
Beta strandi236 – 2394Combined sources
Helixi241 – 2455Combined sources
Beta strandi246 – 2483Combined sources
Helixi251 – 26212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N2ZX-ray2.00A/B22-266[»]
1N4AX-ray2.00A/B23-266[»]
1N4DX-ray3.00A/B23-266[»]
2QI9X-ray2.60F22-266[»]
4DBLX-ray3.49E/J22-266[»]
4FI3X-ray3.47F22-266[»]
ProteinModelPortaliP37028.
SMRiP37028. Positions 22-266.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37028.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 266242Fe/B12 periplasmic-bindingUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni242 – 2465Cobalamin-bindingUniRule annotation2 Publications

Sequence similaritiesi

Belongs to the BtuF family.UniRule annotationCurated
Contains 1 Fe/B12 periplasmic-binding domain.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105JKQ. Bacteria.
COG0614. LUCA.
HOGENOMiHOG000282913.
InParanoidiP37028.
KOiK06858.
OMAiVSVFYQV.
OrthoDBiEOG63Z761.
PhylomeDBiP37028.

Family and domain databases

HAMAPiMF_01000. BtuF.
InterProiIPR002491. ABC_transptr_periplasmic_BD.
IPR023544. ABC_transptr_vit_B12-bd.
[Graphical view]
PfamiPF01497. Peripla_BP_2. 1 hit.
[Graphical view]
PROSITEiPS50983. FE_B12_PBP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P37028-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKSLFRALV ALSFLAPLWL NAAPRVITLS PANTELAFAA GITPVGVSSY
60 70 80 90 100
SDYPPQAQKI EQVSTWQGMN LERIVALKPD LVIAWRGGNA ERQVDQLASL
110 120 130 140 150
GIKVMWVDAT SIEQIANALR QLAPWSPQPD KAEQAAQSLL DQYAQLKAQY
160 170 180 190 200
ADKPKKRVFL QFGINPPFTS GKESIQNQVL EVCGGENIFK DSRVPWPQVS
210 220 230 240 250
REQVLARSPQ AIVITGGPDQ IPKIKQYWGE QLKIPVIPLT SDWFERASPR
260
IILAAQQLCN ALSQVD
Length:266
Mass (Da):29,367
Last modified:November 1, 1997 - v2
Checksum:i480F2E620ACD6EA1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti208 – 2081S → L (PubMed:8202364).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70214 Genomic DNA. Translation: AAB08588.1.
U00096 Genomic DNA. Translation: AAC73269.1.
AP009048 Genomic DNA. Translation: BAB96735.2.
PIRiF64739.
RefSeqiNP_414700.1. NC_000913.3.
WP_001129927.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73269; AAC73269; b0158.
BAB96735; BAB96735; BAB96735.
GeneIDi947574.
KEGGiecj:JW0154.
eco:b0158.
PATRICi32115425. VBIEscCol129921_0164.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70214 Genomic DNA. Translation: AAB08588.1.
U00096 Genomic DNA. Translation: AAC73269.1.
AP009048 Genomic DNA. Translation: BAB96735.2.
PIRiF64739.
RefSeqiNP_414700.1. NC_000913.3.
WP_001129927.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N2ZX-ray2.00A/B22-266[»]
1N4AX-ray2.00A/B23-266[»]
1N4DX-ray3.00A/B23-266[»]
2QI9X-ray2.60F22-266[»]
4DBLX-ray3.49E/J22-266[»]
4FI3X-ray3.47F22-266[»]
ProteinModelPortaliP37028.
SMRiP37028. Positions 22-266.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261861. 275 interactions.
DIPiDIP-11194N.
IntActiP37028. 5 interactions.
MINTiMINT-6803779.
STRINGi511145.b0158.

Proteomic databases

PaxDbiP37028.
PRIDEiP37028.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73269; AAC73269; b0158.
BAB96735; BAB96735; BAB96735.
GeneIDi947574.
KEGGiecj:JW0154.
eco:b0158.
PATRICi32115425. VBIEscCol129921_0164.

Organism-specific databases

EchoBASEiEB2238.
EcoGeneiEG12334. btuF.

Phylogenomic databases

eggNOGiENOG4105JKQ. Bacteria.
COG0614. LUCA.
HOGENOMiHOG000282913.
InParanoidiP37028.
KOiK06858.
OMAiVSVFYQV.
OrthoDBiEOG63Z761.
PhylomeDBiP37028.

Enzyme and pathway databases

BioCyciEcoCyc:EG12334-MONOMER.
ECOL316407:JW0154-MONOMER.
MetaCyc:EG12334-MONOMER.
BRENDAi3.6.3.33. 2026.

Miscellaneous databases

EvolutionaryTraceiP37028.
PROiP37028.

Family and domain databases

HAMAPiMF_01000. BtuF.
InterProiIPR002491. ABC_transptr_periplasmic_BD.
IPR023544. ABC_transptr_vit_B12-bd.
[Graphical view]
PfamiPF01497. Peripla_BP_2. 1 hit.
[Graphical view]
PROSITEiPS50983. FE_B12_PBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
    Fujita N., Mori H., Yura T., Ishihama A.
    Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  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], SEQUENCE REVISION TO 208.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Identification of the periplasmic cobalamin-binding protein BtuF of Escherichia coli."
    Cadieux N., Bradbeer C., Reeger-Schneider E., Koester W., Mohanty A.K., Wiener M.C., Kadner R.J.
    J. Bacteriol. 184:706-717(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-6 AND 23-27, FUNCTION, SUBCELLULAR LOCATION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  6. "The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter."
    Borths E.L., Locher K.P., Lee A.T., Rees D.C.
    Proc. Natl. Acad. Sci. U.S.A. 99:16642-16647(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-266 IN COMPLEX WITH VITAMIN B12, SUBUNIT.
  7. "Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding."
    Karpowich N.K., Huang H.H., Smith P.C., Hunt J.F.
    J. Biol. Chem. 278:8429-8434(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-266 IN COMPLEX WITH VITAMIN B12.

Entry informationi

Entry nameiBTUF_ECOLI
AccessioniPrimary (citable) accession number: P37028
Secondary accession number(s): P77436
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: January 20, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Vitamin B12 is bound in a deep cleft formed at the interface between the two lobes of BtuF.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.