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P06129 (BTUB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vitamin B12 transporter BtuB
Alternative name(s):
Cobalamin receptor
Outer membrane cobalamin translocator
Gene names
Name:btuB
Synonyms:bfe, cer, dcrC
Ordered Locus Names:b3966, JW3938
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length614 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins. HAMAP MF_01531

Enzyme regulation

Calcium increases vitamin B12 binding affinity by a factor of 50-100. HAMAP MF_01531

Subcellular location

Cell outer membrane; Multi-pass membrane protein HAMAP MF_01531.

Induction

Constitutively expressed. Ref.9

Miscellaneous

Primary control of btuB expression by cobalamin occurs at the level of translation initiation. HAMAP MF_01531

Sequence similarities

Belongs to the TonB-dependent receptor family. BtuB (TC 1.B.14.3.1) subfamily. [View classification]

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ceaCP006461EBI-1037258,EBI-1029919From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.6
Chain21 – 614594Vitamin B12 transporter BtuB HAMAP MF_01531
PRO_0000003479

Regions

Topological domain21 – 157137Periplasmic HAMAP MF_01531
Transmembrane158 – 1658Beta stranded HAMAP MF_01531
Topological domain166 – 1683Extracellular HAMAP MF_01531
Transmembrane169 – 17810Beta stranded HAMAP MF_01531
Topological domain179 – 1835Periplasmic HAMAP MF_01531
Transmembrane184 – 19512Beta stranded HAMAP MF_01531
Topological domain196 – 21621Extracellular HAMAP MF_01531
Transmembrane217 – 22711Beta stranded HAMAP MF_01531
Topological domain228 – 2314Periplasmic HAMAP MF_01531
Transmembrane232 – 24817Beta stranded HAMAP MF_01531
Topological domain249 – 26214Extracellular HAMAP MF_01531
Transmembrane263 – 27715Beta stranded HAMAP MF_01531
Topological domain2781Periplasmic HAMAP MF_01531
Transmembrane279 – 29618Beta stranded HAMAP MF_01531
Topological domain297 – 30812Extracellular HAMAP MF_01531
Transmembrane309 – 32517Beta stranded HAMAP MF_01531
Topological domain326 – 3272Periplasmic HAMAP MF_01531
Transmembrane328 – 33710Beta stranded HAMAP MF_01531
Topological domain338 – 35215Extracellular HAMAP MF_01531
Transmembrane353 – 36917Beta stranded HAMAP MF_01531
Topological domain3701Periplasmic HAMAP MF_01531
Transmembrane371 – 38111Beta stranded HAMAP MF_01531
Topological domain382 – 3843Extracellular HAMAP MF_01531
Transmembrane385 – 40016Beta stranded HAMAP MF_01531
Topological domain401 – 4022Periplasmic HAMAP MF_01531
Transmembrane403 – 41715Beta stranded HAMAP MF_01531
Topological domain418 – 43316Extracellular HAMAP MF_01531
Transmembrane434 – 44310Beta stranded HAMAP MF_01531
Topological domain444 – 4485Periplasmic HAMAP MF_01531
Transmembrane449 – 45810Beta stranded HAMAP MF_01531
Topological domain459 – 47214Extracellular HAMAP MF_01531
Transmembrane473 – 49018Beta stranded HAMAP MF_01531
Topological domain491 – 4933Periplasmic HAMAP MF_01531
Transmembrane494 – 50916Beta stranded HAMAP MF_01531
Topological domain510 – 5167Extracellular HAMAP MF_01531
Transmembrane517 – 52913Beta stranded HAMAP MF_01531
Topological domain530 – 5345Periplasmic HAMAP MF_01531
Transmembrane535 – 55016Beta stranded HAMAP MF_01531
Topological domain551 – 5577Extracellular HAMAP MF_01531
Transmembrane558 – 57215Beta stranded HAMAP MF_01531
Topological domain573 – 58412Periplasmic HAMAP MF_01531
Transmembrane585 – 59612Beta stranded HAMAP MF_01531
Topological domain597 – 6015Extracellular HAMAP MF_01531
Transmembrane602 – 61413Beta stranded HAMAP MF_01531
Region108 – 1125Cobalamin-binding HAMAP MF_01531
Region249 – 2513Cobalamin-binding HAMAP MF_01531
Region515 – 5184Cobalamin-binding HAMAP MF_01531
Motif26 – 338TonB box HAMAP MF_01531
Motif597 – 61418TonB C-terminal box HAMAP MF_01531

Sites

Metal binding1991Calcium 1
Metal binding2111Calcium 1
Metal binding2131Calcium 1
Metal binding2131Calcium 2
Metal binding2151Calcium 1
Metal binding2151Calcium 2
Metal binding2491Calcium 2; via carbonyl oxygen
Metal binding2501Calcium 1
Metal binding2501Calcium 2
Metal binding2611Calcium 2

