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Q2G506 (ATM1_NOVAD) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 67. 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:
ATM1-type heavy metal exporter
Alternative name(s):
ATP-binding cassette transporter Atm1
Short name=NaAtm1
Gene names
Name:atm1
Ordered Locus Names:Saro_2631
OrganismNovosphingobium aromaticivorans (strain DSM 12444 / F199) [Complete proteome] [HAMAP]
Taxonomic identifier279238 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeNovosphingobium

Protein attributes

Sequence length608 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates the ATP-dependent export of glutathione-conjugated substrates, such as heavy metal-glutathione conjugates. ATP hydrolysis is stimulated by glutathione binding. Protects cells against toxic heavy metal ions, such as silver and mercury ions. May also mediate the transport of glutathione-conjugated aromatic hydrocarbons, such as dinitrobenzene. Ref.2

Subunit structure

Homodimer. Ref.2

Subcellular location

Cell inner membrane; Multi-pass membrane protein Ref.2.

Sequence similarities

Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily. [View classification]

Contains 1 ABC transmembrane type-1 domain.

Contains 1 ABC transporter domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 608608ATM1-type heavy metal exporter
PRO_0000429375

Regions

Topological domain1 – 3838Cytoplasmic Ref.2
Transmembrane39 – 6022Helical
Topological domain61 – 8222Periplasmic Ref.2
Transmembrane83 – 10523Helical
Topological domain106 – 15449Cytoplasmic Ref.2
Transmembrane155 – 17824Helical
Topological domain1791Periplasmic Ref.2
Transmembrane180 – 20223Helical
Topological domain203 – 26664Cytoplasmic Ref.2
Transmembrane267 – 28519Helical
Topological domain286 – 30015Periplasmic Ref.2
Transmembrane301 – 32222Helical
Topological domain323 – 608286Cytoplasmic Ref.2
Domain39 – 327289ABC transmembrane type-1
Domain361 – 595235ABC transporter
Nucleotide binding394 – 40512ATP By similarity
Region206 – 2105Glutathione binding
Region269 – 2724Glutathione binding

Sites

Binding site3191Glutathione; via amide nitrogen
Binding site3701ATP By similarity

Experimental info

Mutagenesis1951Y → F: Strongly increases basal rate of ATP hydrolysis. Ref.2
Mutagenesis2691N → A: Increases basal rate of ATP hydrolysis and abolishes stimulation of ATP hydrolysis by glutathione. Ref.2
Mutagenesis2721Q → A: Abolishes glutathione-dependent ATP hydrolysis. Ref.2
Mutagenesis3191G → L: Abolishes glutathione-dependent ATP hydrolysis. Ref.2
Mutagenesis5231E → Q: Abolishes transporter activity. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q2G506 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: C6D669186EFC501E

FASTA60866,867
        10         20         30         40         50         60 
MPPETATNPK DARHDGWQTL KRFLPYLWPA DNAVLRRRVV GAILMVLLGK ATTLALPFAY 

        70         80         90        100        110        120 
KKAVDAMTLG GGAQPALTVA LAFVLAYALG RFSGVLFDNL RNIVFERVGQ DATRHLAENV 

       130        140        150        160        170        180 
FARLHKLSLR FHLARRTGEV TKVIERGTKS IDTMLYFLLF NIAPTVIELT AVIVIFWLNF 

       190        200        210        220        230        240 
GLGLVTATIL AVIAYVWTTR TITEWRTHLR EKMNRLDGQA LARAVDSLLN YETVKYFGAE 

       250        260        270        280        290        300 
SREEARYASA ARAYADAAVK SENSLGLLNI AQALIVNLLM AGAMAWTVYG WSQGKLTVGD 

       310        320        330        340        350        360 
LVFVNTYLTQ LFRPLDMLGM VYRTIRQGLI DMAEMFRLID THIEVADVPN APALVVNRPS 

       370        380        390        400        410        420 
VTFDNVVFGY DRDREILHGL SFEVAAGSRV AIVGPSGAGK STIARLLFRF YDPWEGRILI 

       430        440        450        460        470        480 
DGQDIAHVTQ TSLRAALGIV PQDSVLFNDT IGYNIAYGRD GASRAEVDAA AKGAAIADFI 

       490        500        510        520        530        540 
ARLPQGYDTE VGERGLKLSG GEKQRVAIAR TLVKNPPILL FDEATSALDT RTEQDILSTM 

       550        560        570        580        590        600 
RAVASHRTTI SIAHRLSTIA DSDTILVLDQ GRLAEQGSHL DLLRRDGLYA EMWARQAAES 


AEVSEAAE 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of Novosphingobium aromaticivorans DSM 12444."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N. expand/collapse author list , Fredrickson J., Balkwill D., Romine M.F., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 12444 / F199.
[2]"Structural basis for heavy metal detoxification by an Atm1-type ABC exporter."
Lee J.Y., Yang J.G., Zhitnitsky D., Lewinson O., Rees D.C.
Science 343:1133-1136(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE AND PHOSPHATE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, MUTAGENESIS OF TYR-195; ASN-269; GLN-272; GLY-319 AND GLU-523.
Strain: DSM 12444 / F199.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000248 Genomic DNA. Translation: ABD27067.1.
RefSeqYP_497901.1. NC_007794.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4MRNX-ray2.50A/B1-608[»]
4MRPX-ray2.50A/B1-608[»]
4MRRX-ray2.97A/B1-608[»]
4MRSX-ray2.35A/B1-608[»]
4MRVX-ray2.50A/B1-608[»]
ProteinModelPortalQ2G506.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279238.Saro_2631.

Protein family/group databases

TCDB3.A.1.210.11. the atp-binding cassette (abc) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD27067; ABD27067; Saro_2631.
GeneID3917064.
KEGGnar:Saro_2631.
PATRIC22788070. VBINovAro50627_2694.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG5265.
KOK06147.
OMAFLPYLWP.
OrthoDBEOG6T7N3V.

Enzyme and pathway databases

BioCycNARO279238:GHBU-2695-MONOMER.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
PROSITEPS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATM1_NOVAD
AccessionPrimary (citable) accession number: Q2G506
Entry history
Integrated into UniProtKB/Swiss-Prot: June 11, 2014
Last sequence update: March 21, 2006
Last modified: July 9, 2014
This is version 67 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