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 import system permease protein BtuC

Gene

btuC

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. Involved in the translocation of the substrate across the membrane.

GO - Molecular functioni

  • cobalamin transporter activity Source: EcoliWiki
  • cobalamin-transporting ATPase activity Source: EcoCyc

GO - Biological processi

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

Keywords - Biological processi

Transport

Enzyme and pathway databases

BioCyciEcoCyc:BTUC-MONOMER.
ECOL316407:JW1701-MONOMER.
MetaCyc:BTUC-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 system permease protein BtuC
Gene namesi
Name:btuC
Ordered Locus Names:b1711, JW1701
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10127. btuC.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010Cytoplasmic1 Publication
Transmembranei11 – 3525Helical; Name=1Add
BLAST
Topological domaini36 – 5621Periplasmic1 PublicationAdd
BLAST
Transmembranei57 – 8125Helical; Name=2Add
BLAST
Topological domaini82 – 9211Cytoplasmic1 PublicationAdd
BLAST
Transmembranei93 – 10715Helical; Name=3Add
BLAST
Topological domaini108 – 1136Periplasmic1 Publication
Transmembranei114 – 13825Helical; Name=4Add
BLAST
Topological domaini139 – 1413Cytoplasmic1 Publication
Transmembranei142 – 16625Helical; Name=5Add
BLAST
Topological domaini167 – 19024Periplasmic1 PublicationAdd
BLAST
Transmembranei191 – 20616Helical; Name=6Add
BLAST
Topological domaini207 – 22822Cytoplasmic1 PublicationAdd
BLAST
Transmembranei229 – 24921Helical; Name=7Add
BLAST
Topological domaini250 – 2578Periplasmic1 Publication
Transmembranei258 – 26710Helical; Name=8
Topological domaini268 – 2747Cytoplasmic1 Publication
Transmembranei275 – 29622Helical; Name=9Add
BLAST
Topological domaini297 – 3048Periplasmic1 Publication
Transmembranei305 – 32420Helical; Name=10Add
BLAST
Topological domaini325 – 3262Cytoplasmic1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Vitamin B12 import system permease protein BtuCPRO_0000059968Add
BLAST

Proteomic databases

PaxDbiP06609.

Interactioni

Subunit structurei

The complex is composed of two ATP-binding proteins (BtuD), two transmembrane proteins (BtuC) and a solute-binding protein (BtuF).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
btuDP066113EBI-1033427,EBI-1033420

Protein-protein interaction databases

BioGridi4263152. 131 interactions.
DIPiDIP-9233N.
IntActiP06609. 2 interactions.
MINTiMINT-6803761.
STRINGi511145.b1711.

Structurei

Secondary structure

1
326
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 3129Combined sources
Beta strandi34 – 363Combined sources
Helixi40 – 423Combined sources
Beta strandi43 – 453Combined sources
Helixi48 – 547Combined sources
Helixi56 – 8025Combined sources
Helixi88 – 914Combined sources
Helixi93 – 10816Combined sources
Helixi114 – 13623Combined sources
Turni137 – 1393Combined sources
Helixi142 – 16524Combined sources
Helixi171 – 1799Combined sources
Helixi188 – 1903Combined sources
Helixi191 – 1944Combined sources
Turni195 – 1973Combined sources
Helixi198 – 2047Combined sources
Helixi208 – 2158Combined sources
Helixi218 – 2236Combined sources
Helixi228 – 25023Combined sources
Beta strandi255 – 2584Combined sources
Helixi259 – 2657Combined sources
Turni266 – 2683Combined sources
Helixi272 – 29524Combined sources
Beta strandi296 – 2983Combined sources
Beta strandi299 – 3013Combined sources
Helixi305 – 32117Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L7VX-ray3.20A/B1-326[»]
2QI9X-ray2.60A/B1-326[»]
4DBLX-ray3.49A/B/F/G1-326[»]
4FI3X-ray3.47A/B1-326[»]
4R9UX-ray2.78A/B1-326[»]
ProteinModelPortaliP06609.
SMRiP06609. Positions 1-324.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06609.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4108ESU. Bacteria.
COG4139. LUCA.
HOGENOMiHOG000045407.
InParanoidiP06609.
KOiK06073.
OMAiLQRIYAW.
OrthoDBiEOG61ZTDC.
PhylomeDBiP06609.

Family and domain databases

Gene3Di1.10.3470.10. 1 hit.
HAMAPiMF_01004. BtuC.
InterProiIPR029022. ABC_BtuC-like.
IPR023691. ABC_transptr_BtuC.
IPR000522. ABC_transptr_permAse.
[Graphical view]
PANTHERiPTHR30472. PTHR30472. 1 hit.
PfamiPF01032. FecCD. 1 hit.
[Graphical view]
SUPFAMiSSF81345. SSF81345. 1 hit.