Experimental info

Mutagenesis281L → P: Inactivates uptake. Ref.8 Ref.11
Mutagenesis301V → G or P: Inactivates uptake. Ref.8 Ref.11
Sequence conflict1621A → G in AAA23524. Ref.1
Sequence conflict3771A → R in AAA23524. Ref.1

Secondary structure

1 ............................................................................... 614
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06129 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: AB43CC46A991FF95

FASTA61468,407
        10         20         30         40         50         60 
MIKKASLLTA CSVTAFSAWA QDTSPDTLVV TANRFEQPRS TVLAPTTVVT RQDIDRWQST 

        70         80         90        100        110        120 
SVNDVLRRLP GVDITQNGGS GQLSSIFIRG TNASHVLVLI DGVRLNLAGV SGSADLSQFP 

       130        140        150        160        170        180 
IALVQRVEYI RGPRSAVYGS DAIGGVVNII TTRDEPGTEI SAGWGSNSYQ NYDVSTQQQL 

       190        200        210        220        230        240 
GDKTRVTLLG DYAHTHGYDV VAYGNTGTQA QTDNDGFLSK TLYGALEHNF TDAWSGFVRG 

       250        260        270        280        290        300 
YGYDNRTNYD AYYSPGSPLL DTRKLYSQSW DAGLRYNGEL IKSQLITSYS HSKDYNYDPH 

       310        320        330        340        350        360 
YGRYDSSATL DEMKQYTVQW ANNVIVGHGS IGAGVDWQKQ TTTPGTGYVE DGYDQRNTGI 

       370        380        390        400        410        420 
YLTGLQQVGD FTFEGAARSD DNSQFGRHGT WQTSAGWEFI EGYRFIASYG TSYKAPNLGQ 

       430        440        450        460        470        480 
LYGFYGNPNL DPEKSKQWEG AFEGLTAGVN WRISGYRNDV SDLIDYDDHT LKYYNEGKAR 

       490        500        510        520        530        540 
IKGVEATANF DTGPLTHTVS YDYVDARNAI TDTPLLRRAK QQVKYQLDWQ LYDFDWGITY 

       550        560        570        580        590        600 
QYLGTRYDKD YSSYPYQTVK MGGVSLWDLA VAYPVTSHLT VRGKIANLFD KDYETVYGYQ 

