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Protein
Submitted name:

Amino acid ABC transporter

Gene

artP

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei14 – 141ADPCombined sources
Binding sitei14 – 141ATP analogCombined sources
Binding sitei136 – 1361ADPCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi39 – 457ATP analogCombined sources
Nucleotide bindingi40 – 456ADPCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

ATP-bindingUniRule annotation, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Submitted name:
Amino acid ABC transporterImported
Submitted name:
ArtPImported (EC:3.6.3.21Imported)
Submitted name:
Protein ArtPImported
Gene namesi
Name:artPImported
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)Imported
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OLJX-ray2.05A/B1-243[»]
2OLKX-ray2.10A/B/C/D1-243[»]
2OUKX-ray2.15A/B/C/D1-243[»]
2Q0HX-ray2.20A/B1-243[»]
3C41X-ray2.25J/K2-243[»]
3C4JX-ray2.33A/B1-243[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 239238ABC transporterInterPro annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ABC transporter domain.UniRule annotation

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR030679. ABC_ATPase_HisP-typ.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00005. ABC_tran. 1 hit.
[Graphical view]
PIRSFiPIRSF039085. ABC_ATPase_HisP. 1 hit.
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D0VWX4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQMIDVHQL KKSFGSLEVL KGINVHIREG EVVVVIGPSG SGKSTFLRCL
60 70 80 90 100
NLLEDFDEGE IIIDGINLKA KDTNLNKVRE EVGMVFQRFN LFPHMTVLNN
110 120 130 140 150
ITLAPMKVRK WPREKAEAKA MELLDKVGLK DKAHAYPDSL SGGQAQRVAI
160 170 180 190 200
ARALAMEPKI MLFDEPTSAL DPEMVGEVLS VMKQLANEGM TMVVVTHEMG
210 220 230 240
FAREVGDRVL FMDGGYIIEE GKPEDLFDRP QHERTKAFLS KVF
Length:243
Mass (Da):27,197
Last modified:December 15, 2009 - v1
Checksum:i2F21B96185D864BD
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OLJX-ray2.05A/B1-243[»]
2OLKX-ray2.10A/B/C/D1-243[»]
2OUKX-ray2.15A/B/C/D1-243[»]
2Q0HX-ray2.20A/B1-243[»]
3C41X-ray2.25J/K2-243[»]
3C4JX-ray2.33A/B1-243[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR030679. ABC_ATPase_HisP-typ.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00005. ABC_tran. 1 hit.
[Graphical view]
PIRSFiPIRSF039085. ABC_ATPase_HisP. 1 hit.
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Crystal structures of the ATP-binding cassette (ABC) protein ArtP from Geobacillus stearothermophilus reveal a stable dimer in the post hydrolysis state and an asymmetry in the dimerization region."
    Thaben P.F., Eckey V., Scheffel F., Saenger W., Schneider E., Vahedi-Faridi A.
    Submitted (JAN-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH ADP.
  2. "Crystal structures of the ATP-binding cassette (ABC) protein ArtP from Geobacillus stearothermophilus reveal a stable dimer in the post hydrolysis state and an asymmetry in the dimerization region."
    Thaben P.F., Eckey V., Scheffel F., Saenger W., Schneider E., Vahedi-Faridi A.
    Submitted (FEB-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
  3. "Crystal structures of the ATP-binding cassette (ABC) protein ArtP from Geobacillus stearothermophilus reveal a stable dimer in the post hydrolysis state and an asymmetry in the dimerization region."
    Thaben P.F., Eckey V., Scheffel F., Saenger W., Schneider E., Vahedi-Faridi A.
    Submitted (MAY-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ADP.
  4. "Crystal Structures of the ATP-binding cassette (ABC) Protein ArtP from Geobacillus stearothermophilus in complexes with nucleotides and nucleotide analogs reveal an intermediate semiclosed dimer in the post hydrolyses state and an asymmetry in the dimerisation region."
    Thaben P.F., Eckey V., Scheffel F., Allings C., Behlke J., Saenger W., Schneider E., Vahedi-Faridi A.
    Submitted (JAN-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 2-243 IN COMPLEX WITH ATP ANALOG, X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS).

Entry informationi

Entry nameiD0VWX4_GEOSE
AccessioniPrimary (citable) accession number: D0VWX4
Entry historyi
Integrated into UniProtKB/TrEMBL: December 15, 2009
Last sequence update: December 15, 2009
Last modified: April 13, 2016
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.