Sequencei

Sequence statusi: Complete.

P06609-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTLARQQQR QNIRWLLCLS VLMLLALLLS LCAGEQWISP GDWFTPRGEL
60 70 80 90 100
FVWQIRLPRT LAVLLVGAAL AISGAVMQAL FENPLAEPGL LGVSNGAGVG
110 120 130 140 150
LIAAVLLGQG QLPNWALGLC AIAGALIITL ILLRFARRHL STSRLLLAGV
160 170 180 190 200
ALGIICSALM TWAIYFSTSV DLRQLMYWMM GGFGGVDWRQ SWLMLALIPV
210 220 230 240 250
LLWICCQSRP MNMLALGEIS ARQLGLPLWF WRNVLVAATG WMVGVSVALA
260 270 280 290 300
GAIGFIGLVI PHILRLCGLT DHRVLLPGCA LAGASALLLA DIVARLALAA
310 320
AELPIGVVTA TLGAPVFIWL LLKAGR
Length:326
Mass (Da):34,949
Last modified:November 1, 1997 - v3
Checksum:iC65882B1C47BFE69
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1122QL → LT in AAA23526 (PubMed:3528129).Curated
Sequence conflicti123 – 1231A → R in AAA23526 (PubMed:3528129).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14031 Genomic DNA. Translation: AAA23526.1.
U00096 Genomic DNA. Translation: AAC74781.1.
AP009048 Genomic DNA. Translation: BAA15479.1.
PIRiG64929. QRECBC.
RefSeqiNP_416226.1. NC_000913.3.
WP_000956528.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74781; AAC74781; b1711.
BAA15479; BAA15479; BAA15479.
GeneIDi945877.
KEGGiecj:JW1701.
eco:b1711.
PATRICi32118728. VBIEscCol129921_1782.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14031 Genomic DNA. Translation: AAA23526.1.
U00096 Genomic DNA. Translation: AAC74781.1.
AP009048 Genomic DNA. Translation: BAA15479.1.
PIRiG64929. QRECBC.
RefSeqiNP_416226.1. NC_000913.3.
WP_000956528.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L7VX-ray3.20A/B1-326[»]
2QI9X-ray2.60A/B1-326[»]
4DBLX-ray3.49A/B/F/G1-326[»]
4FI3X-ray3.47A/B1-326[»]
4R9UX-ray2.78A/B1-326[»]
ProteinModelPortaliP06609.
SMRiP06609. Positions 1-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263152. 131 interactions.
DIPiDIP-9233N.
IntActiP06609. 2 interactions.
MINTiMINT-6803761.
STRINGi511145.b1711.

Protein family/group databases

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

Proteomic databases

PaxDbiP06609.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74781; AAC74781; b1711.
BAA15479; BAA15479; BAA15479.
GeneIDi945877.
KEGGiecj:JW1701.
eco:b1711.
PATRICi32118728. VBIEscCol129921_1782.

Organism-specific databases

EchoBASEiEB0125.
EcoGeneiEG10127. btuC.

Phylogenomic databases

eggNOGiENOG4108ESU. Bacteria.
COG4139. LUCA.
HOGENOMiHOG000045407.
InParanoidiP06609.
KOiK06073.
OMAiLQRIYAW.
OrthoDBiEOG61ZTDC.
PhylomeDBiP06609.

Enzyme and pathway databases

BioCyciEcoCyc:BTUC-MONOMER.
ECOL316407:JW1701-MONOMER.
MetaCyc:BTUC-MONOMER.
BRENDAi3.6.3.33. 2026.

Miscellaneous databases

EvolutionaryTraceiP06609.
PROiP06609.

Family and domain databases

Gene3Di1.10.3470.10. 1 hit.
HAMAPiMF_01004. BtuC.
InterProiIPR029022. ABC_BtuC-like.
IPR023691. ABC_transptr_BtuC.
IPR000522. ABC_transptr_permAse.
[Graphical view]
PANTHERiPTHR30472. PTHR30472. 1 hit.
PfamiPF01032. FecCD. 1 hit.
[Graphical view]
SUPFAMiSSF81345. SSF81345. 1 hit.
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. "Vitamin B12 transport in Escherichia coli K12 does not require the btuE gene of the btuCED operon."
    Rioux C.R., Kadner R.J.
    Mol. Gen. Genet. 217:301-308(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "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: CHARACTERIZATION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  7. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  8. "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 BTUD.

Entry informationi

Entry nameiBTUC_ECOLI
AccessioniPrimary (citable) accession number: P06609
Secondary accession number(s): P77197
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1997
Last modified: January 20, 2016
This is version 141 of the entry and version 3 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.