       610 
TAGREYTLSG SYTF

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the gene for the vitamin B12 receptor protein in the outer membrane of Escherichia coli."
Heller K., Kadner R.J.
J. Bacteriol. 161:904-908(1985) [PubMed: 3882670] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The trmA promoter has regulatory features and sequence elements in common with the rRNA P1 promoter family of Escherichia coli."
Gustafsson C., Lindstroem P.H.R., Hagervall T.G., Esberg K.B., Bjoerk G.R.
J. Bacteriol. 173:1757-1764(1991) [PubMed: 1999392] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
[6]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-32.
Strain: K12 / EMG2.
[7]"The Escherichia coli mutant requiring D-glutamic acid is the result of mutations in two distinct genetic loci."
Dougherty T.J., Thanassi J.A., Pucci M.J.
J. Bacteriol. 175:111-116(1993) [PubMed: 8093236] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 456-614.
Strain: B.
[8]"Point mutations in a conserved region (TonB box) of Escherichia coli outer membrane protein BtuB affect vitamin B12 transport."
Gudmundsdottir A., Bell P.E., Lundrigan M.D., Bradbeer C., Kadner R.J.
J. Bacteriol. 171:6526-6533(1989) [PubMed: 2687240] [Abstract]
Cited for: MUTAGENESIS OF THE TONB BOX.
[9]"Coupled changes in translation and transcription during cobalamin-dependent regulation of btuB expression in Escherichia coli."
Nou X., Kadner R.J.
J. Bacteriol. 180:6719-6728(1998) [PubMed: 9852020] [Abstract]
Cited for: REGULATION OF EXPRESSION.
Strain: K12.
[10]"Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter."
Cadieux N., Kadner R.J.
Proc. Natl. Acad. Sci. U.S.A. 96:10673-10678(1999) [PubMed: 10485884] [Abstract]
Cited for: INTERACTION WITH TONB.
Strain: K12.
[11]"Transport-defective mutations alter the conformation of the energy-coupling motif of an outer membrane transporter."
Coggshall K.A., Cadieux N., Piedmont C., Kadner R.J., Cafiso D.S.
Biochemistry 40:13964-13971(2001) [PubMed: 11705387] [Abstract]
Cited for: MUTAGENESIS OF LEU-28 AND VAL-30.
Strain: K12.
[12]"The Escherichia coli outer membrane cobalamin transporter BtuB: structural analysis of calcium and substrate binding, and identification of orthologous transporters by sequence/structure conservation."
Chimento D.P., Kadner R.J., Wiener M.C.
J. Mol. Biol. 332:999-1014(2003) [PubMed: 14499604] [Abstract]
Cited for: CALCIUM AND SUBSTRATE BINDING SITES.
[13]"Crystallization and initial X-ray diffraction of BtuB, the integral membrane cobalamin transporter of Escherichia coli."
Chimento D.P., Mohanty A.K., Kadner R.J., Wiener M.C.
Acta Crystallogr. D 59:509-511(2003) [PubMed: 12595710] [Abstract]
Cited for: CRYSTALLIZATION.
[14]"Substrate-induced transmembrane signaling in the cobalamin transporter BtuB."
Chimento D.P., Mohanty A.K., Kadner R.J., Wiener M.C.
Nat. Struct. Biol. 10:394-401(2003) [PubMed: 12652322] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-614 OF NATIVE PROTEIN AND COMPLEX WITH CYANOCOBALAMIN.
[15]"The structure of BtuB with bound colicin E3 R-domain implies a translocon."
Kurisu G., Zakharov S.D., Zhalnina M.V., Bano S., Eroukova V.Y., Rokitskaya T.I., Antonenko Y.N., Wiener M.C., Cramer W.A.
Nat. Struct. Biol. 10:948-954(2003) [PubMed: 14528295] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 21-614 IN COMPLEX WITH COLICIN E3 RECEPTOR BINDING DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M10112 Genomic DNA. Translation: AAA23524.1.
U00006 Genomic DNA. Translation: AAC43072.1.
U00096 Genomic DNA. Translation: AAC76948.1.
AP009048 Genomic DNA. Translation: BAE77345.1.
M57568 Genomic DNA. No translation available.
L14556 Genomic DNA. Translation: AAA23676.1.
PIRQRECBT. A65204.
RefSeqNP_418401.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NQEX-ray2.00A21-614[»]
1NQFX-ray2.70A21-614[»]
1NQGX-ray3.31A21-614[»]
1NQHX-ray3.10A21-614[»]
1UJWX-ray2.75A21-614[»]
2GSKX-ray2.10A25-614[»]
2GUFX-ray1.95A21-614[»]
2YSUX-ray3.50A21-614[»]
3M8BX-ray2.44A21-614[»]
3M8DX-ray2.44A21-614[»]
3RGMX-ray2.60A21-614[»]
3RGNX-ray2.30A21-614[»]
ProteinModelPortalP06129.
SMRP06129. Positions 25-614.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9232N.
IntActP06129. 1 interaction.

Protein family/group databases

TCDB1.B.14.3.1. outer membrane receptor (OMR) family.

Proteomic databases

PRIDEP06129.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000000335; EBESCP00000000335; EBESCG00000000271.
EBESCT00000017022; EBESCP00000016313; EBESCG00000016081.
GeneID948468.
GenomeReviewsGene locus JW3938 in contig AP009048_GR.
Gene locus b3966 in contig U00096_GR.
KEGGecj:JW3938.
eco:b3966.
PATRIC32123453. VBIEscCol129921_4087.

Organism-specific databases

EchoBASEEB0124.
EcoGeneEG10126. btuB.

Phylogenomic databases

eggNOGCOG4206.
GeneTreeEBGT00070000031689.
HOGENOMHBG644936.
OMAETAYGYN.
PhylomeDBP06129.
ProtClustDBPRK10641.

Enzyme and pathway databases

BioCycEcoCyc:EG10126-MONOMER.

Gene expression databases

GenevestigatorP06129.

Family and domain databases

HAMAPMF_01531. BtuB.
[Tree]
InterProIPR010101. B12_transptr_BtuB.
IPR012910. Plug.
IPR000531. TonB-dep_rcpt_b-brl.
IPR010916. TonB_box_CS.
IPR010917. TonB_rcpt_CS.
[Graphical view]
Gene3DG3DSA:2.170.130.10. Plug. 1 hit.
G3DSA:2.40.170.20. TonB-dep_rcpt_b-brl. 1 hit.
KOK02014.
PfamPF07715. Plug. 1 hit.
PF00593. TonB_dep_Rec. 1 hit.
[Graphical view]
TIGRFAMsTIGR01779. TonB-B12. 1 hit.
PROSITEPS00430. TONB_DEPENDENT_REC_1. 1 hit.
PS01156. TONB_DEPENDENT_REC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00115. Cyanocobalamin.

Entry information

Entry nameBTUB_ECOLI
AccessionPrimary (citable) accession number: P06129
Secondary accession number(s): Q2M8R1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 1, 1993
Last modified: January 25, 2012
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents