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Q9WY65 (ECFA2_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Energy-coupling factor transporter ATP-binding protein EcfA2

Short name=ECF transporter A component EcfA2
EC=3.6.3.-
Gene names
Name:ecfA2
Synonyms:ecfA, ecfA'
Ordered Locus Names:TM_0222
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates Probable. Expression of the complex plus RibU in E.coli allows riboflavin uptake; uptake does not occur in the absence of RibU or the EcfA1A2T complex. Ref.3

Subunit structure

Forms a heterodimer with EcfA1. Forms a stable energy-coupling factor (ECF) transporter complex composed of 2 membrane-embedded substrate-binding proteins (S component, RibU, BioY), 2 ATP-binding proteins (A component) and 2 transmembrane proteins (T component) upon coexpression in E.coli. Stable subcomplexes with both A plus T components can also be isolated. This complex interacts with at least 2 substrate-specific components, BioY and RibU. Ref.3

Subcellular location

Cell inner membrane; Peripheral membrane protein Probable Ref.3.

Miscellaneous

Structure 4HLU is probably in the open state.

Sequence similarities

Belongs to the ABC transporter superfamily. Energy-coupling factor EcfA family.

Contains 1 ABC transporter domain.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell inner membrane
Cell membrane
Membrane
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processriboflavin transport

Inferred from genetic interaction Ref.3. Source: UniProtKB

   Cellular_componentplasma membrane

Inferred from direct assay Ref.3. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.3. Source: UniProtKB

ATPase activity

Inferred from electronic annotation. Source: InterPro

riboflavin transporter activity

Inferred from genetic interaction Ref.3. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 266266Energy-coupling factor transporter ATP-binding protein EcfA2
PRO_0000092115

Regions

Domain3 – 238236ABC transporter
Nucleotide binding43 – 486ATP
Region220 – 26647Required for heterodimer formation

Sites

Active site1641Proton acceptor By similarity

Secondary structure

..................................................... 266
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9WY65 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: EB146157FC21EB4F

FASTA26630,233
        10         20         30         40         50         60 
MRIEVVNVSH IFHRGTPLEK KALENVSLVI NEGECLLVAG NTGSGKSTLL QIVAGLIEPT 

        70         80         90        100        110        120 
SGDVLYDGER KKGYEIRRNI GIAFQYPEDQ FFAERVFDEV AFAVKNFYPD RDPVPLVKKA 

       130        140        150        160        170        180 
MEFVGLDFDS FKDRVPFFLS GGEKRRVAIA SVIVHEPDIL ILDEPLVGLD REGKTDLLRI 

       190        200        210        220        230        240 
VEKWKTLGKT VILISHDIET VINHVDRVVV LEKGKKVFDG TRMEFLEKYD PRFFTSKMLV 

       250        260 
MRRLVLKGED PFSMSDDELL ERVCNS 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Purification, crystallization and preliminary X-ray diffraction analysis of the putative ABC transporter ATP-binding protein from Thermotoga maritima."
Ethayathulla A.S., Bessho Y., Shinkai A., Padmanabhan B., Singh T.P., Kaur P., Yokoyama S.
Acta Crystallogr. F 64:498-500(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[3]"Assembly and mechanism of a group II ECF transporter."
Karpowich N.K., Wang D.N.
Proc. Natl. Acad. Sci. U.S.A. 110:2534-2539(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A TRANSPORT COMPONENT, SUBUNIT, SUBCELLULAR LOCATION, EXPRESSION IN E.COLI, ATP-BINDING, X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-266 IN COMPLEX WITH ADP.
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD35314.1.
PIRA72401.
RefSeqNP_228037.1. NC_000853.1.
YP_007976571.1. NC_021214.1.
YP_008990804.1. NC_023151.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YZ2X-ray2.30A/B1-266[»]
4HLUX-ray2.70A/B2-266[»]
ProteinModelPortalQ9WY65.
SMRQ9WY65. Positions 1-266.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM0222.

Protein family/group databases

TCDB3.A.1.25.5. the atp-binding cassette (abc) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD35314; AAD35314; TM_0222.
GeneID15493824.
18092577.
897116.
KEGGtma:TM0222.
tmm:Tmari_0220.
PATRIC23935316. VBITheMar51294_0224.

Phylogenomic databases

eggNOGCOG1122.
KOK16787.
OMAVSHIFHR.
OrthoDBEOG6T7N3V.
ProtClustDBCLSK795008.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00005. ABC_tran. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9WY65.

Entry information

Entry nameECFA2_THEMA
AccessionPrimary (citable) accession number: Q9WY65
Entry history
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references