P06611 (BTUD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vitamin B12 import ATP-binding protein BtuD
EC=3.6.3.33

Alternative name(s):
Vitamin B12-transporting ATPase

Gene names

Name:	btuD
Ordered Locus Names:	b1709, JW1699

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Responsible for energy coupling to the transport system By similarity. HAMAP MF_01005
Catalytic activity	ATP + H2O + vitamin B12(Out) = ADP + phosphate + vitamin B12(In). HAMAP MF_01005
Subunit structure	The complex is composed of two ATP-binding proteins (BtuD), two transmembrane proteins (BtuC) and a solute-binding protein (BtuF).
Subcellular location	Cell inner membrane; Peripheral membrane protein HAMAP MF_01005.
Sequence similarities	Belongs to the ABC transporter superfamily. Vitamin B12 importer (TC 3.A.1.13.1) family. [View classification] Contains 1 ABC transporter domain.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	peripheral to membrane of membrane fraction Inferred from direct assay. Source: EcoliWiki plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cobalamin-transporting ATPase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 249

249

Vitamin B12 import ATP-binding protein BtuD HAMAP MF_01005

PRO_0000091950

Regions

Domain

1 – 233

233

ABC transporter

Nucleotide binding

33 – 40

8

ATP Potential

Secondary structure

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249

Helix Strand Turn

Details...

Beta strand

3 – 10

8

Turn

13 – 15

3

Beta strand

18 – 24

7

Beta strand

28 – 30

3

Helix

39 – 47

9

Beta strand

53 – 62

10

Helix

63 – 65

3

Helix

68 – 74

7

Beta strand

75 – 78

4

Helix

90 – 97

8

Helix

104 – 113

10

Turn

117 – 121

5

Helix

124 – 126

3

Helix

129 – 144

16

Turn

146 – 148

3

Beta strand

154 – 159

6

Helix

166 – 181

16

Beta strand

185 – 188

4

Helix

193 – 199

7

Beta strand

205 – 207

3

Helix

217 – 220

4

Helix

223 – 230

8

Sequences

	Sequence		Length	Mass (Da)
	P06611 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 760004A5C0134245	FASTA	249	27,081
	10 20 30 40 50 60 MSIVMQLQDV AESTRLGPLS GEVRAGEILH LVGPNGAGKS TLLARMAGMT SGKGSIQFAG 70 80 90 100 110 120 QPLEAWSATK LALHRAYLSQ QQTPPFATPV WHYLTLHQHD KTRTELLNDV AGALALDDKL 130 140 150 160 170 180 GRSTNQLSGG EWQRVRLAAV VLQITPQANP AGQLLLLDEP MNSLDVAQQS ALDKILSALC 190 200 210 220 230 240 QQGLAIVMSS HDLNHTLRHA HRAWLLKGGK MLASGRREEV LTPPNLAQAY GMNFRRLDIE GHRMLISTI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 3528129] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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 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: 12004122] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH BTUC.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M14031 Genomic DNA. Translation: AAA23528.1.
U00096 Genomic DNA. Translation: AAC74779.1.
AP009048 Genomic DNA. Translation: BAA15477.1.

PIR

QRECBD. C24498.

RefSeq

NP_416224.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L7V	X-ray	3.20	C/D	1-249	[»]
2QI9	X-ray	2.60	C/D	1-249	[»]

ProteinModelPortal

P06611.

SMR

P06611. Positions 2-232.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9234N.

IntAct

P06611. 9 interactions.

MINT

MINT-6803741.

Protein family/group databases

TCDB

3.A.1.13.1. ATP-binding cassette (ABC) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000002353; EBESCP00000002353; EBESCG00000001921.
EBESCT00000016809; EBESCP00000016100; EBESCG00000015868.

GeneID

945751.

GenomeReviews

Gene locus JW1699 in contig AP009048_GR.
Gene locus b1709 in contig U00096_GR.

KEGG

ecj:JW1699.
eco:b1709.

PATRIC

32118724. VBIEscCol129921_1780.

Organism-specific databases

EchoBASE

EB0126.

EcoGene

EG10128. btuD.

Phylogenomic databases

eggNOG

COG4138.

GeneTree

EBGT00050000008236.

HOGENOM

HBG758042.

OMA

VWHYLAL.

PhylomeDB

P06611.

ProtClustDB

PRK03695.

Enzyme and pathway databases

BioCyc

EcoCyc:BTUD-MONOMER.

Gene expression databases

Genevestigator

P06611.

Family and domain databases

HAMAP

MF_01005. BtuD.
[Tree]

InterPro

IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR023693. ABC_transptr_BtuD.
IPR003593. ATPase_AAA+_core.
[Graphical view]

KO

K06074.

Pfam

PF00005. ABC_tran. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 1 hit.
[Graphical view]

PROSITE

PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BTUD_ECOLI

Accession

Primary (citable) accession number: P06611

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	January 25, 2012
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program